|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
2-365 |
0e+00 |
|
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: 556.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 2 ASVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPEGGTGDTgRERTKTFTYDFSYFSADSKSPSFVCQETVFKN 81
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 82 LGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKIsEKTKRNEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI-ADTTNQNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 162 L-RRKSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSE- 239
Cdd:cd01365 159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAtnplSKKKQVFVPYRDSVLTWL 318
Cdd:cd01365 239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGK----SKKKSSFIPYRDSVLTWL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2024488903 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365 315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
3-365 |
1.33e-151 |
|
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: 457.03 E-value: 1.33e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPeggtgdTGRERTKTFTYDFSYFSADSkspsfvcQETVFKNL 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSP------KNRQGEKKFTFDKVFDATAS-------QEDVFEET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKIseKTKRNEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129 68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI--DKREEGWQFSVKVSYLEIYNEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 163 rrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMPC 242
Cdd:smart00129 146 ---NPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdatnplskkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024488903 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
9-358 |
3.61e-150 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 453.18 E-value: 3.61e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 9 RVRPMNRREKDLNAKFIISMEKNKTTITNLKIpeggtgDTGRERTKTFTYDFSYfsadsksPSFVCQETVFKNLGTDVLQ 88
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVF-------DPEATQEDVYEETAKPLVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 89 SAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKTKRNEasFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225 68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSE--FSVKVSYLEIYNEKIRDLLSPSNKN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 169 TNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225 146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225 226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
|
330 340 350
....*....|....*....|....*....|..
gi 2024488903 327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225 295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
3-356 |
8.25e-138 |
|
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: 420.89 E-value: 8.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPEGGTgdtgrertKTFTYDFSyFSADSKspsfvcQETVFKNL 82
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAV-FDSTST------QEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMG-NAGDAGLIPRICEGLFSKISEKTKRNeASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGpDPEQRGIIPRALEDIFERIDKRKETK-SSFSVSASYLEIYNEKIYDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 162 LRrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMP 241
Cdd:cd00106 145 LS--PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 2024488903 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106 292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
3-358 |
1.35e-119 |
|
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: 372.95 E-value: 1.35e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITnLKIPEGGTGdtgrERTKTFTYDFSYfsadsksPSFVCQETVFKNL 82
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFDAVF-------DPNSKQLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA---GLIPRICEGLFSKISEKtkRNEASFRTEVSYLEIYNERVR 159
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARS--QNNQQFLVRVSYLEIYNEEIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 160 DLLRRKSSKtnNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKF--D 237
Cdd:cd01371 148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTW 317
Cdd:cd01371 226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024488903 318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371 294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
3-358 |
8.79e-117 |
|
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: 365.89 E-value: 8.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITnlkipeggtgdtgRERTKTFTYDFSYFSADSkspsfvcQETVFKNL 82
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVFDPSTE-------QEEVYNTC 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA------GLIPRICEGLFSKISEKTKRNEasFRTEVSYLEIYNE 156
Cdd:cd01372 62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKKDTFE--FQLKVSFLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 157 RVRDLLRRKSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKF 236
Cdd:cd01372 140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplSKKKQVFV 308
Cdd:cd01372 220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---------ESKKGAHV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024488903 309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372 291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
3-358 |
6.97e-105 |
|
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: 334.31 E-value: 6.97e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTI-------TNLKIPEGGTGDTGRERTKTFTYDFSY-FSADSkspsfvC 74
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVfdpkdeeDGFFHGGSNNRDRRKRRNKELKYVFDRvFDETS------T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 75 QETVFKNLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKIseKTKRNEASFRTEVSYLEIY 154
Cdd:cd01370 75 QEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI--ESLKDEKEFEVSMSYLEIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 155 NERVRDLLRrKSSKTnnLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQ- 233
Cdd:cd01370 153 NETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQq 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplSKKKQVFVPYRDS 313
Cdd:cd01370 230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---------PGKKNKHIPYRDS 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024488903 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370 301 KLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
3-358 |
1.79e-100 |
|
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: 321.20 E-value: 1.79e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNktTITNLKIPEGgtgdtgrertkTFTYDFSYfsaDSKSPSfvcqETVFKNL 82
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDND--TIYLVEPPST-----------SFTFDHVF---GGDSTN----REVYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKTKRNeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 163 rrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTIN-FTQAKFDSEMP 241
Cdd:cd01374 138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplsKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374 215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 2024488903 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374 285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-360 |
2.06e-100 |
|
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: 321.47 E-value: 2.06e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 9 RVRPMNRREKDLNAKFIISMEKNKTTITNLKipeggtgdtGRERTKTFTYDFSYFSADSkspsfvcQETVFKNLGTDVlQ 88
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELTS---------IGAKQKEFSFDKVFDPEAS-------QEDVFEEVSPLV-Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 89 SAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKTKRNeASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:cd01366 72 SALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKG-WSYTIKASMLEIYNETIRDLLAPGNAP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 169 TNNLRIREHPKEGP-YVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINF------TQAKfdsemp 241
Cdd:cd01366 151 QKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 242 ceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdatnplskKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01366 225 --SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQD 290
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024488903 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366 291 SLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
4-367 |
2.10e-99 |
|
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: 319.45 E-value: 2.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 4 VKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPeggtgdtgrertKTFTYDfSYFSADSKspsfvcQETVFKNLG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPP------------KTFTFD-HVADSNTN------QESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 84 TDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA--------GLIPRICEGLFSKIS-EKTKRNEA-SFRTEVSYLEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrEKEKAGEGkSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 154 YNERVRDLLRRKSSktnNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQ 233
Cdd:cd01373 144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDatnplskkKQVFVPYRDS 313
Cdd:cd01373 221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2024488903 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373 293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
1-358 |
1.17e-97 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 313.88 E-value: 1.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1 MASVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNlkipeggtgdtGRERTKTFTYDfSYFSADSKspsfvcQETVFK 80
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIA-----------TSETGKTFSFD-RVFDPNTT------QEDVYN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 81 NLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA---GLIPRICEGLFSKISEKTKrnEASFRTEVSYLEIYNER 157
Cdd:cd01369 63 FAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDE--NLEFHVKVSYFEIYMEK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 158 VRDLLrrKSSKTNnLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAkfD 237
Cdd:cd01369 141 IRDLL--DVSKTN-LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--N 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 238 SEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTW 317
Cdd:cd01369 216 VETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLTR 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024488903 318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369 285 ILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
1-367 |
1.07e-90 |
|
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: 296.16 E-value: 1.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1 MASVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITnlkipEGGTGDTGRERTKTFTYDFSyFSADSKspsfvcQETVFK 80
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS-----VRTGGLADKSSTKTYTFDMV-FGPEAK------QIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 81 NLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAG-----------DAGLIPRICEGLFSKISektkRNEASFRTEVS 149
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDRSpneeytweldpLAGIIPRTLHQLFEKLE----DNGTEYSVKVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 150 YLEIYNERVRDLLRRKSSKTNNLRIREHP--KEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364 145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 228 TINFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskkK 304
Cdd:cd01364 225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024488903 305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364 291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
75-441 |
1.43e-80 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 275.46 E-value: 1.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 75 QETVFKNLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKtkRNEASFRTEVSYLEIY 154
Cdd:COG5059 70 QEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDL--SMTKDFAVSISYLEIY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 155 NERVRDLLrrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTInfTQA 234
Cdd:COG5059 148 NEKIYDLL---SPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplsKKKQVFVPYRDSV 314
Cdd:COG5059 223 SKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINEDPNVKL--------IRELRAEIARLKAL 386
Cdd:COG5059 293 LTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFR 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 387 LAQGNQIALLDSPTA--LSMEEKLQQNEARVQELTKEWTNKWNETQNILKEQTLALR 441
Cdd:COG5059 373 EQSQLSQSSLSGIFAymQSLKKETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYK 429
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
446-562 |
9.81e-80 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438784 [Multi-domain] Cd Length: 117 Bit Score: 256.40 E-value: 9.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVN 525
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2024488903 526 GIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
4-385 |
1.23e-71 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 262.18 E-value: 1.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 4 VKVAVRVRPMNRREKDlnAKFIISMEKNKTTITNlkipeggtgdtgrertKTFTYDfsyfsadSKSPSFVCQETVFKNLG 83
Cdd:PLN03188 100 VKVIVRMKPLNKGEEG--EMIVQKMSNDSLTING----------------QTFTFD-------SIADPESTQEDIFQLVG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 84 TDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNA---------GDA-GLIPRICEGLFSKISE---KTKRNEASFRTEVSY 150
Cdd:PLN03188 155 APLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsGDQqGLTPRVFERLFARINEeqiKHADRQLKYQCRCSF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 151 LEIYNERVRDLLrrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTIN 230
Cdd:PLN03188 235 LEIYNEQITDLL---DPSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 231 FtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAtnpls 301
Cdd:PLN03188 312 V-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG----- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 302 kkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DPNV--KLIRE 375
Cdd:PLN03188 380 --KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQ 457
|
410
....*....|
gi 2024488903 376 LRAEIARLKA 385
Cdd:PLN03188 458 LRDELQRVKA 467
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
3-356 |
1.42e-69 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 236.71 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREKDlnakfIISMEKNKTTITNLKIPEGGTGDTGRERTKtFTYDFSYFSADSKspsfvcQETVFKNL 82
Cdd:cd01375 1 KVQAFVRVRPTDDFAHE-----MIKYGEDGKSISIHLKKDLRRGVVNNQQED-WSFKFDGVLHNAS------QELVYETV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMG---NAGDAGLIPRICEGLFSKISEktkRNEASFRTEVSYLEIYNERVR 159
Cdd:cd01375 69 AKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE---RPTKAYTVHVSYLEIYNEQLY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 160 DLLR---RKSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKF 236
Cdd:cd01375 146 DLLStlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLT 316
Cdd:cd01375 226 TLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKLT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2024488903 317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375 295 HVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
4-356 |
7.62e-69 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 234.50 E-value: 7.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 4 VKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLkipeggtgdtgrERTK----------TFTYDFSyFSADSKSpsfv 73
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYV-FDESSSN---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 74 cqETVFKNLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEG----LFSKISEKTKRNEasFRTEVS 149
Cdd:cd01367 65 --ETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 150 YLEIYNERVRDLLRRKSSktnnLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367 141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 230 NFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdatnplskKKQVFV 308
Cdd:cd01367 217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2024488903 309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367 280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
4-356 |
4.84e-68 |
|
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: 232.67 E-value: 4.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 4 VKVAVRVRPMNRREKDLNAKFIISMEkNKTTITnLKIPEGgtgDTGRERTKTFTYDFSYFSADSKSPSFVCQETVFKNLG 83
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVI-NSTTVV-LHPPKG---SAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 84 TDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEktkrneasFRTEVSYLEIYNERVRDLLR 163
Cdd:cd01368 78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG--------YSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 164 RKSS----KTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSE 239
Cdd:cd01368 150 PSPSsptkKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatNPLSKKKQVfVPYRDS 313
Cdd:cd01368 230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024488903 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368 303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
4-356 |
2.38e-67 |
|
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: 229.70 E-value: 2.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 4 VKVAVRVRPMNRREKDLNAKFIIS-MEKNKTTITNlkipeggtgdtGRERTKTFTYDFSYFSADSKSpsfvcQETVFKNL 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSgIDSCSVELAD-----------PRNHGETLKYQFDAFYGEEST-----QEDIYARE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSkISEKTKRneaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376 66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQ-MTRKEAW---ALSFTMSYLEIYQEKILDLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 163 rrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMPC 242
Cdd:cd01376 142 ---EPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdatnplsKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376 219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 2024488903 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376 286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| FHA_KIF16 |
cd22708 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ... |
446-554 |
7.89e-65 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438760 [Multi-domain] Cd Length: 109 Bit Score: 214.44 E-value: 7.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVN 525
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 2024488903 526 GIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22708 81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
|
|
| FHA_KIF16A_STARD9 |
cd22731 |
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ... |
446-564 |
1.44e-49 |
|
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 171.11 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVN 525
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024488903 526 GIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22731 81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
|
|
| FHA_PHLB1 |
cd22713 |
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ... |
438-561 |
4.88e-34 |
|
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438765 Cd Length: 120 Bit Score: 126.67 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTeqdIVLHGLDLESEHCIFENLNGTVNLIPL 517
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024488903 518 nGAQCSVNGIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713 78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
|
|
| FHA_KIF1 |
cd22705 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
453-553 |
2.75e-31 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438757 [Multi-domain] Cd Length: 101 Bit Score: 118.10 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVNGIQITEA 532
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 2024488903 533 THLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705 81 TRLKTGSRVILGKNHVFRFNH 101
|
|
| FHA_KIF14 |
cd22707 |
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ... |
450-554 |
1.58e-26 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438759 [Multi-domain] Cd Length: 108 Bit Score: 105.04 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVNGIQI 529
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 2024488903 530 TEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707 84 SEPTVLHHGDRVILGGDHYFRFNHP 108
|
|
| FHA_KIF1A |
cd22726 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
454-562 |
1.73e-26 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438778 [Multi-domain] Cd Length: 115 Bit Score: 105.01 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGT-----VNLIPLNGAQCSVNGIQ 528
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 2024488903 529 ITEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22726 82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
|
|
| FHA_KIF1B |
cd22727 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ... |
454-556 |
5.86e-24 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438779 [Multi-domain] Cd Length: 110 Bit Score: 97.80 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIF---ENLNG--TVNLIPLNGAQCSVNGIQ 528
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrseRNNNGevIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 2024488903 529 ITEATHLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727 83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
75-288 |
6.44e-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: 96.65 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 75 QETVFKNLGtDVLQSAFEGYN-ACVFAYGQTGSGKSYTMMgnagdaGLIPRICEGLFSKIseKTKRNEASFRTEVSYLEI 153
Cdd:cd01363 32 QPHVFAIAD-PAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGI--NKGETEGWVYLTEITVTL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 154 YNErvrdllrrkssktnnlrirehpkegpyvedlskhlvqnygdIEELMDAGNINRtTAATGMNDVSSRSHAIFTInftq 233
Cdd:cd01363 103 EDQ-----------------------------------------ILQANPILEAFG-NAKTTRNENSSRFGKFIEI---- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 234 akfdsempcetvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363 137 ----------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
454-554 |
1.47e-22 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438761 [Multi-domain] Cd Length: 102 Bit Score: 93.43 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLN-GAQCSVNGIQITEA 532
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 2024488903 533 THLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709 81 TELHHLDRVILGSNHLYVFVGP 102
|
|
| FHA_KIF13 |
cd22706 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ... |
471-554 |
3.64e-21 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438758 [Multi-domain] Cd Length: 101 Bit Score: 89.28 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 471 YHLKEgQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVNGIQITEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 2024488903 551 FNHP 554
Cdd:cd22706 98 LNCP 101
|
|
| FHA_KIF1C |
cd22728 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
454-553 |
1.66e-19 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 84.54 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAmteqDIVLHGLDLESEHCIFE---NLNG--TVNLIPLNGAQCSVNGIQ 528
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRsipNPSGevVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 2024488903 529 ITEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
3-162 |
8.10e-17 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 78.42 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 3 SVKVAVRVRPMNRREkdlnakFIISMEKNKTTITnlkipeggtgdTGRERTKTFTYDfSYFSADSKSpSFVCQEtvFKNL 82
Cdd:pfam16796 21 NIRVFARVRPELLSE------AQIDYPDETSSDG-----------KIGSKNKSFSFD-RVFPPESEQ-EDVFQE--ISQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 83 gtdvLQSAFEGYNACVFAYGQTGSGksytmmgnaGDAGLIPRICEGLFSKISEKTKrnEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796 80 ----VQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-1088 |
1.55e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEkLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLL 684
Cdd:COG1196 279 LELELEEAQAEEYE-LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 685 AEKEKfeeeRLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKmQIFRELEKLKKEKDEQYIKLESEKKRIEE 764
Cdd:COG1196 358 AELAE----AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 765 QEREQVMLVAHLEEQLREKQVmIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQL 844
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 845 EQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLqSKVRQLEYLKN 924
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL-DKIRARAALAA 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 925 NHLPALLEEKQRATEVLDRGLLGLDNTL--YQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFT---------------- 986
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLgdTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEggsaggsltggsrrel 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 987 ANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQ----AGLQAS 1062
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEElleeEELLEE 750
|
490 500
....*....|....*....|....*.
gi 2024488903 1063 LEAEQKALEQDRERLDQEIQQLKQKI 1088
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
608-1090 |
2.36e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhiESRLKDLLAEK 687
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-----LEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 688 EKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELnHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 767
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 768 EQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQhsfiefkkKQLEQL 847
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE--------EEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 848 TILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVF----------------------KAEEFDMV 905
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllaglrglagavavligveAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 906 KLTEYRLQSKV--------RQLEYLKNNHL------------PALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQ 965
Cdd:COG1196 542 AALAAALQNIVveddevaaAAIEYLKAAKAgratflpldkirARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 966 LAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQK 1045
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2024488903 1046 LATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1090
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
453-554 |
2.28e-14 |
|
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438763 [Multi-domain] Cd Length: 106 Bit Score: 70.04 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNG-AQCSV 524
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 2024488903 525 NGIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
456-564 |
2.42e-12 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438781 [Multi-domain] Cd Length: 109 Bit Score: 64.52 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 456 LIGIDDDLLSTGIILYHLKeGQTYVGredAMTEQDIVLHGLDLESEHCIFE-NLNGTVNLIPLNGAQCSVNGIQITEATH 534
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 2024488903 535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
364-476 |
3.23e-12 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 66.40 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 364 INEDPNVKLIRELRAEIARLKALL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 2024488903 463 LLSTGIILYHLKEG 476
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
605-1106 |
1.57e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKLESKRKQIE---EMEEKQRSD----KAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHiE 677
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEakkKAEEAKKADeakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE-A 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 678 SRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKmqifrELEKLKKEKDEQYIKLES 757
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-----KADEAKKKAEEKKKADEA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 758 EKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGD-VQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSF 836
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 837 IEFKKKQLEQLTILE--KDLVQQMNHLEKDIAHEKETPEYLRLAEEEHV--NLKKDDENFGDAVFKAEEFDMVKLTEYRL 912
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEeaKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 913 QSKVRQLE-YLKNNHLPALLEEKQRATEVldrgllgldNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVAR 991
Cdd:PTZ00121 1597 VMKLYEEEkKMKAEEAKKAEEAKIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 992 QEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIE--EQKQKLATLNNSCSEQAGLQAslEAEQKA 1069
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEA--EEDKKK 1745
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2024488903 1070 LEQDR--ERLDQEIQQL-KQKIYESDGGQKGNHGMLEEKL 1106
Cdd:PTZ00121 1746 AEEAKkdEEEKKKIAHLkKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
611-886 |
7.60e-11 |
|
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: 66.69 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEME-------EKQRSDKAELVRMQQEVEsqrKETEIVQLQIRKQE-ESLKRRSVHIE-SRLK 681
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAMERE---RELERIRQEERKRElERIRQEEIAMEiSRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 682 DLlaEKEKFEEERLREQQEIELQ---KKKQQEEIFARVKEELQRLQELNHKEKAEKMQifRELEKLKKEKDEqyiklESE 758
Cdd:pfam17380 379 EL--ERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ--REVRRLEEERAR-----EME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 759 KKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKR-----DLEDIRESLLKVKEARSEGEENCEELEKAQ 833
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERKRKLLEKEMEERQKAI 529
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2024488903 834 HSFIEFKKKQLEQLTilekdlvqqmnhlEKDIAHEKETPEYLRLAEEEHVNLK 886
Cdd:pfam17380 530 YEEERRREAEEERRK-------------QQEMEERRRIQEQMRKATEERSRLE 569
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
456-554 |
8.27e-11 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438782 [Multi-domain] Cd Length: 99 Bit Score: 59.93 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 456 LIGIDDDLLSTGIILYHLKEgQTYVGREDAmteQDIVLHGLDLESEHCIFE-NLNGTVNLIPLNGAQCSVNGIQITEATH 534
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 2024488903 535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-863 |
3.32e-10 |
|
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: 64.69 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 606 RLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVEsqRKETEIVQlqIRKQEESLKRRSVHIESRLKDLLA 685
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS--RLEQQKQI--LRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 686 EKEKFEEERLREQQEIElQKKKQQEEIFARVKEELQRLQELNHKEKAekmqIFRELEKLKKEKDEQYIKLESEKKRIEEQ 765
Cdd:TIGR02168 331 KLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 766 EREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLE 845
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250
....*....|....*...
gi 2024488903 846 QLTILEKDLVQQMNHLEK 863
Cdd:TIGR02168 486 QLQARLDSLERLQENLEG 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
606-817 |
1.03e-09 |
|
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: 62.83 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 606 RLEFERQQREEL--EKLESKRKQIEEMEEKQRSDKAELVRMQQeVESQRKETEIVQLQIRKQEESLKRRSVHIEsrlkdl 683
Cdd:pfam17380 382 RLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQ-IRAEQEEARQREVRRLEEERAREMERVRLE------ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 684 laEKEKFEEERLREQQEIELQKKKQQEEifaRVKEELQRLQELNHK-----EKAEKMQIFRELEK---LKKEKDE-QYIK 754
Cdd:pfam17380 455 --EQERQQQVERLRQQEEERKRKKLELE---KEKRDRKRAEEQRRKilekeLEERKQAMIEEERKrklLEKEMEErQKAI 529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024488903 755 LESEKKRIEEQEREQVMlvaHLEEQLR-EKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKE 817
Cdd:pfam17380 530 YEEERRREAEEERRKQQ---EMEERRRiQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
605-906 |
1.22e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELE---KLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIvqlqIRKQEESLKRRSVHIESRLK 681
Cdd:TIGR02168 682 LEEKIEELEEKIAElekALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 682 DLLAEKEKFEEERLREQQEIE--LQKKKQQEEIFARVKEELQ----RLQELN------HKEKAEKMQIFRELEKLKKEKD 749
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAeaEAEIEELEAQIEQLKEELKalreALDELRaeltllNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 750 EQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLL---KRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENC 826
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 827 EELEKAQHSFIEfKKKQLEQ--LTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKA-EEFD 903
Cdd:TIGR02168 918 EELREKLAQLEL-RLEGLEVriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAiEEYE 996
|
...
gi 2024488903 904 MVK 906
Cdd:TIGR02168 997 ELK 999
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
602-948 |
3.21e-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: 61.53 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 602 PICLRLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLK 681
Cdd:pfam02463 189 IIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 682 DLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVK---------EELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQY 752
Cdd:pfam02463 269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKlerrkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 753 IKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKA 832
Cdd:pfam02463 349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 833 qhsfIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKEtpeyLRLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRL 912
Cdd:pfam02463 429 ----LEILEEEEESIELKQGKLTEEKEELEKQELKLLK----DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
330 340 350
....*....|....*....|....*....|....*.
gi 2024488903 913 QSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGL 948
Cdd:pfam02463 501 KESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
611-1082 |
3.74e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVES-----QRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLA 685
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 686 EKEKFEEERLREQqeielQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ 765
Cdd:COG4717 154 RLEELRELEEELE-----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 766 --EREQVMLVAHLEEQLREKQVMIQLLkrGDVQRVEEEKRDLEDIRESLLKVkearsegeENCEELEKAQHSFIEFKKKQ 843
Cdd:COG4717 229 leQLENELEAAALEERLKEARLLLLIA--AALLALLGLGGSLLSLILTIAGV--------LFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 844 LEQLTILEKDLVQQMNHLEKDiaheketpEYLRLAEEEHVNLKKDDENFGDAVFKAEEfdmvklteyrLQSKVRQLEYLK 923
Cdd:COG4717 299 SLGKEAEELQALPALEELEEE--------ELEELLAALGLPPDLSPEELLELLDRIEE----------LQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 924 NNHLPALLEEKQRAteVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETF-EFTANVARQEEKVRKKEKE 1002
Cdd:COG4717 361 EELQLEELEQEIAA--LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeELLEALDEEELEEELEELE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1003 ILQSREKQQREALEQAVAKLERRHSALQRrstiDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQ 1082
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEE----DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
611-772 |
6.16e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.88 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEMEEKQRS----DKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAE 686
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQqeqlERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 687 KEKFEEERLREQQEIELQKKKQQEEIfARVKEELQRLQELNHK--EKAEKMQIFRELEKL----KKEKDEQYIKLESEKK 760
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQEEA-ERAEAEKQRQKELEMQlaEEQKRLMEMAEEERLeyqrQKQEAEEKARLEAEER 497
|
170
....*....|..
gi 2024488903 761 RIEEQEREQVML 772
Cdd:pfam15709 498 RQKEEEAARLAL 509
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-944 |
6.83e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.29 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQ-QEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDL 683
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 684 LAEKEKFEEERLREQQEIELQKKKQQEE-----IFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESE 758
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVlkenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 759 KKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIE 838
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 839 FKKKQLEQLTILEKDLVQQMNhLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKA--EEFDMVKLTEYRLQSKV 916
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKE-EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdeLELKKSEDLLKETQLVK 481
|
330 340
....*....|....*....|....*...
gi 2024488903 917 RQLEYLKNNHLPALLEEKQRATEVLDRG 944
Cdd:pfam02463 482 LQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
607-920 |
7.94e-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: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 607 LEFERQQREELEK-LESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESL---KRRSVHIESRLKD 682
Cdd:TIGR02169 690 LSSLQSELRRIENrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 683 LLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQE-LNHKEKAEKMQIFRE--LEKLKKEKDEQYIKLE--- 756
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArLREIEQKLNRLTLEKeyLEKEIQELQEQRIDLKeqi 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 757 -SEKKRIEEQEREqvmlVAHLEEQLREKQVMIQLLkrgdvqrvEEEKRDLE-DIRESLLKVKEARSEGEENCEElekaqh 834
Cdd:TIGR02169 850 kSIEKEIENLNGK----KEELEEELEELEAALRDL--------ESRLGDLKkERDELEAQLRELERKIEELEAQ------ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 835 sfIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKK---DDENFGDAVFKA-EEFDMVKLTEY 910
Cdd:TIGR02169 912 --IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRveeEIRALEPVNMLAiQEYEEVLKRLD 989
|
330
....*....|
gi 2024488903 911 RLQSKVRQLE 920
Cdd:TIGR02169 990 ELKEKRAKLE 999
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
455-551 |
1.02e-07 |
|
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.
Pssm-ID: 438714 [Multi-domain] Cd Length: 92 Bit Score: 50.74 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 455 HLIGIDDDllsTGIILYHLKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENLNGTVNLIPL---NGaqCSVNGIQITE 531
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGRSP---DCDIVLDDPSVSRRHARIEVDGGGVYLEDLgstNG--TFVNGKRITP 72
|
90 100
....*....|....*....|
gi 2024488903 532 ATHLNQGAVILLGRTNmFRF 551
Cdd:cd00060 73 PVPLQDGDVIRLGDTT-FRF 91
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
605-817 |
1.10e-07 |
|
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: 56.37 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELvrmqqevesQRKETEIVQLQirKQEESLKRRSVHIESRLKDLL 684
Cdd:pfam10174 455 LKEQREREDRERLEELESLKKENKDLKEKVSALQPEL---------TEKESSLIDLK--EHASSLASSGLKKDSKLKSLE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 685 AEKEKFEEERLREQQEIelqKKKQQEEIFARVKEEL-QRLQELN-----HKEKAEKMQ--------IFRELEKLKKEKDE 750
Cdd:pfam10174 524 IAVEQKKEECSKLENQL---KKAHNAEEAVRTNPEInDRIRLLEqevarYKEESGKAQaeverllgILREVENEKNDKDK 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024488903 751 QYIKLESEKKRieeQEREQVMLVAHL-----EEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKE 817
Cdd:pfam10174 601 KIAELESLTLR---QMKEQNKKVANIkhgqqEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ 669
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-888 |
1.18e-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: 56.22 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQqreeLEKLESKRKQIEEMEE-KQRSDKAELVRMQQEVESQRKETEIVQLQIRK---QEESLKRRSVHIES----- 678
Cdd:TIGR02168 197 ELERQ----LKSLERQAEKAERYKElKAELRELELALLVLRLEELREELEELQEELKEaeeELEELTAELQELEEkleel 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 679 RLKDLLAEKEKFEEERLREQQEIELQKKKQQEEI----FARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIK 754
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 755 LESEKKRIEEQEREQVMLVAHLE------EQLREKQVMIQL---LKRGDVQRVEEEKRDLEDIRESLLkvKEARSEGEEN 825
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEeleeqlETLRSKVAQLELqiaSLNNEIERLEARLERLEDRRERLQ--QEIEELLKKL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024488903 826 CEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAhEKETPEYLRLAEEEHVNLKKD 888
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
627-920 |
1.19e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 627 IEEMEEKQRSDKAELvrmqQEVESQRKETEIVQLQIRKQEESLKRRSVHIEsRLKDLLAEKEKFeeerlreQQEIELQKK 706
Cdd:TIGR02169 165 VAEFDRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY-------EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 707 KQQEEIFARVKEELQRLQElnhkekaEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ-EREQVmlvaHLEEQLREKQV 785
Cdd:TIGR02169 233 EALERQKEAIERQLASLEE-------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQL----RVKEKIGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 786 MIQLLKRgdvqRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAqhsfIEFKKKQLEQLTILEKDLVQQMNHLEKDI 865
Cdd:TIGR02169 302 EIASLER----SIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 866 AHEKETpeyLRLAEEEHVNLKKDDENFGdavfkaEEFDMVKLTEYRLQSKVRQLE 920
Cdd:TIGR02169 374 EEVDKE---FAETRDELKDYREKLEKLK------REINELKRELDRLQEELQRLS 419
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-819 |
1.20e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 606 RLEFERQQREELEK-LESKRKQIEEMEEKQRSDKAELVRMQQEVESQ----RKETEIVQLQIRKQEESLKrrsVHIEsRL 680
Cdd:TIGR02169 231 EKEALERQKEAIERqLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELE---AEIA-SL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 681 KDLLAEKEKFEEERLREQQEIELQKKKQQEEI------FARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIK 754
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIeelereIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 755 LESEKKRIEEQEREqvmlvahLEEQLREKQVMIQLLKRGDvQRVEEEKRDLEDIRESLLKVKEAR 819
Cdd:TIGR02169 387 LKDYREKLEKLKRE-------INELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEK 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1007-1108 |
2.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1007 REKQQREALEQAVAKLERRHSALQRRSTID-----FEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEI 1081
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100
....*....|....*....|....*..
gi 2024488903 1082 QQLKQKIYESDGGQKGNhgmLEEKLSH 1108
Cdd:COG4913 326 DELEAQIRGNGGDRLEQ---LEREIER 349
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-880 |
2.95e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 606 RLEFERQQREELEKLESKRKQIEEMEEKQRsdKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLA 685
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEGYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 686 EKEKfeeerLREQQEIELQKK--------KQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLES 757
Cdd:TIGR02169 280 KIKD-----LGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 758 EKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgDVQRVEEEKRDLEDIRESLLKVKEaRSEGEENCEELEKAQHSFI 837
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-YREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGI 432
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2024488903 838 EFKKKQLE-QLTILEKDLVQQMNHLEKDIAH-EKETPEYLRLAEE 880
Cdd:TIGR02169 433 EAKINELEeEKEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEE 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
612-820 |
3.01e-07 |
|
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: 54.00 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 612 QQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhIESRLKDLLAEKEKFE 691
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 692 EERLREQQEIE-----LQKKKQQEEI------------------FARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEK 748
Cdd:COG4942 97 AELEAQKEELAellraLYRLGRQPPLalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024488903 749 DEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgdvqrveeEKRDLEDIRESLLKVKEARS 820
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLEAEAAAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
607-881 |
3.78e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 607 LEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEivqlQIRKQEESLKRRSVHIESrLKDLLAE 686
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP----ELREELEKLEKEVKELEE-LKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 687 KEKFEEERLREQQEIElQKKKQQEEIFARVKEELQRLQElnhkekaekmqIFRELEKLKKEKDEqYIKLESEKKRIEEQE 766
Cdd:PRK03918 243 LEKELESLEGSKRKLE-EKIRELEERIEELKKEIEELEE-----------KVKELKELKEKAEE-YIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 767 REQVMLVAHLEEQLREKQVMIQLLKRGD------VQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFK 840
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEerleelKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2024488903 841 KKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEE 881
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
611-1092 |
3.78e-07 |
|
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: 54.59 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRK--------------QIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHI 676
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQslckeldilqreqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 677 ESRLKDLLAEKEKFEEERLREQQEIElqkKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKK---EKDEQYI 753
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETR---KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRrmqRGEQTYA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 754 KLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDvQRVEEEKRDLEDIRESLLKVKEARSegeenceelekaq 833
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD-NRSKEDIPNLQNITVRLQDLTEKLS------------- 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 834 hsfiEFKKKQLEQLTILEKDLVQQMNHLEKdIAHEKETPEYLRLA----EEEHVNLKKDDENFGDA---VFKAEEFDMVK 906
Cdd:TIGR00618 605 ----EAEDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELALKltalHALQLTLTQERVREHALsirVLPKELLASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 907 LTEYRLQSKVRQLEYLKN--NHLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQ----YRASTNQLQQLQ 980
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEmlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQslkeLMHQARTVLKAR 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 981 ETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEI-----EEQKQKLATLNNSCSE 1055
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIlnlqcETLVQEEEQFLSRLEE 839
|
490 500 510
....*....|....*....|....*....|....*..
gi 2024488903 1056 QAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYESD 1092
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-1016 |
4.09e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 610 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 689
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 690 FEEERLREQQEIE--LQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 767
Cdd:COG1196 419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 768 EQVMLVAHLEEQLREKQVMIQLLKRGDVQRVeeekRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQL 847
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVL----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 848 TILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEH---------------VNLKKDDENFGDAVFKAEEFDMVKLTEYR- 911
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadaryyvlgdtllgRTLVAARLEAALRRAVTLAGRLREVTLEGe 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 912 ----LQSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTA 987
Cdd:COG1196 655 ggsaGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2024488903 988 NVARQEEKVRKKEKEILQSRE-----------------KQQREALE 1016
Cdd:COG1196 735 EELLEELLEEEELLEEEALEElpeppdleelerelerlEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
609-940 |
9.37e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 609 FERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEV----ESQRKETEIVQLQIRKQEESlkrRSVHIESRLKDll 684
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKRVEIARKAEDA---RKAEEARKAED-- 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 685 AEKEKFEEERLREQQEIELQKKKQQEEI-FARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEqyiklesekKRIE 763
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE---------AKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 764 EQEREQvmlvahlEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIR--ESLLKVKEARSEGEENCEELEKAQHSfiefKK 841
Cdd:PTZ00121 1246 EEERNN-------EEIRKFEEARMAHFARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAE----EA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 842 KQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQS-KVRQLE 920
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeEKKKAD 1394
|
330 340
....*....|....*....|
gi 2024488903 921 YLKNNhlpaLLEEKQRATEV 940
Cdd:PTZ00121 1395 EAKKK----AEEDKKKADEL 1410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
610-785 |
1.11e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 610 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRR--------------SVH 675
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsylDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 676 IESR-LKDLLAEKEKFEEERLREQQEIELQKKKQQ--EEIFARVKEELQRLQELnhKEKAEKMQifRELEKLKKEKDEQY 752
Cdd:COG3883 109 LGSEsFSDFLDRLSALSKIADADADLLEELKADKAelEAKKAELEAKLAELEAL--KAELEAAK--AELEAQQAEQEALL 184
|
170 180 190
....*....|....*....|....*....|...
gi 2024488903 753 IKLESEKKRIEEQEREQVMLVAHLEEQLREKQV 785
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-992 |
1.48e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 651 QRKETEivqLQIRKQEESLKRrsvhiesrLKDLLAEKEKFEEErlreqqeieLQKKKQQEEIFARVKEEL---------Q 721
Cdd:TIGR02168 173 RRKETE---RKLERTRENLDR--------LEDILNELERQLKS---------LERQAEKAERYKELKAELrelelallvL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 722 RLQELNHK------EKAEKMQIFRELEKLKKEKDEQYIKLESEK---------------------KRIEEQEREQVMLVA 774
Cdd:TIGR02168 233 RLEELREEleelqeELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelqkelyalaneiSRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 775 HLEEQLREKQVMIQLLKRgDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDL 854
Cdd:TIGR02168 313 NLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 855 VQQMNHLEKDIAHEKETPEYLrlaEEEHVNLKKDDENFGDavfkaeefdmvKLTEYRLQSKVRQLEYLKnnhlpALLEEK 934
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERL---EDRRERLQQEIEELLK-----------KLEEAELKELQAELEELE-----EELEEL 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024488903 935 QRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQ 992
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
611-945 |
1.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEM---EEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSvHIESRLKDLLAEK 687
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 688 EKFEEerlreqqeiELQKKKQQEEIFARVKEELQRLQELNHKEKAEkmqifrELEKLKKEKDEqyikLESEKKRIEEQER 767
Cdd:PRK03918 348 KELEK---------RLEELEERHELYEEAKAKKEELERLKKRLTGL------TPEKLEKELEE----LEKAKEEIEEEIS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 768 EQVMLVAHLEEQLREKQVMIQLLKRGDVQ-----RVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKK 842
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 843 QLEQLTIL-EKDLVQQMNHLEKDIAH------EKETPEYlRLAEEEHVNLKKDDENFGDAVFKAEEFDMvKLTEyrLQSK 915
Cdd:PRK03918 489 LKKESELIkLKELAEQLKELEEKLKKynleelEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKK-KLAE--LEKK 564
|
330 340 350
....*....|....*....|....*....|
gi 2024488903 916 VRQLEYLKNNHLPALLEEKQRATEVLDRGL 945
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERL 594
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-892 |
1.54e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.67 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEivqLQIRKQEESLKRRSVHIESRLKDLL 684
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA---EEREKTEKLKVEEEKEEKLKAQEEE 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 685 AEKEKFEEERLREQQEIELQKKKQQEEIfaRVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEE 764
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKI--KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELE 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 765 QEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRvEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQhSFIEFKKKQL 844
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKELEEESQKLNLLE-EKENEIEERIKEEAEILLKYEEEPEELLLEEADEK-EKEENNKEEE 958
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2024488903 845 EQLTILEKDLVQQ---MNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENF 892
Cdd:pfam02463 959 EERNKRLLLAKEElgkVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-939 |
1.55e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 702 ELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEqereqvmlvahLEEQLR 781
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 782 EKQVMIQLLkRGDVQRVEEEKRDLED-IRESLLKVKEARSEGEENCEELEKAQH--SFIEFKKKQLEQLTILEK---DLV 855
Cdd:PRK03918 242 ELEKELESL-EGSKRKLEEKIRELEErIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKrlsRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 856 QQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDavfKAEEFDMVKLTEYRLQSKVRQLEYLKNNHLPALLEEKQ 935
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE---RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
....
gi 2024488903 936 RATE 939
Cdd:PRK03918 398 KAKE 401
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
451-554 |
1.81e-06 |
|
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438764 [Multi-domain] Cd Length: 120 Bit Score: 48.07 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDAMTEQ-DIVLHGLDLESEHCIFEN---------------LN 509
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWIRRkpeplsddedsdkesAD 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024488903 510 GTVNLIPLNGAQCSVNGIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712 76 YRVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
610-1088 |
2.21e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 610 ERQQREELEKLESKRKQIEEMEEKQrsdkAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 689
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 690 FEEERLREQQEIELQKKKQQ-EEIFARVKEELQRLQELnhKEKAEKMQifRELEKLKKEKDEqyikLESEKKRIEEQERE 768
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREiEKRLSRLEEEINGIEER--IKELEEKE--ERLEELKKKLKE----LEKRLEELEERHEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 769 QVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAqhsFIEFKK------- 841
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA---IEELKKakgkcpv 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 842 -------------------------KQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEE--------EHVNLKKD 888
Cdd:PRK03918 441 cgrelteehrkelleeytaelkrieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklKKYNLEEL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 889 DENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKNNhLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQ 968
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 969 Y-------RASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREAL----EQAVAKLERRHSALQRrstidf 1037
Cdd:PRK03918 600 FyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkysEEEYEELREEYLELSR------ 673
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 1038 EIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLD------QEIQQLKQKI 1088
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklekalERVEELREKV 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1092 |
3.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 844 LEQLTILEKDLVQQMNHLEKdiaHEKETPEYLRL-AEEEHVNLkkdDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYL 922
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLER---QAEKAERYKELkAELRELEL---ALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 923 KNNhLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKE 1002
Cdd:TIGR02168 262 LQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1003 ILQSREKQQREALEQAVAKLERRHSALQ----RRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLD 1078
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250
....*....|....
gi 2024488903 1079 QEIQQLKQKIYESD 1092
Cdd:TIGR02168 421 QEIEELLKKLEEAE 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-1087 |
8.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 702 ELQKKKQQEEIFARV------KEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEE---QEREQVML 772
Cdd:COG1196 217 ELKEELKELEAELLLlklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 773 VAHLEEQLREKQVMIQLLKrgdvQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSfiefKKKQLEQLTILEK 852
Cdd:COG1196 297 LARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE----AEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 853 DLVQQMNHLEKDIAHEKEtpEYLRLAEEEHVNLKKDDEnfgdavfkaeefdmvklTEYRLQSKVRQLEylknnhlpALLE 932
Cdd:COG1196 369 EAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEE-----------------LEEAEEALLERLE--------RLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 933 EKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQR 1012
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 1013 EALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLAtlnnscsEQAGLQASLEAEQKALEQDRERLDQEIQQLKQK 1087
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-------EAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
608-819 |
1.12e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMqqEVESQRKETEivqLQIRKQEESLKRRSvhiesrlkdllAEK 687
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLERAE-----------KMR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 688 EKFEEERLREQQEIELQKKKQQEEIFARVKEEL-QRLQELNHKEKAEKMQ--IFRELEKLKKEKDEQyiklesEKKRIEE 764
Cdd:pfam15709 376 EELELEQQRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRKKQQE------EAERAEA 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 765 QEREQvmlvAHLEEQLREKQVmiQLLKRGDVQRVEEEKRDLEDIRESLLKVKEAR 819
Cdd:pfam15709 450 EKQRQ----KELEMQLAEEQK--RLMEMAEEERLEYQRQKQEAEEKARLEAEERR 498
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
471-551 |
1.37e-05 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 44.95 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 471 YHLKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENLNGTVNLIPL---NGAQcsVNGIQITEATHLNQGAVILLGRTn 547
Cdd:COG1716 16 FPLDGGPLTIGRAP---DNDIVLDDPTVSRRHARIRRDGGGWVLEDLgstNGTF--VNGQRVTEPAPLRDGDVIRLGKT- 89
|
....
gi 2024488903 548 MFRF 551
Cdd:COG1716 90 ELRF 93
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
723-1087 |
1.77e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 723 LQELNHKEKAEKMqifrELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEK 802
Cdd:pfam17380 284 VSERQQQEKFEKM----EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 803 RDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKD----LVQQMNHLEKDIAHEKET-PEYLRL 877
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEErqrkIQQQKVEMEQIRAEQEEArQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 878 AEEEhvnlkkddenfgdavfKAEEFDMVKLTEyrlQSKVRQLEYLKNNHlpallEEKQRATEVLDRgllgldntlyqiek 957
Cdd:pfam17380 440 LEEE----------------RAREMERVRLEE---QERQQQVERLRQQE-----EERKRKKLELEK-------------- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 958 eiedkeEQLAQYRASTNQLQQLQETFEftanvARQEEKVRKKEKEILQSREKQQREaleQAVAKLERRHSALQRRSTiDF 1037
Cdd:pfam17380 482 ------EKRDRKRAEEQRRKILEKELE-----ERKQAMIEEERKRKLLEKEMEERQ---KAIYEEERRREAEEERRK-QQ 546
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1038 EIEEQKQKLATLNNSCSEQAGLQAsleaeqkaLEQDRERLDQEIQQLKQK 1087
Cdd:pfam17380 547 EMEERRRIQEQMRKATEERSRLEA--------MEREREMMRQIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
702-1088 |
2.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 702 ELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKD--EQYIKLESEKKRIEEQEREQVMLVAHLEEq 779
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEE- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 780 LREKQVMIQLLKrgdvQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEfkkKQLEQLTILEKDLVQQMN 859
Cdd:COG4717 158 LRELEEELEELE----AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE---EELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 860 HLEKDIAHEKETPEYLRLA------------EEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKNNHL 927
Cdd:COG4717 231 QLENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 928 PALLE-EKQRATEVLDRglLGLDNTLyqIEKEIEDKEEQLAQYRASTNQLQQLQEtfeftanvARQEEKVRKKEKEILQS 1006
Cdd:COG4717 311 PALEElEEEELEELLAA--LGLPPDL--SPEELLELLDRIEELQELLREAEELEE--------ELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1007 REKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQ--ASLEAEQKALEQDRERLDQEIQQL 1084
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAEL 458
|
....
gi 2024488903 1085 KQKI 1088
Cdd:COG4717 459 EAEL 462
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-1145 |
2.07e-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: 48.91 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 606 RLEFERQQREEL--------EKLESKRKQIEEMEEKQRSDKAELVRMQQEVES-QRKETEIVQLQIRKQEESLKRRS--V 674
Cdd:TIGR02169 344 EIEEERKRRDKLteeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKlKREINELKRELDRLQEELQRLSEelA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 675 HIESRLKDLLAEKEKFeeerlreqqeiELQKKKQQEEIfARVKEELQRLQELNHKEKAEKMQIFRELEKLKKE---KDEQ 751
Cdd:TIGR02169 424 DLNAAIAGIEAKINEL-----------EEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 752 YIKLESEKKRIEEQEREQVM--------------LVAHLEEQLREKQVMIQLLKRGDVQR--VEEEKRDLEDI------- 808
Cdd:TIGR02169 492 LAEAEAQARASEERVRGGRAveevlkasiqgvhgTVAQLGSVGERYATAIEVAAGNRLNNvvVEDDAVAKEAIellkrrk 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 809 --RESLLKVKEARSEGEENCEELEKAQHSF----IEFKKK----------------QLE---------QLTILEKDLVQQ 857
Cdd:TIGR02169 572 agRATFLPLNKMRDERRDLSILSEDGVIGFavdlVEFDPKyepafkyvfgdtlvveDIEaarrlmgkyRMVTLEGELFEK 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 858 -------MNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKAEE-----FDMVKLTEYRLQSKVRQLEYLKNN 925
Cdd:TIGR02169 652 sgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENrldelSQELSDASRKIGEIEKEIEQLEQE 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 926 H--LPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQL---------QQLQETFEFTANVARQEE 994
Cdd:TIGR02169 732 EekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIE 811
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 995 KVRKKEKEILQSREkQQREALEQAVAKLERRHSALQ-RRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQD 1073
Cdd:TIGR02169 812 ARLREIEQKLNRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1074 RERLDQEIQQLKQKIYE----------SDGGQKGNHGMLEEKLSHSNSPTNPTKPQPPSAPLVDDrinafIEQEVQRRLQ 1143
Cdd:TIGR02169 891 RDELEAQLRELERKIEEleaqiekkrkRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-----VQAELQRVEE 965
|
..
gi 2024488903 1144 NI 1145
Cdd:TIGR02169 966 EI 967
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
605-1090 |
2.50e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKLESkrkQIEEMEEKQRSDKAELVRMQQEVESQRKETEivqlqirkqeeslkrrsvHIESRLKDLL 684
Cdd:PRK02224 241 EVLEEHEERREELETLEA---EIEDLRETIAETEREREELAEEVRDLRERLE------------------ELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 685 AEKEKFEEERLREQQEIE-LQKKKqqEEIFARVKEELQRLQELNHKEKAEKMQIfRELEKLKKEKDEQYIKLESEKKRIE 763
Cdd:PRK02224 300 AEAGLDDADAEAVEARREeLEDRD--EELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 764 EQEREQVMLVAHLEEQLREkqvmiqllKRGDVQRVEEEKRDLEDIRESLLKVKEARSegeenceelekaqhsfiefkkkq 843
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEE--------LRERFGDAPVDLGNAEDFLEELREERDELR----------------------- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 844 lEQLTILEKDLVQQMNHLEK--DIAHEKETPEYLR-LAEEEHVNLKKDDEnfgDAVFK-AEEFDMVKLTEYRLQSKVRQL 919
Cdd:PRK02224 426 -EREAELEATLRTARERVEEaeALLEAGKCPECGQpVEGSPHVETIEEDR---ERVEElEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 920 EYLKN--NHLPALLEEKQRATEVLDrgllgldntlyQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVR 997
Cdd:PRK02224 502 EDLVEaeDRIERLEERREDLEELIA-----------ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 998 KKEKEILQSRekqqREALEQAVAKLERRHSALQRRSTIDFEIE---EQKQKLATLNNSCSEQ--------AGLQASLEAE 1066
Cdd:PRK02224 571 REEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIErlrEKREALAELNDERRERlaekrerkRELEAEFDEA 646
|
490 500
....*....|....*....|....*
gi 2024488903 1067 Q-KALEQDRERLDQEIQQLKQKIYE 1090
Cdd:PRK02224 647 RiEEAREDKERAEEYLEQVEEKLDE 671
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1009-1143 |
2.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1009 KQQREALEQAVAKLERRHSALQRRSTIDF----------EIEEQKQKLATLNNSCSEQAGLQASLE---AEQKALEQDRE 1075
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWdeidvasaerEIAELEAELERLDASSDDLAALEEQLEeleAELEELEEELD 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024488903 1076 RLDQEIQQLKQKIYESDGGQKGNHGMLEEKlshsnsptnPTKPQPPSAPLVDDRINAFIEQEVQRRLQ 1143
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAA---------EDLARLELRALLEERFAAALGDAVERELR 768
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-940 |
2.83e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQQRE---------------------ELEKLESKRKQIEEMEEKQRSDKAELVRMQQEV----ESQRKETEIVQLQI 662
Cdd:PTZ00121 1078 DFDFDAKEdnradeateeafgkaeeakktETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 663 RKQEESlkrRSVHIESRLKDllAEKEKFEEERLREQQEIELQKKKQQEEI-FARVKEELQRLQELNHKEKAEKMQIFREL 741
Cdd:PTZ00121 1158 RKAEDA---RKAEEARKAED--AKKAEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 742 EKLKKeKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQL----REKQVMIQLLKRGDVQRVE-----EEKRDLEDIR--- 809
Cdd:PTZ00121 1233 EEAKK-DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKADeakkaEEKKKADEAKkka 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 810 ESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEehVNLKKDD 889
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA--AKKKAEE 1389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024488903 890 ENFGDAVFKAEEFDMVKLTEYRLQSKVRQleylKNNHLPALLEEKQRATEV 940
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKKKAEEKKKADEA 1436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
705-937 |
2.96e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 705 KKKQQEEIFARVKE---ELQRLQELNHKEKAEKMQIFRElEKLKKEKDEQYIKLESEKKRIEEQEREQVMlvahleEQLR 781
Cdd:pfam17380 294 EKMEQERLRQEKEEkarEVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKREL------ERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 782 EKQVMIQLLKRGDVQRVE-EEKRDLEDIRESLlkvKEARSEGEENCEELEKAQHSFIEFKKKQLEQ-------LTILEKD 853
Cdd:pfam17380 367 QEEIAMEISRMRELERLQmERQQKNERVRQEL---EAARKVKILEEERQRKIQQQKVEMEQIRAEQeearqreVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 854 LVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKAEEFDMvKLTEYRLQSKVRQL--EYLKNNHLPALL 931
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR-KILEKELEERKQAMieEERKRKLLEKEM 522
|
....*.
gi 2024488903 932 EEKQRA 937
Cdd:pfam17380 523 EERQKA 528
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
615-1076 |
3.15e-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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 615 EELEKLESKRKQIEEMEEKQRSDKAELVRMQqevesqrKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKFEEER 694
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLT-------LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 695 LREQQEIELQK---KKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKL----------KKEKDEQYIKLESeKKR 761
Cdd:TIGR00618 243 AYLTQKREAQEeqlKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLaahikavtqiEQQAQRIHTELQS-KMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 762 IEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDV---QRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIE 838
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhirDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 839 FKKKQLEQLTIL-----EKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVF---KAEEFDMVKLTEY 910
Cdd:TIGR00618 402 LDILQREQATIDtrtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslKEREQQLQTKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 911 RLQ----SKVRQLEYLKNNHLPALLEEKQR--ATEVLDRGLLGLDNTLYQIEKEIEDKEEQL-----AQYRASTNQLQ-- 977
Cdd:TIGR00618 482 HLQetrkKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQTYAQLETSeedvyHQLTSERKQRAsl 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 978 --QLQETFEFTANVARQEEKVRKKEKEILQSREKQQREAleQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCS- 1054
Cdd:TIGR00618 562 keQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT--EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSq 639
|
490 500
....*....|....*....|..
gi 2024488903 1055 EQAGLQASLEAEQKALEQDRER 1076
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVR 661
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
555-891 |
4.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSCEN--LSAVMLYNPGLFPVKGPICLRLEFERQQREELEKLESKRKQIEEMEE 632
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 633 KQRSD--KAELVRMQQEVESQRKETEIVQLQ-----------------------IRKQEESLKrrsvhiesrlkdllaek 687
Cdd:PTZ00121 1641 KEAEEkkKAEELKKAEEENKIKAAEEAKKAEedkkkaeeakkaeedekkaaealKKEAEEAKK----------------- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 688 ekfeeerlreqqeIELQKKKQQEEIfaRVKEELQRLQELNhKEKAEKMQifRELEKLKKeKDEQYIKLESEKKRIEEQER 767
Cdd:PTZ00121 1704 -------------AEELKKKEAEEK--KKAEELKKAEEEN-KIKAEEAK--KEAEEDKK-KAEEAKKDEEEKKKIAHLKK 1764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 768 EQvmlVAHLEEQLREKQVMIQL-LKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIE----FKKK 842
Cdd:PTZ00121 1765 EE---EKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKevadSKNM 1841
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2024488903 843 QLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDEN 891
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEI 1890
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
605-949 |
4.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEK----LESKRKQIEEMEEKQRSDKAELVRMQqevESQRKETEIVQLQIRKQEESLKRRSVHIEsRL 680
Cdd:PRK03918 314 KRLSRLEEEINGIEErikeLEEKEERLEELKKKLKELEKRLEELE---ERHELYEEAKAKKEELERLKKRLTGLTPE-KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 681 KDLLAEKEKFEEERLREQQEIElQKKKQQEEIFARVKEELQRLQ-----------ELNHKEKAEKMQIF-RELEKLKKEK 748
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKIT-ARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLEEYtAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 749 deqyIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQL------LKRGDVQRVEEEKRDLEDIRESLLK-------V 815
Cdd:PRK03918 469 ----KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLkeleekLKKYNLEELEKKAEEYEKLKEKLIKlkgeiksL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 816 KEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAH-EKETPEYLRL--AEEEHVNLKKDDENF 892
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKElEPFYNEYLELkdAEKELEREEKELKKL 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 893 GDAVFKAEEfdMVKLTEYRLQSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGLD 949
Cdd:PRK03918 625 EEELDKAFE--ELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR 679
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
616-926 |
4.36e-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: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 616 ELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQE--------------ESLKRRSVHIESRLK 681
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEehylkevedlktelEKEKLKNIELTAHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 682 DLLAEKEKFEEERLReqqeIELQKKKQQEEIFARVKEELQRLQELNHKEKAEkMQIFRELEKLKKEKDEQYIKLESEKKR 761
Cdd:pfam05483 496 KLLLENKELTQEASD----MTLELKKHQEDIINCKKQEERMLKQIENLEEKE-MNLRDELESVREEFIQKGDEVKCKLDK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 762 IEEQEREQVMLVAHLEEQLREKQVMIQLLKRgdvqRVEEEKRDLEDIRESLLKVKEARSEGEEnceelekaQHSFIEFKK 841
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKK----QIENKNKNIEELHQENKALKKKGSAENK--------QLNAYEIKV 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 842 KQLE-QLTILEKDLVQQMNHLEKDIAHEKETPEYLrLAEEEHVNLKKDdenfgDAVFKAEEFDMvklteyRLQSKVRQLE 920
Cdd:pfam05483 639 NKLElELASAKQKFEEIIDNYQKEIEDKKISEEKL-LEEVEKAKAIAD-----EAVKLQKEIDK------RCQHKIAEMV 706
|
....*.
gi 2024488903 921 YLKNNH 926
Cdd:pfam05483 707 ALMEKH 712
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
662-1009 |
6.89e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 662 IRKQEESLKRRSVHIEsRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQ-ELNHKEKA--EKMQIF 738
Cdd:TIGR02168 198 LERQLKSLERQAEKAE-RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTaELQELEEKleELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 739 RELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgDVQRVEEEKRDLEDIRESLLKVKEA 818
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 819 RSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLrlaeeehvnlkkddenfgdavfk 898
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL----------------------- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 899 aeefdmvkltEYRLQSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQ----YRASTN 974
Cdd:TIGR02168 413 ----------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAER 482
|
330 340 350
....*....|....*....|....*....|....*
gi 2024488903 975 QLQQLQETFEFTANVARQEEKVRKKEKEILQSREK 1009
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
600-809 |
7.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 600 KGPICLRlEFERQQREEL-----EKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQL--QIRKQEESL--- 669
Cdd:PRK03918 437 KCPVCGR-ELTEEHRKELleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLkky 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 670 ---------------KRRSVHIESRLKDLLAEKEKfeeERLREQQEIELQKKKQQEEifARVKEELQRLQELNHKEKAEK 734
Cdd:PRK03918 516 nleelekkaeeyeklKEKLIKLKGEIKSLKKELEK---LEELKKKLAELEKKLDELE--EELAELLKELEELGFESVEEL 590
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 735 MQIFRELEKLKKEkdeqYIKLESEKKRIEEQEREQvmlvAHLEEQLREKQVMIQLLKRgdvqRVEEEKRDLEDIR 809
Cdd:PRK03918 591 EERLKELEPFYNE----YLELKDAEKELEREEKEL----KKLEEELDKAFEELAETEK----RLEELRKELEELE 653
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
608-754 |
7.34e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQQREELEKLESkrkqieEMEEKQRSDKAELVRMQQEVEsQRKEteivqlQIRKQEESLKRRSVHIESRLKDLLAEK 687
Cdd:PRK12704 57 EALLEAKEEIHKLRN------EFEKELRERRNELQKLEKRLL-QKEE------NLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024488903 688 EKFEEERLREQQEIELQKKK-------QQEEIfarvKEELqrLQELNHKEKAEKMQIFRELEKLKKEKDEQYIK 754
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQElerisglTAEEA----KEIL--LEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
615-1088 |
7.50e-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: 47.04 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 615 EELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVE----------------SQRKETEIVQLQIRKQEESLKRRSVHIES 678
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEitgltekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 679 RLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKaEKMQIFRELEKLKKEkdeqyIKLESE 758
Cdd:pfam15921 325 TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD-QLQKLLADLHKREKE-----LSLEKE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 759 K-KRIEEQEREQVMLVAHLEEQLREKQVMIQLLkrgdvqrveeekrdledirESLLKVKEARSEGEENCeelekaQHSFI 837
Cdd:pfam15921 399 QnKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-------------------EALLKAMKSECQGQMER------QMAAI 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 838 EFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVfKAEEFDMVKLTEyRLQSKVR 917
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAI-EATNAEITKLRS-RVDLKLQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 918 QLEYLKN--NHlpalLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARqeek 995
Cdd:pfam15921 532 ELQHLKNegDH----LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR---- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 996 VRKKEKEILQSREKQQREALEQAVAKLERRHSAL------QRRSTIDFEiEEQKQKLATLNNSCSEQAGLQASLEAEQKA 1069
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagseRLRAVKDIK-QERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
490
....*....|....*....
gi 2024488903 1070 LEQDRERLDQEIQQLKQKI 1088
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQL 701
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
612-1105 |
8.31e-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: 47.02 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 612 QQREELEKLESKRK----QIEEMEEKQRSDKAEL----VRMQQEVESQRKETEIVQLQIR-----------KQEESLKRR 672
Cdd:pfam05483 265 ESRDKANQLEEKTKlqdeNLKELIEKKDHLTKELedikMSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 673 SVH---------IESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIfarvkEELQRLQELNHKEKAEKMQIFRELEK 743
Cdd:pfam05483 345 AAHsfvvtefeaTTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-----EEMTKFKNNKEVELEELKKILAEDEK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 744 LKKEKdEQYIKLESEkkrIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGD---VQRVEEEKRDLEDIR----------- 809
Cdd:pfam05483 420 LLDEK-KQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEehyLKEVEDLKTELEKEKlknieltahcd 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 810 ESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQ---LEQLTILEKDLVQQMNHLEKdiahekETPEYLRLAEEEHVNLK 886
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEermLKQIENLEEKEMNLRDELES------VREEFIQKGDEVKCKLD 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 887 KDDENfgdavfkaeefdmVKLTEYRLQSKVRQLEYLKN--NHLPALLEEKQRATEVLDRGLLGLdntlyqiEKEIEDKEE 964
Cdd:pfam05483 570 KSEEN-------------ARSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 965 QLAQYRASTNQLQ-----QLQETFEFTANVARQEEKVRKKEKEILQSREKQ----------QREALEQAVAKLERRHSAL 1029
Cdd:pfam05483 630 QLNAYEIKVNKLElelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALM 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 1030 QR-RSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYESDGGQKGNHGMLEEK 1105
Cdd:pfam05483 710 EKhKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
796-1090 |
8.33e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 796 QRVEEEKRDLEDIRESLLKV---------------------KEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDL 854
Cdd:COG1196 172 ERKEEAERKLEATEENLERLedilgelerqleplerqaekaERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 855 VQQMNHLEKDIAHEKETPEYLRLAEEEhvnlkkddenfgdavfKAEEFDMVKLTEYRLQSKVRQLEYLKNnhlpALLEEK 934
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEE----------------LELELEEAQAEEYELLAELARLEQDIA----RLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 935 QRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREA 1014
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024488903 1015 LEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1090
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
611-820 |
1.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKF 690
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 691 EEERLREQQEIELQKKKQQeEIFARVKEELQRLQELNHKekaekmqifreLEKLKKEKDEqyikLESEKKRIEEqEREQV 770
Cdd:TIGR02169 888 KKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAK-----------LEALEEELSE----IEDPKGEDEE-IPEEE 950
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024488903 771 MLVAHLEEQLREKQVMIQLLkrGDV-----QRVEEEKRDLEDIRESLLKVKEARS 820
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERK 1003
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
611-865 |
1.05e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEMEEKQRSdkaelVRMQQEVESQRKETEIVQ-----LQIRKQEESLKRRSVHIESRLKDLLA 685
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTIKREKK-----LRETEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVELA 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 686 EKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQifrELEKLKKEKD------------EQYI 753
Cdd:COG5022 881 ERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIA---RLKKLLNNIDleegpsieyvklPELN 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 754 KLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgDVQRVEEEKRDLEDIRE--SLLKVKEARSEGEENCEELEK 831
Cdd:COG5022 958 KLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQEstKQLKELPVEVAELQSASKIIS 1036
|
250 260 270
....*....|....*....|....*....|....
gi 2024488903 832 AQHSFiefkKKQLEQLTILEKDLVQQMNHLEKDI 865
Cdd:COG5022 1037 SESTE----LSILKPLQKLKGLLLLENNQLQARY 1066
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1004-1124 |
1.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1004 LQSREKQQREALEQAVAKLERRHSALQR-RSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQ 1082
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAkLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2024488903 1083 QLKQKIYESDGGQKGNHGMLEEKLSHSNSPTNPTKPQPPSAP 1124
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
613-819 |
1.72e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.41 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 613 QREELEKLESKRKQIEEmEEKQRSDKAELVRMQQEVESQRKEteiVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKFEE 692
Cdd:pfam15558 33 AWEELRRRDQKRQETLE-RERRLLLQQSQEQWQAEKEQRKAR---LGREERRRADRREKQVIEKESRWREQAEDQENQRQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 693 ERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMl 772
Cdd:pfam15558 109 EKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLV- 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024488903 773 vahlEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEAR 819
Cdd:pfam15558 188 ----DCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQK 230
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
612-1114 |
1.73e-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: 45.97 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 612 QQREELEKLESKRKQIEEMEEKQRSDKAELvrmqqevesQRKETEIVQLQIR-----KQEESLKRrsvHIESrLKDLLAE 686
Cdd:pfam10174 269 DREEEIKQMEVYKSHSKFMKNKIDQLKQEL---------SKKESELLALQTKletltNQNSDCKQ---HIEV-LKESLTA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 687 KEKFEEERLREQQEIELqKKKQQEEIFARVKEELQRLQElnhkekaEKMQIFRELEKLKKEKDEQYIKLESEKKRIEeqe 766
Cdd:pfam10174 336 KEQRAAILQTEVDALRL-RLEEKESFLNKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIE--- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 767 reqvmlvaHLEEQLREKQVMIQLLKRgdvqRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQ 846
Cdd:pfam10174 405 --------NLQEQLRDKDKQLAGLKE----RVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 847 LTILEKDLVQQMNHLEKDIAhEKETPeYLRLAE-------------------EEHVNLKKDDENFGDAVF-KAEEFDMVK 906
Cdd:pfam10174 473 LKKENKDLKEKVSALQPELT-EKESS-LIDLKEhasslassglkkdsklkslEIAVEQKKEECSKLENQLkKAHNAEEAV 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 907 LTEYRLQSKVRQLEylknNHLPALLEEKQRATEVLDRgLLGLdntLYQIEKEIEDKEEQLAQYRASTnqLQQLQETFEFT 986
Cdd:pfam10174 551 RTNPEINDRIRLLE----QEVARYKEESGKAQAEVER-LLGI---LREVENEKNDKDKKIAELESLT--LRQMKEQNKKV 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 987 ANVARQEEKVRKKEKEILQ-SREKQQREALEQAVAKLERRHSALQRRSTidfEIEEQKQKLATLNNSCSEQAGLQASLEA 1065
Cdd:pfam10174 621 ANIKHGQQEMKKKGAQLLEeARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKARLSSTQQSLAEKDGHLTNLRA 697
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2024488903 1066 EQKalEQDRERLDQEIQQLKQKIYESDggqkGNHGMLEekLSHSNSPTN 1114
Cdd:pfam10174 698 ERR--KQLEEILEMKQEALLAAISEKD----ANIALLE--LSSSKKKKT 738
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
610-882 |
2.54e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 610 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQI--RKQEESLKRRSVHIESRLKDLLAEK 687
Cdd:pfam13868 30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 688 EKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELnhKEKAEKMQIFRELeklkKEKDEQYIKLESEKKRI-EEQE 766
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE--EEREEDERILEYL----KEKAEREEEREAEREEIeEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 767 REQVMLVAHLEEQLREKQVMIQLLkrgdVQRVEEEKRDLEDIREsllkvKEARSEGEENCEELEKAQHSFIEFKKKQLEQ 846
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELR----AKLYQEEQERKERQKE-----REEAEKKARQRQELQQAREEQIELKERRLAE 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024488903 847 LTILEKDLVQQM-NHLEKDIAHEKETPEYLRLAEEEH 882
Cdd:pfam13868 255 EAEREEEEFERMlRKQAEDEEIEQEEAEKRRMKRLEH 291
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
471-555 |
2.60e-04 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 41.09 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 471 YHLKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENLNGTVNLIPLN-GAQCSVNGIQITEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87
|
....*..
gi 2024488903 549 FRFNHPK 555
Cdd:pfam16697 88 FCLVPAD 94
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
611-783 |
2.98e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhIESRLKDLLAEKEKF 690
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 691 EEERLREQQE---------IELQKKKQQ--EEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEK 759
Cdd:COG1579 79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|....
gi 2024488903 760 KRIEEQEREqvmLVAHLEEQLREK 783
Cdd:COG1579 159 EELEAEREE---LAAKIPPELLAL 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
607-1088 |
3.41e-04 |
|
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: 44.96 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 607 LEFERQQREELEKLESKRKQIEEM---EEKQRSDKAELVRMQQEVESQRKETEIVQ-----LQIRKQ-EESLKRRSVHIE 677
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQLLKQLrarIEELRAQEAVLEETQERINRARKAAPLAAhikavTQIEQQaQRIHTELQSKMR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 678 SRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFAR-------VKEELQRLQELNHKEKAEKMQIFRELEKLK----- 745
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahevatsIREISCQQHTLTQHIHTLQQQKTTLTQKLQslcke 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 746 --KEKDEQY-------------IKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGdVQRVEEEKRDLEDIRE 810
Cdd:TIGR00618 402 ldILQREQAtidtrtsafrdlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES-AQSLKEREQQLQTKEQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 811 SLLKVKEARSEGEENCEELEKAQHSFIE---FKKKQLEQLTILEKD--LVQQMNHLEKDIAHEKETPEYLRLAEEEHVNL 885
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGsciHPNPARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 886 KKDDENFGDAVFKAEEFDMVKLTEyrLQSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGL-------DNTLYQIEKE 958
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKE--DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLqpeqdlqDVRLHLQQCS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 959 IEDKEEQLAQYRASTNQLQQLQ-ETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDF 1037
Cdd:TIGR00618 639 QELALKLTALHALQLTLTQERVrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR 718
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024488903 1038 EIEEQKQKL----ATLNNSCSEQAGLQASLEAEQ----KALEQDRER----------LDQEIQQLKQKI 1088
Cdd:TIGR00618 719 EFNEIENASsslgSDLAAREDALNQSLKELMHQArtvlKARTEAHFNnneevtaalqTGAELSHLAAEI 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
758-1088 |
4.39e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 758 EKKRIEEQEREQVmlvahlEEQLREKQVMIQLlKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFI 837
Cdd:TIGR02169 170 RKKEKALEELEEV------EENIERLDLIIDE-KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 838 EF----KKKQLEQLTILEKDLVQQMNHLEKDIahEKETPEYLRLAEEEHVNLKKDDENfgdavfkaeefdmvklteyrLQ 913
Cdd:TIGR02169 243 ERqlasLEEELEKLTEEISELEKRLEEIEQLL--EELNKKIKDLGEEEQLRVKEKIGE--------------------LE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 914 SKVRQLEylknnhlpALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQE 993
Cdd:TIGR02169 301 AEIASLE--------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 994 EKVRKKEKEILQSREKQQREALEqavaKLERRHSALQR-RSTIDFEIEEQKQKLATLNNSCseqaglqASLEAEQKALEQ 1072
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLE----KLKREINELKReLDRLQEELQRLSEELADLNAAI-------AGIEAKINELEE 441
|
330
....*....|....*.
gi 2024488903 1073 DRERLDQEIQQLKQKI 1088
Cdd:TIGR02169 442 EKEDKALEIKKQEWKL 457
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
605-768 |
4.52e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKLESKRKQIEEMEEKQRSDKA-ELVRMQQEVESQRKETE-----IVQLQIRKQEESLKRrsvhies 678
Cdd:pfam15709 374 MREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQEefrrkLQELQRKKQQEEAER------- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 679 rlkdllAEKEKfeeerlREQQEIELQKKKQQEEIFARVKEElqRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESE 758
Cdd:pfam15709 447 ------AEAEK------QRQKELEMQLAEEQKRLMEMAEEE--RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
170
....*....|
gi 2024488903 759 KKRIEEQERE 768
Cdd:pfam15709 513 MKQAQEQARQ 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
609-769 |
5.74e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 609 FERQQREELEKLESKRKQI---EEMEEKQRSDKAELvRMQQEVESQRKETE----IVQLQIRKQEESLKRRSVHIESRLK 681
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRIleeAKKEAEAIKKEALL-EAKEEIHKLRNEFEkelrERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 682 DLLAEKEKFEEERLREQQEIELQKKKQQE--EIFARVKEELQRLQELNhKEKAEKMQIFRELEKLKKEKDEQYiklesek 759
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEEleELIEEQLQELERISGLT-AEEAKEILLEKVEEEARHEAAVLI------- 175
|
170
....*....|
gi 2024488903 760 KRIEEQEREQ 769
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
611-765 |
5.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQ----LQIRKQEESLKRRSVHIESRLKDLLAE 686
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSpedfLDAVRRLQYLKYLAPARREQAEELRAD 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024488903 687 KEKFEEERLREQqeielQKKKQQEEIFARVKEELQRLQelnhKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ 765
Cdd:COG4942 159 LAELAALRAELE-----AERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
452-554 |
5.80e-04 |
|
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438785 Cd Length: 113 Bit Score: 40.55 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGT-------VNLIPLNGAQCSV 524
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 2024488903 525 NGIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
708-804 |
6.77e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 42.12 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 708 QQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREqvmlvahLEEQLREKQVMI 787
Cdd:pfam06785 80 LDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLE-------SEEQLAEKQLLI 152
|
90
....*....|....*...
gi 2024488903 788 QLLKRGDV-QRVEEEKRD 804
Cdd:pfam06785 153 NEYQQTIEeQRSVLEKRQ 170
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
865-1090 |
6.77e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 865 IAHEKETP-EYLRLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQ-LEYLKNNHLpaLLEEKQRATEvld 942
Cdd:pfam17380 342 MAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKVKI--LEEERQRKIQ--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 943 rgllgldntlyqiEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEIL-QSREKQQREALEQAVAK 1021
Cdd:pfam17380 417 -------------QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024488903 1022 LERRHSALQRRSTIDFEIEEQKQKLATLNNscsEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1090
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEERKQAMIEEER---KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
615-847 |
7.42e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 615 EELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQE---------ESLKRRSVHIESRLKDLLA 685
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGgldeeeaflDRTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 686 EKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ 765
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 766 EREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDL--------EDIRESLLKVKEARSEGEENCEELEKAQHSFI 837
Cdd:pfam02029 165 EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHpevksqngEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL 244
|
250
....*....|
gi 2024488903 838 EFKKKqLEQL 847
Cdd:pfam02029 245 EAEQK-LEEL 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
605-1087 |
7.68e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 605 LRLEFERQQREELEKleskrkQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIR----KQEESLKRRSVHIESRL 680
Cdd:COG4913 281 LRLWFAQRRLELLEA------ELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 681 KDLLAEKEKFEEERLREQQEIELQkkkqqEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKK 760
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPAS-----AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 761 RIEEQ----EREQVMLVAHLEEQL--REKQVMI--QLLkrgDVQRVEEEKRD-----LEDIRESLL-------KVKEA-R 819
Cdd:COG4913 430 SLERRksniPARLLALRDALAEALglDEAELPFvgELI---EVRPEEERWRGaiervLGGFALTLLvppehyaAALRWvN 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 820 SEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQ-------MNHLEKDIAHEK-ETPEYLR----------LAEEE 881
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPhpfrawlEAELGRRFDYVCvDSPEELRrhpraitragQVKGN 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 882 HVNLKKDDENFGDAV----FKAEEfdmvklteyRLQSKVRQLEYLKNNHLPAL-----LEEKQRATEVLDRGLLGLDNT- 951
Cdd:COG4913 587 GTRHEKDDRRRIRSRyvlgFDNRA---------KLAALEAELAELEEELAEAEerleaLEAELDALQERREALQRLAEYs 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 952 -----LYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEfTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRH 1026
Cdd:COG4913 658 wdeidVASAEREIAELEAELERLDASSDDLAALEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024488903 1027 SALQRRSTID--FEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQK 1087
Cdd:COG4913 737 EAAEDLARLElrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
702-1042 |
1.38e-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: 42.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 702 ELQKKKQQEEIFARVKEELQRLQELNHKekAEKMQI-FRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQL 780
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAIAGIMKIRPE--FTKLQQeFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 781 REKQVMIQllkrgdvQRVEEEKRDLEDIREsllKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLtilekDLVQ-QMN 859
Cdd:pfam12128 293 RTLDDQWK-------EKRDELNGELSAADA---AVAKDRSELEALEDQHGAFLDADIETAAADQEQL-----PSWQsELE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 860 HLEKDI-----AHEKETPEYLRLaeeehvNLKKDDENfgdavfKAEEFDMVKLTEYRLQSKVRQLEYLKNnHLPALleeK 934
Cdd:pfam12128 358 NLEERLkaltgKHQDVTAKYNRR------RSKIKEQN------NRDIAGIKDKLAKIREARDRQLAVAED-DLQAL---E 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 935 QRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQlQETFEFTANVARQEEKVRKKEKEILQSREKQQREA 1014
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ-LENFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
330 340
....*....|....*....|....*...
gi 2024488903 1015 LEQAVAKLERRHSALQRRSTIDFEIEEQ 1042
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQ 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-1014 |
1.40e-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: 43.04 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 354 RAKNIINKPTINEDPNVKLIRELRAEIARLKALLAQGNQIALLDSPTALSMEEKLQQNEARVQELTKEWT--NKWNETQN 431
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEqlELLLSRQK 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 432 ILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHC--IFENLN 509
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvrALTELP 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 510 GTVNLIPLNGAQCSVNGIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAV 589
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 590 MlynPGLFPVKGPICLRLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESL 669
Cdd:pfam02463 655 E---EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 670 KRRSVHIESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKD 749
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 750 EQYIKLESEKKRIEEQEREQvmlvahlEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEEL 829
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIK-------EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL 884
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 830 EKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENfgdavfkaeefdmvklte 909
Cdd:pfam02463 885 KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD------------------ 946
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 910 yrlqskvrqLEYLKNNHLPALLEEKQRATEVLDrgLLGLDNtlyqiekeiedkeeqlaqyrastnqlqqLQETFEFTANV 989
Cdd:pfam02463 947 ---------EKEKEENNKEEEEERNKRLLLAKE--ELGKVN----------------------------LMAIEEFEEKE 987
|
650 660
....*....|....*....|....*
gi 2024488903 990 ARQEEKVRKKEKEILQSREKQQREA 1014
Cdd:pfam02463 988 ERYNKDELEKERLEEEKKKLIRAII 1012
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
606-812 |
1.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 606 RLEFERQQREELEKLESKRKQIEEMEEKqRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLA 685
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAA-VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 686 EKEkfeeERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLK-----KEKDEQYIKLESEKK 760
Cdd:COG1196 652 EGE----GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERelaeaEEERLEEELEEEALE 727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024488903 761 RIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESL 812
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
661-870 |
1.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 661 QIRKQEESLKRRSVHIESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEeIFARVKEELQRLQELNHKEKaekmqifrE 740
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAELAELEKEIA--------E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 741 LEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARS 820
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024488903 821 EGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKE 870
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
928-1090 |
1.63e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 928 PALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSR 1007
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1008 EKQQREALEQAVAKLER--RHSALQ-------------RRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQ 1072
Cdd:COG4942 99 LEAQKEELAELLRALYRlgRQPPLAlllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*...
gi 2024488903 1073 DRERLDQEIQQLKQKIYE 1090
Cdd:COG4942 179 LLAELEEERAALEALKAE 196
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
608-769 |
2.75e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQQREeleKLESKRKQieEMEEKQRSDKAELVRMQQEVESQR-KETEIVQLQIRKQEESlkrrsvHIESRLKDLLAE 686
Cdd:PRK09510 63 QYNRQQQQ---QKSAKRAE--EQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQ------AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 687 KEKfeeerlreqqeiELQKKKQQEEIFARVKEELQRLQELNHKEKAEKmQIFRELEKLKKEKDEQYIKLESEKKRIEEQE 766
Cdd:PRK09510 132 KQA------------EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE 198
|
...
gi 2024488903 767 REQ 769
Cdd:PRK09510 199 AKK 201
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
610-784 |
2.90e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 610 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEE--SLKRRSVHIESR------LK 681
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESkvFLDQKRGHPEVKsqngeeEV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 682 DLLAEKEKFEEERLREQQEIELQKKKQQEEifARVKEELQRLQELNHKEKAEKMQIFR-----ELEKLKKEKDEQYIKLE 756
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSQEREEEAEVFLEA--EQKLEELRRRRQEKESEEFEKLRQKQqeaelELEELKKKREERRKLLE 294
|
170 180
....*....|....*....|....*...
gi 2024488903 757 SEKKRIEEQEREQvmLVAHLEEQLREKQ 784
Cdd:pfam02029 295 EEEQRRKQEEAER--KLREEEEKRRMKE 320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
614-812 |
3.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 614 REELEKLESKRKQIEEMEEKQRsdkaELVRMQQEVESQRKETEIVQLQIRKQE-ESLKRRSVHIESRLKDLLAEKEKFEE 692
Cdd:COG4913 241 HEALEDAREQIELLEPIRELAE----RYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 693 ERLREQQEIElQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREQVML 772
Cdd:COG4913 317 RLDALREELD-ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024488903 773 VAHLEEQLREKQVMIqllkRGDVQRVEEEKRDLEDIRESL 812
Cdd:COG4913 396 LEEELEALEEALAEA----EAALRDLRRELRELEAEIASL 431
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
611-816 |
3.27e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREEL-EKLESKRKQIEEMEEKQ---RSDKAELVRMQQEVESQRKETEIVQLQIRKQEEsLKRRSVHIESRLKDLLAE 686
Cdd:COG1340 77 KEERDELnEKLNELREELDELRKELaelNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 687 KEKFEEERLREQQEIELqkKKQQEEIFARVKEELQRLQELnhkeKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQE 766
Cdd:COG1340 156 LEKNEKLKELRAELKEL--RKEAEEIHKKIKELAEEAQEL----HEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024488903 767 REQVMLVAHLEEqlREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVK 816
Cdd:COG1340 230 EEIIELQKELRE--LRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
608-920 |
3.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 608 EFERQ------QREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESL--------KRRS 673
Cdd:pfam15921 445 QMERQmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 674 vHIESRLKDL--LAEKEKFEEERLREQQEIELQKKkQQEEIFARVKEELQRLQEL--NHKEKAEKMQIFR---------- 739
Cdd:pfam15921 525 -RVDLKLQELqhLKNEGDHLRNVQTECEALKLQMA-EKDKVIEILRQQIENMTQLvgQHGRTAGAMQVEKaqlekeindr 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 740 --ELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLRE----KQVMIQLLK-----RGDVQRVEEekrDLEDI 808
Cdd:pfam15921 603 rlELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNELNSLSE---DYEVL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 809 RESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMNHLEKDIAHEKETPEYL----RLAEEEHVN 884
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALqskiQFLEEAMTN 759
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024488903 885 LKKDDENFGDAVFK---------------AEEFDMVKLTEYRLQSKVRQLE 920
Cdd:pfam15921 760 ANKEKHFLKEEKNKlsqelstvateknkmAGELEVLRSQERRLKEKVANME 810
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
611-735 |
3.39e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.67 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLEskRKQIEEMEEKQRSDKAELvrmqqEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEkf 690
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQL-----RLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQE-- 389
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024488903 691 eeerlreqqeIELQKKKQQEeifarVKEELQRlQELNHKEKAEKM 735
Cdd:pfam09731 390 ----------IELQREFLQD-----IKEKVEE-ERAGRLLKLNEL 418
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
613-1084 |
3.43e-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: 41.57 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 613 QREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRK-----ETEIVQLQIRKQEESLKRRSVHiesRLKDLLAEK 687
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREivksyENELDPLKNRLKEIEHNLSKIM---KLDNEIKAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 688 EKFEEERLREQQEIELQKkkqqEEIFARVKEELQRLQELNHKEKAEK----MQIFRELEKLKKEKDEqyikLESEKKRIE 763
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKM----EKVFQGTDEQLNDLYHNHQRTVREKerelVDCQRELEKLNKERRL----LNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 764 -EQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKK 842
Cdd:TIGR00606 347 vEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 843 QLEQLTILEKDLVQQMnHLEKDIAHEKETPEYLRLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRL-QSKVRQLEY 921
Cdd:TIGR00606 427 QADEIRDEKKGLGRTI-ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLtETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 922 LKNNHLPalleekqratevLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETfEFTANVARQEEKVRKKEK 1001
Cdd:TIGR00606 506 LQNEKAD------------LDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI-KSRHSDELTSLLGYFPNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1002 EILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEI 1081
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSS 652
|
...
gi 2024488903 1082 QQL 1084
Cdd:TIGR00606 653 KQR 655
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
610-846 |
4.25e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 610 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 689
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 690 FEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELnhkekaEKMQIFRELEKLKKEKDEQyiklesEKKRIEEQEREQ 769
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER------DELRAKLYQEEQERKERQK------EREEAEKKARQR 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 770 VMLVAHLEEQLREKQVMIQLLKRgdvQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQ 846
Cdd:pfam13868 235 QELQQAREEQIELKERRLAEEAE---REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAA 308
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
473-551 |
4.39e-03 |
|
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.
Pssm-ID: 438725 [Multi-domain] Cd Length: 95 Bit Score: 37.58 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 473 LKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENL-NGTVNLIPL---NGAQcsVNGIQITEATHLNQGAVILLGrTNM 548
Cdd:cd22673 18 LTKKSCTFGRDL---SCDIRIQLPGVSREHCRIEVDeNGKAYLENLsttNPTL--VNGKAIEKSAELKDGDVITIG-GRS 91
|
...
gi 2024488903 549 FRF 551
Cdd:cd22673 92 FRF 94
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1010-1088 |
4.57e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 1010 QQREALEQAVAKLERRHSALQR----------RSTIDFEIEEQKQKLAtlnnscSEQAGLQASLEAEQKALEQDRERLDQ 1079
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRaerllaefckRLGKNLDDEDELEQLQ------EELEARLESLSESVSEARERRMALRQ 586
|
....*....
gi 2024488903 1080 EIQQLKQKI 1088
Cdd:PRK04863 587 QLEQLQARI 595
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
719-804 |
5.57e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 40.88 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 719 ELQRLQELNHKEKAEKMQIfreLEKLKKEKDEQYIKLESEKKRIEEQEREQVMlvahlEEQLREKQVMIQLLKRGDVQRV 798
Cdd:PTZ00266 436 ERARIEKENAHRKALEMKI---LEKKRIERLEREERERLERERMERIERERLE-----RERLERERLERDRLERDRLDRL 507
|
....*.
gi 2024488903 799 EEEKRD 804
Cdd:PTZ00266 508 ERERVD 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
651-819 |
6.04e-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: 39.91 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 651 QRKETEIVQlqIRKQEESLKRRSVHIESRLKDLLAEKEKfeeerlreqqeIELQKKKQQEEIfARVKEELQRLQELNHKE 730
Cdd:COG1579 13 QELDSELDR--LEHRLKELPAELAELEDELAALEARLEA-----------AKTELEDLEKEI-KRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 731 KAEKMQIF--RELEKLKKEKDeqyiKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDI 808
Cdd:COG1579 79 EEQLGNVRnnKEYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|.
gi 2024488903 809 RESLLKVKEAR 819
Cdd:COG1579 155 EAELEELEAER 165
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
618-833 |
6.70e-03 |
|
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as found in Bacillus cereus. EntB is related to EntA, EntC, and EndD. All Ent family proteins have a signal peptide, an N-terminal SH3 domain and a C-terminal 3D (Asp-Asp-Asp) domain. EntB and EndC have a central region with a highly variable number of repeats resembling KAXEXX. The gene symbol derives from the notion that at least some members of the family function as enterotoxins, but more recent descriptions focus on roles in stress response and cell wall integrity.
Pssm-ID: 468642 [Multi-domain] Cd Length: 476 Bit Score: 40.54 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 618 EKLESKRKQIEEMeekQRSDKAELVRMQQEVeSQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKfeeerlre 697
Cdd:NF040676 149 KKADEKTKQVAKV---QKSVKAKEEAKTQKV-AKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPK-------- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 698 qqeielQKKKQQEEifARVKEElQRLQELNHKEKAEKMQifrELEKLKKEKDEQYIKLESEKKRIE------EQEREQVM 771
Cdd:NF040676 217 ------EEVKVQEE--VKPKEE-EKVQEIVKPKEEAKVQ---EEVKVKEEAKVQEIAKAKEEAKAQeiakakEEAKAQEI 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024488903 772 LVAHLEEQLREKQVMIQLLKRGDVQRVEEEkrdlEDIRESLLKVKEARSEGEENCEELEKAQ 833
Cdd:NF040676 285 AKAKEEAKAQEIAKAKEEEKAQEIAKAKEE----AKAREIAKAKEEEKAREIAKAKEEAKAR 342
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
611-764 |
6.98e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.48 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 611 RQQREELEKLESKRKQIEEME---EKQRSDKAELVRMQQEVESQRKETEivqlqiRKQEESLKRRSVhIESRLKDLLAEK 687
Cdd:pfam05672 21 RQAREQREREEQERLEKEEEErlrKEELRRRAEEERARREEEARRLEEE------RRREEEERQRKA-EEEAEEREQREQ 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 688 EKfeeerlreqqEIELQKKKQQEEIFARvkeelqrlqelnhkEKAEKMQIFRELEKLKKEKDEQyikleSEKKRIEE 764
Cdd:pfam05672 94 EE----------QERLQKQKEEAEAKAR--------------EEAERQRQEREKIMQQEEQERL-----ERKKRIEE 141
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
900-1087 |
7.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 900 EEFDMVKLTEYRLQSKVRQLEYLKnnHLPALLEEKQRATE---VLDRGLLGLDntLYQIEKEIEDKEEQLAQYRASTNQL 976
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELLE--PIRELAERYAAARErlaELEYLRAALR--LWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 977 QQLQETFEftANVARQEEKVRKKEKEILQS------REKQQREALEQAVAKLERRHSALQRR-STIDFEI-------EEQ 1042
Cdd:COG4913 308 EAELERLE--ARLDALREELDELEAQIRGNggdrleQLEREIERLERELEERERRRARLEALlAALGLPLpasaeefAAL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024488903 1043 KQKLATLNNSCSEQAGL----QASLEAEQKALEQDRERLDQEIQQLKQK 1087
Cdd:COG4913 386 RAEAAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
653-940 |
7.98e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 653 KETEIVQLQIRKQEESLKRRSVHIES--RLKDLLAEKEKFEEERLREQQEIELQKKKQQE---------EIFARVKEELQ 721
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQdeGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEakktetgkaEEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 722 RLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLEsekKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEE 801
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA---RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDA 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 802 KRDLEDIR-ESLLKVKEARSEGEENCEELEKAqhsfIEFKKKQLEQLTILEKdlvqQMNHLEKDIAHEKETPEYLRlaee 880
Cdd:PTZ00121 1200 RKAEAARKaEEERKAEEARKAEDAKKAEAVKK----AEEAKKDAEEAKKAEE----ERNNEEIRKFEEARMAHFAR---- 1267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 881 EHVNLKKDDENFGDAVFKAEEfdMVKLTEYRLQSKVRQLEYLKNNhlpalLEEKQRATEV 940
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEE--KKKADEAKKAEEKKKADEAKKK-----AEEAKKADEA 1320
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
666-819 |
9.19e-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: 40.21 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024488903 666 EESLKRRSVHIESRLKDLLAEKEKFEEERLREQQEIELQKKkqqEEIFAR--VKEELQRLQELNHKEKAEKMQIFRELEK 743
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR---EETFARtaLKNARLDLRRLFDEKQSEKDKKNKALAE 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024488903 744 LKKEKDEQYIKLESEKKRIeeqEREQVMLVAHLEEQLREKQVMIQllkrGDVQRVEEEKRDLED-IRESLLKVKEAR 819
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKQ----AYWQVVEGALDAQLAlLKAAIAARRSGA 745
|
|
| |
