|
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: 556.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 2 ASVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPEGGTGDTgRERTKTFTYDFSYFSADSKSPSFVCQETVFKN 81
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 82 LGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKIsEKTKRNEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI-ADTTNQNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 162 L-RRKSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSE- 239
Cdd:cd01365 159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAtnplSKKKQVFVPYRDSVLTWL 318
Cdd:cd01365 239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGK----SKKKSSFIPYRDSVLTWL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2024393536 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-150 |
|
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: 457.80 E-value: 1.33e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPeggtgdTGRERTKTFTYDFSYFSADSkspsfvcQETVFKNL 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSP------KNRQGEKKFTFDKVFDATAS-------QEDVFEET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKIseKTKRNEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129 68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI--DKREEGWQFSVKVSYLEIYNEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 163 rrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMPC 242
Cdd:smart00129 146 ---NPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdatnplskkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024393536 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
9-358 |
5.64e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 453.18 E-value: 5.64e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 9 RVRPMNRREKDLNAKFIISMEKNKTTITNLKIpeggtgDTGRERTKTFTYDFSYfsadsksPSFVCQETVFKNLGTDVLQ 88
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVF-------DPEATQEDVYEETAKPLVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 89 SAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKTKRNEasFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225 68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSE--FSVKVSYLEIYNEKIRDLLSPSNKN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 169 TNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225 146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225 226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
|
330 340 350
....*....|....*....|....*....|..
gi 2024393536 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 |
1.05e-136 |
|
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: 1.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPEGGTgdtgrertKTFTYDFSyFSADSKspsfvcQETVFKNL 82
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAV-FDSTST------QEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMG-NAGDAGLIPRICEGLFSKISEKTKRNeASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGpDPEQRGIIPRALEDIFERIDKRKETK-SSFSVSASYLEIYNEKIYDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 162 LRrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMP 241
Cdd:cd00106 145 LS--PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 2024393536 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 |
3.13e-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: 374.49 E-value: 3.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITnLKIPEGGTGdtgrERTKTFTYDFSYfsadsksPSFVCQETVFKNL 82
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFDAVF-------DPNSKQLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA---GLIPRICEGLFSKISEKtkRNEASFRTEVSYLEIYNERVR 159
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARS--QNNQQFLVRVSYLEIYNEEIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 160 DLLRRKSSKtnNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKF--D 237
Cdd:cd01371 148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTW 317
Cdd:cd01371 226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024393536 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 |
4.00e-116 |
|
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: 366.27 E-value: 4.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITnlkipeggtgdtgRERTKTFTYDFSYFSADSkspsfvcQETVFKNL 82
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVFDPSTE-------QEEVYNTC 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA------GLIPRICEGLFSKISEKTKRNEasFRTEVSYLEIYNE 156
Cdd:cd01372 62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKKDTFE--FQLKVSFLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 157 RVRDLLRRKSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKF 236
Cdd:cd01372 140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplSKKKQVFV 308
Cdd:cd01372 220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---------ESKKGAHV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024393536 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 |
1.29e-104 |
|
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: 335.47 E-value: 1.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNKTTI-------TNLKIPEGGTGDTGRERTKTFTYDFSY-FSADSkspsfvC 74
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVfdpkdeeDGFFHGGSNNRDRRKRRNKELKYVFDRvFDETS------T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 75 QETVFKNLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKIseKTKRNEASFRTEVSYLEIY 154
Cdd:cd01370 75 QEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI--ESLKDEKEFEVSMSYLEIY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 155 NERVRDLLRrKSSKTnnLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQ- 233
Cdd:cd01370 153 NETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQq 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplSKKKQVFVPYRDS 313
Cdd:cd01370 230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---------PGKKNKHIPYRDS 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024393536 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370 301 KLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-360 |
5.70e-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: 322.24 E-value: 5.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 9 RVRPMNRREKDLNAKFIISMEKNKTTITNLKipeggtgdtGRERTKTFTYDFSYFSADSkspsfvcQETVFKNLGTDVlQ 88
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELTS---------IGAKQKEFSFDKVFDPEAS-------QEDVFEEVSPLV-Q 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 89 SAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKTKRNeASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:cd01366 72 SALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKG-WSYTIKASMLEIYNETIRDLLAPGNAP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 169 TNNLRIREHPKEGP-YVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINF------TQAKfdsemp 241
Cdd:cd01366 151 QKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 242 ceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdatnplskKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01366 225 --SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQD 290
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024393536 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366 291 SLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
3-358 |
1.04e-99 |
|
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: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDLNAKFIISMEKNktTITNLKIPEGgtgdtgrertkTFTYDFSYfsaDSKSPSfvcqETVFKNL 82
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEIDND--TIYLVEPPST-----------SFTFDHVF---GGDSTN----REVYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKTKRNeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 163 rrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTIN-FTQAKFDSEMP 241
Cdd:cd01374 138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplsKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374 215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 2024393536 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374 285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
4-367 |
6.59e-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: 319.84 E-value: 6.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 4 VKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLKIPeggtgdtgrertKTFTYDfSYFSADSKspsfvcQETVFKNLG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPP------------KTFTFD-HVADSNTN------QESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 84 TDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA--------GLIPRICEGLFSKIS-EKTKRNEA-SFRTEVSYLEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrEKEKAGEGkSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 154 YNERVRDLLRRKSSktnNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQ 233
Cdd:cd01373 144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDatnplskkKQVFVPYRDS 313
Cdd:cd01373 221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2024393536 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 |
4.01e-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: 314.27 E-value: 4.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1 MASVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNlkipeggtgdtGRERTKTFTYDfSYFSADSKspsfvcQETVFK 80
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIA-----------TSETGKTFSFD-RVFDPNTT------QEDVYN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 81 NLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDA---GLIPRICEGLFSKISEKTKrnEASFRTEVSYLEIYNER 157
Cdd:cd01369 63 FAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDE--NLEFHVKVSYFEIYMEK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 158 VRDLLrrKSSKTNnLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAkfD 237
Cdd:cd01369 141 IRDLL--DVSKTN-LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--N 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 238 SEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLTW 317
Cdd:cd01369 216 VETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLTR 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024393536 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 |
7.44e-91 |
|
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: 297.70 E-value: 7.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1 MASVKVAVRVRPMNRREKDLNAKFIISMEKNKTTITnlkipEGGTGDTGRERTKTFTYDFSyFSADSKspsfvcQETVFK 80
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS-----VRTGGLADKSSTKTYTFDMV-FGPEAK------QIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 81 NLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAG-----------DAGLIPRICEGLFSKISektkRNEASFRTEVS 149
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDRSpneeytweldpLAGIIPRTLHQLFEKLE----DNGTEYSVKVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 150 YLEIYNERVRDLLRRKSSKTNNLRIREHP--KEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364 145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 228 TINFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskkK 304
Cdd:cd01364 225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393536 305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364 291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
75-441 |
3.43e-81 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 278.16 E-value: 3.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 75 QETVFKNLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEKtkRNEASFRTEVSYLEIY 154
Cdd:COG5059 70 QEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDL--SMTKDFAVSISYLEIY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 155 NERVRDLLrrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTInfTQA 234
Cdd:COG5059 148 NEKIYDLL---SPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplsKKKQVFVPYRDSV 314
Cdd:COG5059 223 SKNKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINEDPNVKL--------IRELRAEIARLKAL 386
Cdd:COG5059 293 LTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFR 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393536 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 |
5.11e-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: 257.94 E-value: 5.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVN 525
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2024393536 526 GIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PX_KIF16B_SNX23 |
cd06874 |
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ... |
1188-1315 |
1.51e-79 |
|
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.
Pssm-ID: 132784 Cd Length: 127 Bit Score: 256.92 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1188 IKISIPRYVLCGQGKDEHYEFEIKITVLDETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSH 1267
Cdd:cd06874 1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2024393536 1268 LETYLRSFFTAMLQSPSSPLHiDKVGSTLSKHTICEFSPFFRKGVFDY 1315
Cdd:cd06874 81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
4-385 |
3.83e-72 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 264.87 E-value: 3.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 4 VKVAVRVRPMNRREKDlnAKFIISMEKNKTTITNlkipeggtgdtgrertKTFTYDfsyfsadSKSPSFVCQETVFKNLG 83
Cdd:PLN03188 100 VKVIVRMKPLNKGEEG--EMIVQKMSNDSLTING----------------QTFTFD-------SIADPESTQEDIFQLVG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 84 TDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNA---------GDA-GLIPRICEGLFSKISE---KTKRNEASFRTEVSY 150
Cdd:PLN03188 155 APLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsGDQqGLTPRVFERLFARINEeqiKHADRQLKYQCRCSF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 151 LEIYNERVRDLLrrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTIN 230
Cdd:PLN03188 235 LEIYNEQITDLL---DPSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 231 FtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAtnpls 301
Cdd:PLN03188 312 V-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG----- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 302 kkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DPNV--KLIRE 375
Cdd:PLN03188 380 --KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQ 457
|
410
....*....|
gi 2024393536 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 |
1.15e-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: 237.48 E-value: 1.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREKDlnakfIISMEKNKTTITNLKIPEGGTGDTGRERTKtFTYDFSYFSADSKspsfvcQETVFKNL 82
Cdd:cd01375 1 KVQAFVRVRPTDDFAHE-----MIKYGEDGKSISIHLKKDLRRGVVNNQQED-WSFKFDGVLHNAS------QELVYETV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMG---NAGDAGLIPRICEGLFSKISEktkRNEASFRTEVSYLEIYNERVR 159
Cdd:cd01375 69 AKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE---RPTKAYTVHVSYLEIYNEQLY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 160 DLLR---RKSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKF 236
Cdd:cd01375 146 DLLStlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatnplskKKQVFVPYRDSVLT 316
Cdd:cd01375 226 TLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKLT 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2024393536 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 |
1.61e-68 |
|
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: 233.73 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 4 VKVAVRVRPMNRREKDLNAKFIISMEKNKTTITNLkipeggtgdtgrERTK----------TFTYDFSyFSADSKSpsfv 73
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYV-FDESSSN---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 74 cqETVFKNLGTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEG----LFSKISEKTKRNEasFRTEVS 149
Cdd:cd01367 65 --ETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 150 YLEIYNERVRDLLRRKSSktnnLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367 141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 230 NFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdatnplskKKQVFV 308
Cdd:cd01367 217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2024393536 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 |
4.78e-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: 233.05 E-value: 4.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 4 VKVAVRVRPMNRREKDLNAKFIISMEkNKTTITnLKIPEGgtgDTGRERTKTFTYDFSYFSADSKSPSFVCQETVFKNLG 83
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVI-NSTTVV-LHPPKG---SAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 84 TDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSKISEktkrneasFRTEVSYLEIYNERVRDLLR 163
Cdd:cd01368 78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG--------YSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 164 RKSS----KTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSE 239
Cdd:cd01368 150 PSPSsptkKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdatNPLSKKKQVfVPYRDS 313
Cdd:cd01368 230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024393536 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 |
2.49e-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: 230.08 E-value: 2.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 4 VKVAVRVRPMNRREKDLNAKFIIS-MEKNKTTITNlkipeggtgdtGRERTKTFTYDFSYFSADSKSpsfvcQETVFKNL 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSgIDSCSVELAD-----------PRNHGETLKYQFDAFYGEEST-----QEDIYARE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 GTDVLQSAFEGYNACVFAYGQTGSGKSYTMMGNAGDAGLIPRICEGLFSkISEKTKRneaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376 66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQ-MTRKEAW---ALSFTMSYLEIYQEKILDLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 163 rrkSSKTNNLRIREHPKEGPYVEDLSKHLVQNYGDIEELMDAGNINRTTAATGMNDVSSRSHAIFTINFTQAKFDSEMPC 242
Cdd:cd01376 142 ---EPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdatnplsKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376 219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 2024393536 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 |
9.72e-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: 9.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVN 525
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 2024393536 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 |
1.09e-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: 171.50 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVN 525
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2024393536 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 |
5.49e-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: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTeqdIVLHGLDLESEHCIFENLNGTVNLIPL 517
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2024393536 518 nGAQCSVNGIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713 78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
|
|
| PX_RUN |
cd07277 |
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ... |
1188-1309 |
1.06e-32 |
|
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.
Pssm-ID: 132810 Cd Length: 118 Bit Score: 123.23 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1188 IKISIPRYVLCGQGKDEHYEFEIKITVLDETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSH 1267
Cdd:cd07277 1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2024393536 1268 LETYLRSFFTAMLQSPSsplhidKVGSTLSKHTICEFSPFFR 1309
Cdd:cd07277 81 LQVYLRRVVNTLIQTSP------ELTACPSKETLIKLLPFFG 116
|
|
| FHA_KIF1 |
cd22705 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
453-553 |
3.44e-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: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVNGIQITEA 532
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 2024393536 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 |
1.66e-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: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVNGIQI 529
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 2024393536 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 |
1.66e-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: 105.40 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGT-----VNLIPLNGAQCSVNGIQ 528
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 2024393536 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 |
4.69e-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: 98.18 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIF---ENLNG--TVNLIPLNGAQCSVNGIQ 528
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrseRNNNGevIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 2024393536 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 |
7.78e-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: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 75 QETVFKNLGtDVLQSAFEGYN-ACVFAYGQTGSGKSYTMMgnagdaGLIPRICEGLFSKIseKTKRNEASFRTEVSYLEI 153
Cdd:cd01363 32 QPHVFAIAD-PAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGI--NKGETEGWVYLTEITVTL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 154 YNErvrdllrrkssktnnlrirehpkegpyvedlskhlvqnygdIEELMDAGNINRtTAATGMNDVSSRSHAIFTInftq 233
Cdd:cd01363 103 EDQ-----------------------------------------ILQANPILEAFG-NAKTTRNENSSRFGKFIEI---- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024393536 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 |
1.45e-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: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLN-GAQCSVNGIQITEA 532
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 2024393536 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 |
4.08e-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: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 471 YHLKEgQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNGAQCSVNGIQITEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 2024393536 551 FNHP 554
Cdd:cd22706 98 LNCP 101
|
|
| PX_domain |
cd06093 |
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ... |
1189-1274 |
9.11e-21 |
|
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.
Pssm-ID: 132768 [Multi-domain] Cd Length: 106 Bit Score: 88.57 E-value: 9.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1189 KISIPRYVLCGQGKDEHYEFEIKITVLD-ETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSH 1267
Cdd:cd06093 1 SVSIPDYEKVKDGGKKYVVYIIEVTTQGgEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQ 80
|
....*..
gi 2024393536 1268 LETYLRS 1274
Cdd:cd06093 81 LEQYLQS 87
|
|
| FHA_KIF1C |
cd22728 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
454-553 |
1.70e-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: 84.92 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAmteqDIVLHGLDLESEHCIFE---NLNG--TVNLIPLNGAQCSVNGIQ 528
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRsipNPSGevVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 2024393536 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 |
8.38e-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: 8.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 3 SVKVAVRVRPMNRREkdlnakFIISMEKNKTTITnlkipeggtgdTGRERTKTFTYDfSYFSADSKSpSFVCQEtvFKNL 82
Cdd:pfam16796 21 NIRVFARVRPELLSE------AQIDYPDETSSDG-----------KIGSKNKSFSFD-RVFPPESEQ-EDVFQE--ISQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 83 gtdvLQSAFEGYNACVFAYGQTGSGksytmmgnaGDAGLIPRICEGLFSKISEKTKrnEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796 80 ----VQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
597-1079 |
9.03e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhiESRLKDLLAEK 676
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-----LEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELnHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 757 EQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQhsfiefkkKQLEQL 836
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE--------EEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 837 TILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVF----------------------KAEEFDMV 894
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllaglrglagavavligveAAYEAALE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 895 KLTEYRLQSKV--------RQLEYLKNNHL------------PALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQ 954
Cdd:COG1196 542 AALAAALQNIVveddevaaAAIEYLKAAKAgratflpldkirARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 955 LAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQK 1034
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2024393536 1035 LATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1079
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
595-1073 |
3.58e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 595 GLEFERQQREELE-KLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLL 673
Cdd:COG1196 303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 674 AEKEKFEEERLReqqeiELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQyIKLESEKKRIEE 753
Cdd:COG1196 383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL-EEAAEEEAELEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 754 QEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARsEGEENCEELEKAQHSFIEFKKKQL 833
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVLIGVEAA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 834 EQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKN 913
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 914 NHLPALLEEKQRATEVLDRGLL---GLDNTLYQIEKEIEDKEEQLAQYRASTNQ-LQQLQETFEFTANVARQEEKVRKKE 989
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRravTLAGRLREVTLEGEGGSAGGSLTGGSRRElLAALLEAEAELEELAERLAEEELEL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 990 KEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQE 1069
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
....
gi 2024393536 1070 IQQL 1073
Cdd:COG1196 776 IEAL 779
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
453-554 |
2.56e-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: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDAMTEQDIVLHGLDLESEHCIFENLNGTVNLIPLNG-AQCSV 524
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 2024393536 525 NGIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| PX_IRAS |
cd06875 |
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ... |
1185-1279 |
7.06e-14 |
|
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.
Pssm-ID: 132785 Cd Length: 116 Bit Score: 69.23 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1185 KDPIKISIPRYVLcgqgKDEHYEFEIKITVLDETWTVFRRYSRFREMHRTLKLKYpEVATLEFPPKKLFGNKDERVIAER 1264
Cdd:cd06875 1 EPETKIRIPSAET----VEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEH-KVDKDLLPPKKLIGNKSPSFVEKR 75
|
90
....*....|....*....
gi 2024393536 1265 RSHLETYLRS----FFTAM 1279
Cdd:cd06875 76 RKELEIYLQTllsfFQKTM 94
|
|
| PX |
smart00312 |
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ... |
1201-1274 |
2.21e-13 |
|
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.
Pssm-ID: 214610 Cd Length: 105 Bit Score: 67.37 E-value: 2.21e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1201 GKDEHYEFEIKITVLD--ETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFG---NKDERVIAERRSHLETYLRS 1274
Cdd:smart00312 8 GDGKHYYYVIEIETKTglEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQS 86
|
|
| PX |
pfam00787 |
PX domain; PX domains bind to phosphoinositides. |
1216-1274 |
1.52e-12 |
|
PX domain; PX domains bind to phosphoinositides.
Pssm-ID: 459940 Cd Length: 84 Bit Score: 64.18 E-value: 1.52e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1216 DETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSHLETYLRS 1274
Cdd:pfam00787 6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQR 64
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
364-476 |
1.56e-12 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 67.17 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 364 INEDPNVKLIRELRAEIARLKALL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 2024393536 463 LLSTGIILYHLKEG 476
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
456-564 |
2.73e-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: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 456 LIGIDDDLLSTGIILYHLKeGQTYVGredAMTEQDIVLHGLDLESEHCIFE-NLNGTVNLIPLNGAQCSVNGIQITEATH 534
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 2024393536 535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| PX_SNX13 |
cd06873 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ... |
1216-1274 |
3.23e-12 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.
Pssm-ID: 132783 Cd Length: 120 Bit Score: 64.60 E-value: 3.23e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1216 DETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSHLETYLRS 1274
Cdd:cd06873 38 EESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYLQS 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
599-1095 |
3.57e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhieSRLKDLLAEKEK 678
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA------AEEKAEAAEKKK 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 679 FEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKmqifrELEKLKKEKDEQYIKLESEKKRIEEQEREQ 758
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK-----KADEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 759 VMLVAHLEEQLREKQVMIQLLKRGD-VQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLT 837
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 838 ILEKdlVQQMDHLEKdiAHEKETLEYLKLAEE----EHV----NLKKDDENFGDAVFKAEEfdMVKLTEYRLQSKVRQLE 909
Cdd:PTZ00121 1529 KAEE--AKKADEAKK--AEEKKKADELKKAEElkkaEEKkkaeEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 910 ---YLKNNHLPALLEEKQRATEVldrgllgldNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVR 986
Cdd:PTZ00121 1603 eekKMKAEEAKKAEEAKIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 987 KKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIE--EQKQKLATLNNSCSEQAGLQAslEAEQKALEQDR- 1063
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaEELKKAEEENKIKAEEAKKEA--EEDKKKAEEAKk 1751
|
490 500 510
....*....|....*....|....*....|....
gi 2024393536 1064 -ERLDQEIQQL-KQKIYESDGGQKGNHGMLEEKL 1095
Cdd:PTZ00121 1752 dEEEKKKIAHLkKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| PX_MONaKA |
cd06871 |
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ... |
1200-1272 |
1.52e-11 |
|
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.
Pssm-ID: 132781 Cd Length: 120 Bit Score: 62.76 E-value: 1.52e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 1200 QGKDEHYEFEIKIT--VLDE-TWTVFRRYSRFREMHRTLKLKYPEvatLEFPPKKLFGNKDERVIAERRSHLETYL 1272
Cdd:cd06871 16 QNIQSHTEYIIRVQrgPSPEnSWQVIRRYNDFDLLNASLQISGIS---LPLPPKKLIGNMDREFIAERQQGLQNYL 88
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
603-877 |
1.63e-11 |
|
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: 69.32 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 603 REELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVEsqrketeivqlQIRKQEESLKRRSVHIESRLKDLLAEKEKfeee 682
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLE-----------ELRLEVSELEEEIEELQKELYALANEISR---- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 683 rlreqqeIELQKKKQQEEiFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLV 762
Cdd:TIGR02168 300 -------LEQQKQILRER-LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 763 AHLE------EQLREKQVMIQL---LKRGDVQRVEEEKRDLEDIRESLLkvKEARSEGEENCEELEKAQHSFIEFKKKQL 833
Cdd:TIGR02168 372 SRLEeleeqlETLRSKVAQLELqiaSLNNEIERLEARLERLEDRRERLQ--QEIEELLKKLEEAELKELQAELEELEEEL 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2024393536 834 EQLTILEKDLVQQMDHLEKDIAhEKETLEYLKLAEEEHVNLKKD 877
Cdd:TIGR02168 450 EELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLD 492
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
600-869 |
2.20e-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: 68.61 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEKLESKRKQIEEME-------EKQRSDKAELVRMQQEVEsqrKETEIVQLQIRKQE-ESLKRRSVHIE-SRLK 670
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAMERE---RELERIRQEERKRElERIRQEEIAMEiSRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 671 DLlaEKEKFEEERLREQQEIELQ---KKKQQEEIFARVKEELQRLQELNHKEKAEKMQifRELEKLKKEKDEqyiklESE 747
Cdd:pfam17380 379 EL--ERLQMERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ--REVRRLEEERAR-----EME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 748 KKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKR-----DLEDIRESLLKVKEARSEGEENCEELEKAQ 822
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERKRKLLEKEMEERQKAI 529
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2024393536 823 HSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEE 869
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
456-554 |
9.29e-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: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 456 LIGIDDDLLSTGIILYHLKEgQTYVGREDAmteQDIVLHGLDLESEHCIFE-NLNGTVNLIPLNGAQCSVNGIQITEATH 534
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 2024393536 535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
599-1077 |
1.25e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 678
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 679 FEEERLREQQEIE--LQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:COG1196 419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 757 EQVMLVAHLEEQLREKQVMIQLLKRGDVQRVeeekRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQL 836
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVL----IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 837 TILEKDLVQQMDHLEKDIAHEKETLEYLKLA---EEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKN 913
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVAsdlREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 914 NHLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEIL 993
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 994 QSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLN--NSCSEQAglQASLEAEQKALEQDRERLDQEIQ 1071
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvNLLAIEE--YEELEERYDFLSEQREDLEEARE 812
|
....*.
gi 2024393536 1072 QLKQKI 1077
Cdd:COG1196 813 TLEEAI 818
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
597-895 |
2.30e-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: 65.46 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIvqlqIRKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR----LEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIE--LQKKKQQEEIFARVKEELQ----RLQELN------HKEKAEKMQIFRELEKLKKEKDEQYIKL 744
Cdd:TIGR02168 764 EELEERLEEAEEELAeaEAEIEELEAQIEQLKEELKalreALDELRaeltllNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 745 ESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLL---KRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKA 821
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALlneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393536 822 QHSFIEfKKKQLEQ--LTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKA-EEFDMVK 895
Cdd:TIGR02168 924 LAQLEL-RLEGLEVriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAiEEYEELK 999
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
601-868 |
3.73e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 64.61 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 601 QQREELEKLESKRKQIEEMEEKQRSDKAEL-------VRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLL 673
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELeeeyllyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 674 AEKEKFEEERLREQQEIELQKKKQQEEIFARVK---------EELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKL 744
Cdd:pfam02463 272 KENKEEEKEKKLQEEELKLLAKEEEELKSELLKlerrkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 745 ESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAqhs 824
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE--- 428
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2024393536 825 fIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAE 868
Cdd:pfam02463 429 -LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
|
| PX_SNARE |
cd06897 |
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ... |
1189-1287 |
8.99e-10 |
|
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.
Pssm-ID: 132807 Cd Length: 108 Bit Score: 57.28 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1189 KISIPRYVLcgQGKDEHYeFEIKITVLDETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLF--GNKDERVIAERRS 1266
Cdd:cd06897 2 EISIPTTSV--SPKPYTV-YNIQVRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFlsTSSNPKLVEERRV 78
|
90 100
....*....|....*....|.
gi 2024393536 1267 HLETYLRsfftAMLQSPSSPL 1287
Cdd:cd06897 79 GLEAFLR----ALLNDEDSRW 95
|
|
| PX_SNX22 |
cd06880 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ... |
1188-1272 |
1.04e-09 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.
Pssm-ID: 132790 Cd Length: 110 Bit Score: 57.28 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1188 IKISIP--RYVLCGQGKdEHYEFEIKITVLDETWTVFRRYSRFREMHRTLKLKYPevaTLEFPPKKLfGNKDERVIAERR 1265
Cdd:cd06880 1 IEVSIPsyRLEVDESEK-PYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIK---TPDFPPKRV-RNWNPKVLEQRR 75
|
....*..
gi 2024393536 1266 SHLETYL 1272
Cdd:cd06880 76 QGLEAYL 82
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
600-1071 |
2.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVES-----QRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLA 674
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreelEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 675 EKEKFEEERLREQqeielQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ 754
Cdd:COG4717 154 RLEELRELEEELE-----ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 755 --EREQVMLVAHLEEQLREKQVMIQLLKrgdvqrveeekrdledireSLLKVKEARSEGEENCEELEKAQHSFIEFKKKQ 832
Cdd:COG4717 229 leQLENELEAAALEERLKEARLLLLIAA-------------------ALLALLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 833 LEQLTILEKDLVQQMDHLEKDIAHEK-ETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEfdmvklteyrLQSKVRQLEYL 911
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEE----------LQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 912 KNNHLPALLEEKQRAteVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETF-EFTANVARQEEKVRKKEK 990
Cdd:COG4717 360 EEELQLEELEQEIAA--LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeELLEALDEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 991 EILQSREKQQREALEQAVAKLERRHSALQRrstiDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEI 1070
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEE----DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
.
gi 2024393536 1071 Q 1071
Cdd:COG4717 514 L 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
595-933 |
3.57e-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: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 595 GLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQ-QEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLL 673
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 674 AEKEKFEEERLREQQEIELQKKKQQEE-----IFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEK 748
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVlkenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 749 KRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEF 828
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 829 KKKQLEQLTILEKDLVQQMDhLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKA--EEFDMVKLTEYRLQSKVR 906
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKE-EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKdeLELKKSEDLLKETQLVKL 482
|
330 340
....*....|....*....|....*..
gi 2024393536 907 QLEYLKNNHLPALLEEKQRATEVLDRG 933
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| PX_SNX20_21_like |
cd07279 |
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ... |
1223-1273 |
4.24e-09 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.
Pssm-ID: 132812 Cd Length: 112 Bit Score: 55.41 E-value: 4.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2024393536 1223 RRYSRFREMHRTLKLKYP-EVATLEFPPKKLFGNKDERVIAERRSHLETYLR 1273
Cdd:cd07279 40 RRYSDFLKLYKALRKQHPqLMAKVSFPRKVLMGNFSSELIAERSRAFEQFLG 91
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
596-790 |
5.71e-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: 60.52 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 596 LEFERQQREEL--EKLESKRKQIEEMEEKQRSDKAELVRMQQ---------EVESQRKETEIVQLQIRKQEESLKR---- 660
Cdd:pfam17380 383 LQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQiraeqeearQREVRRLEEERAREMERVRLEEQERqqqv 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 661 ---RSVHIESRLKDLLAEKEKFEEERLReqqeiELQKKKQQEEIFARVKE--ELQRLQELNHKEKAEKMQIFRELEKLKK 735
Cdd:pfam17380 463 erlRQQEEERKRKKLELEKEKRDRKRAE-----EQRRKILEKELEERKQAmiEEERKRKLLEKEMEERQKAIYEEERRRE 537
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 736 EKDEQYIKLE-SEKKRIEEQEREQVMLVAHLEEQLREKQVMIQlLKRGDVQRVEEE 790
Cdd:pfam17380 538 AEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQ-IVESEKARAEYE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
597-1093 |
1.61e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVEsqRKETEIVQlqIRKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS--RLEQQKQI--LRERLANLERQLEELEAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIElQKKKQQEEIFARVKEELQRLQELNHKEKAekmqIFRELEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:TIGR02168 333 DELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 757 EQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQL 836
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 837 TILEKDLVQQMDHLEKdiahEKETLEYLKLAEEE---HVNLKKD----DENFGDAVFKAEEFDMVKLTEYRLQSKVRQLE 909
Cdd:TIGR02168 488 QARLDSLERLQENLEG----FSEGVKALLKNQSGlsgILGVLSElisvDEGYEAAIEAALGGRLQAVVVENLNAAKKAIA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 910 YLKNNHL------------PALLEEKQRATEVLDRGLLGLDNTL-YQIEKEIEDKEEQLAQYR------ASTNQLQQLQE 970
Cdd:TIGR02168 564 FLKQNELgrvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLvKFDPKLRKALSYLLGGVLvvddldNALELAKKLRP 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 971 TFEF-TAN---VARQEEKVRKKEKEILQSREKQQR-EALEQAVAKLERR-HSALQRRSTIDFEIEEQKQKLATLNNSCSE 1044
Cdd:TIGR02168 644 GYRIvTLDgdlVRPGGVITGGSAKTNSSILERRREiEELEEKIEELEEKiAELEKALAELRKELEELEEELEQLRKELEE 723
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2024393536 1045 QAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYESDGGQKGNHGMLEE 1093
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
586-809 |
1.68e-08 |
|
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: 58.24 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 586 LSAVMLYNPGLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhI 665
Cdd:COG4942 6 LLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 666 ESRLKDLLAEKEKFEEERLREQQEIE-----LQKKKQQEEI--------FARVKEELQRLQELN----------HKEKAE 722
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAellraLYRLGRQPPLalllspedFLDAVRRLQYLKYLAparreqaeelRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 723 KMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgdvqrveeEKRDLEDIRESLL 802
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLE 233
|
....*..
gi 2024393536 803 KVKEARS 809
Cdd:COG4942 234 AEAAAAA 240
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
600-771 |
1.72e-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: 58.81 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEKLESKRKQIEEMEEKQRS----DKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAE 675
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQqeqlERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 676 KEKFEEERLREQQEIELQKKKQQEEIfARVKEELQRLQELNHK--EKAEKMQIFRELEKL----KKEKDEQYIKLESEKK 749
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQEEA-ERAEAEKQRQKELEMQlaEEQKRLMEMAEEERLeyqrQKQEAEEKARLEAEER 497
|
170 180
....*....|....*....|....*
gi 2024393536 750 RIEEQEREQVML---VAHLEEQLRE 771
Cdd:pfam15709 498 RQKEEEAARLALeeaMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
645-960 |
1.87e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 645 EIVQLQIRKQEESLKRrsvhiESR-------LKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNH 717
Cdd:COG1196 192 EDILGELERQLEPLER-----QAEkaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 718 KEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDI 797
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 798 RESLLKVKEARSEGEENCEELEKAQHSFIEfKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKD 877
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAE-AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 878 DENfgDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKNNHLpALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQ 957
Cdd:COG1196 426 LEE--ALAELEEEEEEEEEALEEAAEEEAELEEEEEALL-ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
...
gi 2024393536 958 YRA 960
Cdd:COG1196 503 YEG 505
|
|
| PX_CISK |
cd06870 |
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ... |
1202-1272 |
3.12e-08 |
|
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.
Pssm-ID: 132780 Cd Length: 109 Bit Score: 52.80 E-value: 3.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393536 1202 KDEHYE-FEIKITVLDETWTVFRRYSRFREMHRTLKLKYPEVAtLEFPPKKLFGNK-DERVIAERRSHLETYL 1272
Cdd:cd06870 16 KKKRFTvYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPASN-LKIPGKRLFGNNfDPDFIKQRRAGLDEFI 87
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
616-909 |
4.95e-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: 57.77 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 616 IEEMEEKQRSDKAELvrmqQEVESQRKETEIVQLQIRKQEESLKRRSVHIEsRLKDLLAEKEKFeeerlreQQEIELQKK 695
Cdd:TIGR02169 165 VAEFDRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY-------EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 696 KQQEEIFARVKEELQRLQElnhkekaEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ-EREQVmlvaHLEEQLREKQV 774
Cdd:TIGR02169 233 EALERQKEAIERQLASLEE-------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQL----RVKEKIGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 775 MIQLLKRgdvqRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAqhsfIEFKKKQLEQLTILEKDLVQQMDHLEKDI 854
Cdd:TIGR02169 302 EIASLER----SIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----IEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2024393536 855 AHEKETLEYLKlaeEEHVNLKKDDENFGdavfkaEEFDMVKLTEYRLQSKVRQLE 909
Cdd:TIGR02169 374 EEVDKEFAETR---DELKDYREKLEKLK------REINELKRELDRLQEELQRLS 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
578-870 |
5.74e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 578 DLSKSCENLSAVMlynpglefeRQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEivqlQIRKQEES 657
Cdd:PRK03918 159 DYENAYKNLGEVI---------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP----ELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 658 LKRRSVHIESrLKDLLAEKEKFEEERLREQQEIElQKKKQQEEIFARVKEELQRLQElnhkekaekmqIFRELEKLKKEK 737
Cdd:PRK03918 226 LEKEVKELEE-LKEEIEELEKELESLEGSKRKLE-EKIRELEERIEELKKEIEELEE-----------KVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 738 DEqYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLL--KRGDVQRVEEE----KRDLEDIRESLLKVKEARSEG 811
Cdd:PRK03918 293 EE-YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEAKAKK 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 812 EENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEE 870
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
600-808 |
5.97e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEK-LESKRKQIEEMEEKQRSDKAELVRMQQEVESQ----RKETEIVQLQIRKqeeslKRRSVHIE-SRLKDLL 673
Cdd:TIGR02169 236 ERQKEAIERqLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKE-----KIGELEAEiASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 674 AEKEKFEEERLREQQEIELQKKKQQEEI------FARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESE 747
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIeelereIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 748 KKRIEEQEREqvmlvahLEEQLREKQVMIQLLKRGDvQRVEEEKRDLEDIRESLLKVKEAR 808
Cdd:TIGR02169 391 REKLEKLKRE-------INELKRELDRLQEELQRLS-EELADLNAAIAGIEAKINELEEEK 443
|
|
| PX_MDM1p |
cd06876 |
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ... |
1218-1276 |
6.04e-08 |
|
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.
Pssm-ID: 132786 Cd Length: 133 Bit Score: 52.70 E-value: 6.04e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 1218 TWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDER--VIAERRSHLETYLRSFF 1276
Cdd:cd06876 56 GWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKtlLVEERRKALEKYLQELL 116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-973 |
6.85e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 640 QRKETEivqLQIRKQEESLKRrsvhiesrLKDLLAEKEKFEEErlreqqeieLQKKKQQEEIFARVKEEL---------Q 710
Cdd:TIGR02168 173 RRKETE---RKLERTRENLDR--------LEDILNELERQLKS---------LERQAEKAERYKELKAELrelelallvL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 711 RLQELNHK------EKAEKMQIFRELEKLKKEKDEQYIKLESEK---------------------KRIEEQEREQVMLVA 763
Cdd:TIGR02168 233 RLEELREEleelqeELKEAEEELEELTAELQELEEKLEELRLEVseleeeieelqkelyalaneiSRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 764 HLEEQLREKQVMIQLLKRgDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDL 843
Cdd:TIGR02168 313 NLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 844 VQQMDHLEKDIAHEKETLEYLKlaeeehVNLKKDDENFGDAVFKAEEFDMVKLTEyrlqskvrQLEYLKnnhlpALLEEK 923
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLE------DRRERLQQEIEELLKKLEEAELKELQA--------ELEELE-----EELEEL 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024393536 924 QRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFE 973
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
598-929 |
8.85e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 598 FERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEV----ESQRKETEIVQLQIRKQEESlkrRSVHIESRLKDll 673
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKRVEIARKAEDA---RKAEEARKAED-- 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 674 AEKEKFEEERLREQQEIELQKKKQQEEI-FARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEqyiklesekKRIE 752
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE---------AKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 753 EQEREQvmlvahlEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIR--ESLLKVKEARSEGEENCEELEKAQHSfiefKK 830
Cdd:PTZ00121 1246 EEERNN-------EEIRKFEEARMAHFARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEKKKADEAKKKAE----EA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 831 KQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQS-KVRQLE 909
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAeEKKKAD 1394
|
330 340
....*....|....*....|
gi 2024393536 910 YLKNNhlpaLLEEKQRATEV 929
Cdd:PTZ00121 1395 EAKKK----AEEDKKKADEL 1410
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
597-806 |
9.96e-08 |
|
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: 56.75 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELvrmqqevesQRKETEIVQLQirKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:pfam10174 458 QREREDRERLEELESLKKENKDLKEKVSALQPEL---------TEKESSLIDLK--EHASSLASSGLKKDSKLKSLEIAV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKfeeeRLREQQEIELQ-KKKQQEEIFARVKEEL-QRLQELN-----HKEKAEKMQ--------IFRELEKLKKEKDEQY 741
Cdd:pfam10174 527 EQ----KKEECSKLENQlKKAHNAEEAVRTNPEInDRIRLLEqevarYKEESGKAQaeverllgILREVENEKNDKDKKI 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 742 IKLESEKKRieeQEREQVMLVAHL-----EEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKE 806
Cdd:pfam10174 603 AELESLTLR---QMKEQNKKVANIkhgqqEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ 669
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
596-909 |
1.08e-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: 56.61 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 596 LEFERQQREELEK-LESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESL---KRRSVHIESRLKD 671
Cdd:TIGR02169 690 LSSLQSELRRIENrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 672 LLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQE-LNHKEKAEKMQIFRE--LEKLKKEKDEQYIKLE--- 745
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArLREIEQKLNRLTLEKeyLEKEIQELQEQRIDLKeqi 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 746 -SEKKRIEEQEREqvmlVAHLEEQLREKQVMIQLLkrgdvqrvEEEKRDLE-DIRESLLKVKEARSEGEENCEElekaqh 823
Cdd:TIGR02169 850 kSIEKEIENLNGK----KEELEEELEELEAALRDL--------ESRLGDLKkERDELEAQLRELERKIEELEAQ------ 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 824 sfIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKK---DDENFGDAVFKA-EEFDMVKLTEY 899
Cdd:TIGR02169 912 --IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRveeEIRALEPVNMLAiQEYEEVLKRLD 989
|
330
....*....|
gi 2024393536 900 RLQSKVRQLE 909
Cdd:TIGR02169 990 ELKEKRAKLE 999
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
455-551 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 455 HLIGIDDDllsTGIILYHLKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENLNGTVNLIPL---NGaqCSVNGIQITE 531
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGRSP---DCDIVLDDPSVSRRHARIEVDGGGVYLEDLgstNG--TFVNGKRITP 72
|
90 100
....*....|....*....|
gi 2024393536 532 ATHLNQGAVILLGRTNmFRF 551
Cdd:cd00060 73 PVPLQDGDVIRLGDTT-FRF 91
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
599-774 |
1.48e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRR--------------SVH 664
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsylDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 665 IESR-LKDLLAEKEKFEEERLREQQEIELQKKKQQ--EEIFARVKEELQRLQELnhKEKAEKMQifRELEKLKKEKDEQY 741
Cdd:COG3883 109 LGSEsFSDFLDRLSALSKIADADADLLEELKADKAelEAKKAELEAKLAELEAL--KAELEAAK--AELEAQQAEQEALL 184
|
170 180 190
....*....|....*....|....*....|...
gi 2024393536 742 IKLESEKKRIEEQEREQVMLVAHLEEQLREKQV 774
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
996-1097 |
1.57e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 996 REKQQREALEQAVAKLERRHSALQRRSTID-----FEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEI 1070
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100
....*....|....*....|....*..
gi 2024393536 1071 QQLKQKIYESDGGQKGNhgmLEEKLSH 1097
Cdd:COG4913 326 DELEAQIRGNGGDRLEQ---LEREIER 349
|
|
| PX_PI3K_C2 |
cd06883 |
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ... |
1194-1278 |
2.35e-07 |
|
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.
Pssm-ID: 132793 Cd Length: 109 Bit Score: 50.43 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1194 RYVLCGQGK---DEHYEFEIKITV--LDETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERR-SH 1267
Cdd:cd06883 2 VSVFGFQKRyspEKYYIYVVKVTRenQTEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSHIKQVAERRkIE 81
|
90
....*....|.
gi 2024393536 1268 LETYLRSFFTA 1278
Cdd:cd06883 82 LNSYLKSLFNA 92
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
603-1077 |
2.93e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 603 REELEKLESKRKQIEEMEEKQRSDKAELVRMQ---QEVESQRKETEIVQLQIRKQEESLK---------RRSVHIESRLK 670
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKVKELKelkekaeeyIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 671 DLLAEKEKFEEERLREQQEIELQ------KKKQQEEIFARVKEELQRLQELN--HKEKAEKMQIFRELEKLKKEK----- 737
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERikeleeKEERLEELKKKLKELEKRLEELEerHELYEEAKAKKEELERLKKRLtgltp 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 738 ---DEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQ-----RVEEEKRDLEDIRESLLKVKEARS 809
Cdd:PRK03918 387 eklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 810 EGEENCEELEKAQHSFIEFKKKQLEQLTIL-EKDLVQQMDHLEKDIahEKETLEYLKLAEEEHVNLKkddenfgdavfka 888
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIkLKELAEQLKELEEKL--KKYNLEELEKKAEEYEKLK------------- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 889 EEFDMVKLTEYRLQSKVRQLEYLKNNhLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQY-------RAS 961
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelKDA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 962 TNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREAL----EQAVAKLERRHSALQRrstidfEIEEQKQKLAT 1037
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkysEEEYEELREEYLELSR------ELAGLRAELEE 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2024393536 1038 LNNSCSEQAGLQASLEAEQKALEQDRERLD------QEIQQLKQKI 1077
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEklekalERVEELREKV 730
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
597-881 |
3.72e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEivqLQIRKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA---EEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIELQKKKQQEEIfaRVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKI--KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 757 EQVMLVAHLEEQLREKQVMIQLLKRGDVQRvEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQhSFIEFKKKQLEQL 836
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLE-EKENEIEERIKEEAEILLKYEEEPEELLLEEADEK-EKEENNKEEEEER 961
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2024393536 837 TILEKDLVQQ---MDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENF 881
Cdd:pfam02463 962 NKRLLLAKEElgkVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
691-913 |
4.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 691 ELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEqereqvmlvahLEEQLR 770
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 771 EKQVMIQLLkRGDVQRVEEEKRDLED-IRESLLKVKEARSEGEENCEELEKAQH--SFIEFKKKQLEQLTILEKDL---- 843
Cdd:PRK03918 242 ELEKELESL-EGSKRKLEEKIRELEErIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLsrle 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 844 ------VQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMVK--LTEYRLQSKVRQLEYLKN 913
Cdd:PRK03918 321 eeingiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKkrLTGLTPEKLEKELEELEK 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-1077 |
7.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 596 LEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQR-----KETEIVQL-----QIRKQEESLKRRSVHI 665
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrleeLEEQLETLrskvaQLELQIASLNNEIERL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 666 ESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLE 745
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 746 SEKKRIEEQEReqvMLVAHLEEQLREKQVMIQLLKRGDVQ-------RVEEE-----------------KRDLEDIR--- 798
Cdd:TIGR02168 486 QLQARLDSLER---LQENLEGFSEGVKALLKNQSGLSGILgvlseliSVDEGyeaaieaalggrlqavvVENLNAAKkai 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 799 ESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIA----------HEKETLEYLKLAE 868
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLR 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 869 EEHVNLKKDDENF---GDAVFKAEEFDMVKLtEYR-----LQSKVRQLEyLKNNHLPALLEEKQRATEVLDRGLLGLDNT 940
Cdd:TIGR02168 643 PGYRIVTLDGDLVrpgGVITGGSAKTNSSIL-ERRreieeLEEKIEELE-EKIAELEKALAELRKELEELEEELEQLRKE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 941 LYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREK---QQREALEQAVAKLERRHSA 1017
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKA 800
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1018 LQRRstidfeIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKI 1077
Cdd:TIGR02168 801 LREA------LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
601-1077 |
8.18e-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: 53.82 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 601 QQREELEKLESKRKQIEEMEEK--QRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 678
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERinRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 679 FEEERLREQQEIELQKKKQQE----EIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQY------------- 741
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVAtsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAtidtrtsafrdlq 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 742 IKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGdVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKA 821
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES-AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 822 QHsfiEFKKKQLE------QLTILEKD--LVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDM 893
Cdd:TIGR00618 503 PC---PLCGSCIHpnparqDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 894 VKLTEyrLQSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGL----DNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQ 969
Cdd:TIGR00618 580 NRSKE--DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLqpeqDLQDVRLHLQQCSQELALKLTALHALQLTLTQ 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 970 ETFEFTANVARQEEKVRKKEKEI----LQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKL----ATLNNS 1041
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLalqkMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASsslgSDLAAR 737
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1042 CSEQAGLQASLEAEQ----KALEQDRER----------LDQEIQQLKQKI 1077
Cdd:TIGR00618 738 EDALNQSLKELMHQArtvlKARTEAHFNnneevtaalqTGAELSHLAAEI 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
591-938 |
9.68e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 591 LYNPGLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEE--SLKRRSVHIESR 668
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEakAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 669 LKDLLAEK-EKFEEERLREQQEIE------LQKKKQQEEIFARVKEELQRLQ-----------ELNHKEKAEKMQIFR-E 729
Cdd:PRK03918 381 LTGLTPEKlEKELEELEKAKEEIEeeiskiTARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLEEYTaE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 730 LEKLKKEKdeqyIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQL------LKRGDVQRVEEEKRDLEDIRESLLK 803
Cdd:PRK03918 461 LKRIEKEL----KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLkeleekLKKYNLEELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 804 VK-EARSEGEENCEELE-KAQHSFIEFKKKQLEQ-----LTILEKDLVQQMDHLEKDIAH-EKETLEYLKL--AEEEHVN 873
Cdd:PRK03918 537 LKgEIKSLKKELEKLEElKKKLAELEKKLDELEEelaelLKELEELGFESVEELEERLKElEPFYNEYLELkdAEKELER 616
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393536 874 LKKDDENFGDAVFKAEEfdMVKLTEYRLQSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGLD 938
Cdd:PRK03918 617 EEKELKKLEEELDKAFE--ELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR 679
|
|
| PX_SNX19_like_plant |
cd06872 |
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ... |
1212-1273 |
1.16e-06 |
|
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.
Pssm-ID: 132782 Cd Length: 107 Bit Score: 48.29 E-value: 1.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 1212 ITVLD---ETWTVFRRYSRFREMHRTLKlKYPEVAtLEFPPKKLFGNK-DERVIAERRSHLETYLR 1273
Cdd:cd06872 23 VAVTDnenETWVVKRRFRNFETLHRRLK-EVPKYN-LELPPKRFLSSSlDGAFIEERCKLLDKYLK 86
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1081 |
1.33e-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: 53.14 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 833 LEQLTILEKDLVQQMDHLEKdiaHEKETLEYLKL-AEEEHVNLkkdDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYL 911
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLER---QAEKAERYKELkAELRELEL---ALLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 912 KNNhLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKE 991
Cdd:TIGR02168 262 LQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 992 ILQSREKQQREALEQAVAKLERRHSALQ----RRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLD 1067
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEelesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
|
250
....*....|....
gi 2024393536 1068 QEIQQLKQKIYESD 1081
Cdd:TIGR02168 421 QEIEELLKKLEEAE 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-1077 |
1.42e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 691 ELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKD--EQYIKLESEKKRIEEQEREQVMLVAHLEEq 768
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEE- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 769 LREKQVMIQLLKrgdvQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEfkkKQLEQLTILEKDLVQQMD 848
Cdd:COG4717 158 LRELEEELEELE----AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE---EELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 849 HLEKD--IAHEKETLEYLK----------LAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKNNHL 916
Cdd:COG4717 231 QLENEleAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 917 PALLE-EKQRATEVLDRglLGLDNTLyqIEKEIEDKEEQLAQYRASTNQLQQLQEtfeftanvARQEEKVRKKEKEILQS 995
Cdd:COG4717 311 PALEElEEEELEELLAA--LGLPPDL--SPEELLELLDRIEELQELLREAEELEE--------ELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 996 REKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQ--ASLEAEQKALEQDRERLDQEIQQL 1073
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAEL 458
|
....
gi 2024393536 1074 KQKI 1077
Cdd:COG4717 459 EAEL 462
|
|
| PX_SNX8_Mvp1p_like |
cd06866 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ... |
1205-1273 |
1.71e-06 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.
Pssm-ID: 132776 Cd Length: 105 Bit Score: 47.99 E-value: 1.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1205 HYEFEIKiTVLDETwTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSHLETYLR 1273
Cdd:cd06866 18 HVEYEVS-SKRFKS-TVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLN 84
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
590-1103 |
1.84e-06 |
|
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: 52.52 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 590 MLYNPGLEFERQQREELEKLESKRKQIEEMEEKQRSDKAELvrmqqevesQRKETEIVQLQIR-----KQEESLKRrsvH 664
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL---------SKKESELLALQTKletltNQNSDCKQ---H 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 665 IESrLKDLLAEKEKFEEERLREQQEIELqKKKQQEEIFARVKEELQRLQElnhkekaEKMQIFRELEKLKKEKDEQYIKL 744
Cdd:pfam10174 326 IEV-LKESLTAKEQRAAILQTEVDALRL-RLEEKESFLNKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 745 ESEKKRIEeqereqvmlvaHLEEQLREKQVMIQLLKRgdvqRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHS 824
Cdd:pfam10174 397 NVLQKKIE-----------NLQEQLRDKDKQLAGLKE----RVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRER 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 825 FIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLK-----LAE------------EEHVNLKKDDENFGDAVF- 886
Cdd:pfam10174 462 EDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKehassLASsglkkdsklkslEIAVEQKKEECSKLENQLk 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 887 KAEEFDMVKLTEYRLQSKVRQLEylknNHLPALLEEKQRATEVLDRgLLGLdntLYQIEKEIEDKEEQLAQYRASTnqLQ 966
Cdd:pfam10174 542 KAHNAEEAVRTNPEINDRIRLLE----QEVARYKEESGKAQAEVER-LLGI---LREVENEKNDKDKKIAELESLT--LR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 967 QLQETFEFTANVARQEEKVRKKEKEILQ-SREKQQREALEQAVAKLERRHSALQRRSTidfEIEEQKQKLATLNNSCSEQ 1045
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQEMKKKGAQLLEeARRREDNLADNSQQLQLEELMGALEKTRQ---ELDATKARLSSTQQSLAEK 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 1046 AGLQASLEAEQKalEQDRERLDQEIQQLKQKIYESDggqkGNHGMLEekLSHSNSPTN 1103
Cdd:pfam10174 689 DGHLTNLRAERR--KQLEEILEMKQEALLAAISEKD----ANIALLE--LSSSKKKKT 738
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
451-554 |
2.04e-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: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDAMTEQ-DIVLHGLDLESEHCIFEN---------------LN 509
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWIRRkpeplsddedsdkesAD 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2024393536 510 GTVNLIPLNGAQCSVNGIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712 76 YRVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| PX_SNX15_like |
cd06881 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ... |
1220-1272 |
2.05e-06 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.
Pssm-ID: 132791 Cd Length: 117 Bit Score: 48.09 E-value: 2.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393536 1220 TVFRRYSRFREMHRTLKLKYPEVATLE----FPPKKLFGNKDERVIAERRSHLETYL 1272
Cdd:cd06881 39 VVWKRYSDFKKLHRELSRLHKQLYLSGsfppFPKGKYFGRFDAAVIEERRQAILELL 95
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
605-1038 |
2.42e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.28 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 605 ELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKFEEERL 684
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 685 REQQEIElqkKKQQEEIFARVKEELQRLQELNHKEKAEKM--------------QIFRELEKLKKEKDEQYIKLESEKKR 750
Cdd:TIGR00618 481 IHLQETR---KKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgpltrrmqRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 751 I------EEQEREQVMLVAHLEEQLRE-----KQVMIQLLKRGDVQrVEEEKRDLEDIRESLLKVKEARSEGEENCEELE 819
Cdd:TIGR00618 558 RaslkeqMQEIQQSFSILTQCDNRSKEdipnlQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 820 KAQHSFIEFKKKQLEQLTILEKD---------------------LVQQMDHLEKDIAHEKETLEY-LKLAEEEHVNLKKD 877
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERvrehalsirvlpkellasrqlALQKMQSEKEQLTYWKEMLAQcQTLLRELETHIEEY 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 878 DEnfgdavfkaeEFDMVKLTEYRLQSKVRQLEYLKNNHLPALLEEKQRAtevldrgLLGLDNTLYQIEKEIEDKEEQLAQ 957
Cdd:TIGR00618 717 DR----------EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV-------LKARTEAHFNNNEEVTAALQTGAE 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 958 Y----RASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQ 1033
Cdd:TIGR00618 780 LshlaAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK 859
|
....*
gi 2024393536 1034 KLATL 1038
Cdd:TIGR00618 860 QLAQL 864
|
|
| PX_SNX25 |
cd06878 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ... |
1219-1272 |
3.09e-06 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.
Pssm-ID: 132788 Cd Length: 127 Bit Score: 47.75 E-value: 3.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 1219 WTVFRRYSRFREMHRTLKLKYPEVATLEFP--PKKLFGNKDERVIAERRSHLETYL 1272
Cdd:cd06878 50 WVVTRKLSEFHDLHRKLKECSSWLKKVELPslSKKWFKSIDKKFLDKSKNQLQKYL 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-998 |
4.28e-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: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 651 IRKQEESLKRRSVHIEsRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQ-ELNHKEKA--EKMQIF 727
Cdd:TIGR02168 198 LERQLKSLERQAEKAE-RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTaELQELEEKleELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 728 RELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgDVQRVEEEKRDLEDIRESLLKVKEA 807
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES-KLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 808 RSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKlaeeehVNLKKDDENFGDAVFK 887
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE------DRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 888 AEEFDMvKLTEYRLQSKVRQLEYLKnnhlpALLEEKQRATEVLDRGLLGLDNTLYQIEkeiedkeeqlaqyrastNQLQQ 967
Cdd:TIGR02168 430 LEEAEL-KELQAELEELEEELEELQ-----EELERLEEALEELREELEEAEQALDAAE-----------------RELAQ 486
|
330 340 350
....*....|....*....|....*....|.
gi 2024393536 968 LQETFEFTANVARQEEKVRKKEKEILQSREK 998
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
601-1094 |
5.46e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 601 QQREELEKLESKRK----QIEEMEEKQRSDKAEL----VRMQQEVESQRKETEIVQLQIR-----------KQEESLKRR 661
Cdd:pfam05483 265 ESRDKANQLEEKTKlqdeNLKELIEKKDHLTKELedikMSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 662 SVH---------IESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIfarvkEELQRLQELNHKEKAEKMQIFRELEK 732
Cdd:pfam05483 345 AAHsfvvtefeaTTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-----EEMTKFKNNKEVELEELKKILAEDEK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 733 LKKEKdEQYIKLESEkkrIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGD---VQRVEEEKRDLEDIR----------- 798
Cdd:pfam05483 420 LLDEK-KQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEehyLKEVEDLKTELEKEKlknieltahcd 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 799 ESLLKVKEARSEGEENCEELEKAQHSFIEFKKKqleqltilEKDLVQQMDHLEKDIAHEKETLEYLK-----LAEEEHVN 873
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQ--------EERMLKQIENLEEKEMNLRDELESVReefiqKGDEVKCK 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 874 LKKDDENfgdavfkaeefdmVKLTEYRLQSKVRQLEYLKN--NHLPALLEEKQRATEVLDRGLLGLdntlyqiEKEIEDK 951
Cdd:pfam05483 568 LDKSEEN-------------ARSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 952 EEQLAQYRASTNQLQ-----QLQETFEFTANVARQEEKVRKKEKEILQSREKQ----------QREALEQAVAKLERRHS 1016
Cdd:pfam05483 628 NKQLNAYEIKVNKLElelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVA 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1017 ALQR-RSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYESDGGQKGNHGMLEEK 1094
Cdd:pfam05483 708 LMEKhKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
604-1077 |
5.76e-06 |
|
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: 50.89 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 604 EELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVE----------------SQRKETEIVQLQIRKQEESLKRRSVHIES 667
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEitgltekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 668 RLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQEL-NHKEKAEKMqiFRELEKLKKEkdeqyIKLES 746
Cdd:pfam15921 325 TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKL--LADLHKREKE-----LSLEK 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 747 EK-KRIEEQEREQVMLVAHLEEQLREKQVMIQLLkrgdvqrveeekrdledirESLLKVKEARSegeencEELEKAQHSF 825
Cdd:pfam15921 398 EQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-------------------EALLKAMKSEC------QGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 826 IEFKKKQLEQLTILEKDLVQQMDHLEK---DIAHEKETLEylklAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEyRLQ 902
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKvveELTAKKMTLE----SSERTVSDLTASLQEKERAIEATNAEITKLRS-RVD 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 903 SKVRQLEYLKN--NHlpalLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVAR 980
Cdd:pfam15921 528 LKLQELQHLKNegDH----LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 981 qeekVRKKEKEILQSREKQQREALEQAVAKLERRHSAL------QRRSTIDFEiEEQKQKLATLNNSCSEQAGLQASLEA 1054
Cdd:pfam15921 604 ----LELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagseRLRAVKDIK-QERDQLLNEVKTSRNELNSLSEDYEV 678
|
490 500
....*....|....*....|...
gi 2024393536 1055 EQKALEQDRERLDQEIQQLKQKI 1077
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKLKMQL 701
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
712-1076 |
7.17e-06 |
|
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: 50.51 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 712 LQELNHKEKAEKMqifrELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEK 791
Cdd:pfam17380 284 VSERQQQEKFEKM----EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 792 RDLEDIRESLLKVKEARSEgeenceelekaqhsfiEFKKKQLEQLTILEKdLVQQMDHLEKDIAHEKETLEYLKLAEEEH 871
Cdd:pfam17380 360 RELERIRQEEIAMEISRMR----------------ELERLQMERQQKNER-VRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 872 VNLKKDDENfgdavfkAEEFDMVKLTEYRlqskVRQLEYLKNNHLpalleEKQRATEVLDRgllgldNTLYQIEKEIEDK 951
Cdd:pfam17380 423 EQIRAEQEE-------ARQREVRRLEEER----AREMERVRLEEQ-----ERQQQVERLRQ------QEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 952 EEQLAQYRASTNQLQQLQETFEftanvARQEEKVRKKEKEILQSREKQQREaleQAVAKLERRHSALQRRSTiDFEIEEQ 1031
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEKELE-----ERKQAMIEEERKRKLLEKEMEERQ---KAIYEEERRREAEEERRK-QQEMEER 551
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2024393536 1032 KQKLATLNNSCSEQAGLQAsleaeqkaLEQDRERLDQEIQQLKQK 1076
Cdd:pfam17380 552 RRIQEQMRKATEERSRLEA--------MEREREMMRQIVESEKAR 588
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
597-929 |
7.45e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQRE---------------------ELEKLESKRKQIEEMEEKQRSDKAELVRMQQEV----ESQRKETEIVQLQI 651
Cdd:PTZ00121 1078 DFDFDAKEdnradeateeafgkaeeakktETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 652 RKQEESlkrRSVHIESRLKDllAEKEKFEEERLREQQEIELQKKKQQEEI-FARVKEELQRLQELNHKEKAEKMQIFREL 730
Cdd:PTZ00121 1158 RKAEDA---RKAEEARKAED--AKKAEAARKAEEVRKAEELRKAEDARKAeAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 731 EKLKKeKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQL----------------REKQVMIQLLKRGDVQRVEEEKRDL 794
Cdd:PTZ00121 1233 EEAKK-DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaeearkadelkkaEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 795 EDIRESLLKVKEARSEGEENCEELEKAQHS--FIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEhv 872
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAkkAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE-- 1389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393536 873 nLKKDDEnfgdAVFKAEEfDMVKLTEYRLQSKVRQleylKNNHLPALLEEKQRATEV 929
Cdd:PTZ00121 1390 -KKKADE----AKKKAEE-DKKKADELKKAAAAKK----KADEAKKKAEEKKKADEA 1436
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
599-871 |
8.90e-06 |
|
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: 49.53 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQI--RKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:pfam13868 30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELnhKEKAEKMQIFRELeklkKEKDEQYIKLESEKKRI-EEQE 755
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE--EEREEDERILEYL----KEKAEREEEREAEREEIeEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 756 REQVMLVAHLEEQLREKQVMIQLLkrgdVQRVEEEKRDLEDIREsllkvKEARSEGEENCEELEKAQHSFIEFKKKQLEQ 835
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELR----AKLYQEEQERKERQKE-----REEAEKKARQRQELQQAREEQIELKERRLAE 254
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024393536 836 LTILEKDLVQQM-DHLEKDIAHEKETLEYLKLAEEEH 871
Cdd:pfam13868 255 EAEREEEEFERMlRKQAEDEEIEQEEAEKRRMKRLEH 291
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
607-1134 |
9.00e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 607 EKLESKRKQIEEMEEKQRSDKAELVRMQQEVES-QRKETEIVQLQIRKQEESLKRRS--VHIESRLKDLLAEKEKFeeer 683
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEKlKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL---- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 684 lreqqeiELQKKKQQEEIfARVKEELQRLQELNHKEKAEKMQIFRELEKLKKE---KDEQYIKLESEKKRIEEQEREQVM 760
Cdd:TIGR02169 440 -------EEEKEDKALEI-KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVRGGRA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 761 --------------LVAHLEEQLREKQVMIQLLKRGDVQR--VEEEKRDLEDI---------RESLLKVKEARSEGEENC 815
Cdd:TIGR02169 512 veevlkasiqgvhgTVAQLGSVGERYATAIEVAAGNRLNNvvVEDDAVAKEAIellkrrkagRATFLPLNKMRDERRDLS 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 816 EELEKAQHSF----IEFKKK----------------QLE---------QLTILEKDLVQQ----------MDHLEKDIAH 856
Cdd:TIGR02169 592 ILSEDGVIGFavdlVEFDPKyepafkyvfgdtlvveDIEaarrlmgkyRMVTLEGELFEKsgamtggsraPRGGILFSRS 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 857 EKETLEYLKLAEEEhvnLKKDDENFGDAVFKAEE-----FDMVKLTEYRLQSKVRQLEYLKNNH--LPALLEEKQRATEV 929
Cdd:TIGR02169 672 EPAELQRLRERLEG---LKRELSSLQSELRRIENrldelSQELSDASRKIGEIEKEIEQLEQEEekLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 930 LDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQL---------QQLQETFEFTANVARQEEKVRKKEKEILQSREkQQ 1000
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLT-LE 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1001 REALEQAVAKLERRHSALQ-RRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1079
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393536 1080 ----------SDGGQKGNHGMLEEKLSHSNSPTNPTKPQPPSAPLVDDrinafIEQEVQRRLQNI 1134
Cdd:TIGR02169 908 leaqiekkrkRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-----VQAELQRVEEEI 967
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
603-1079 |
9.01e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 603 REELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEE-----------------SLKRRSVHI 665
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterereelaeevrDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 666 ESRLKDLLAEKEKFEEERLREQQEIE-LQKKKqqEEIFARVKEELQRLQELNHKEKAEKMQIfRELEKLKKEKDEQYIKL 744
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREeLEDRD--EELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAEL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 745 ESEKKRIEEQEREQVMLVAHLEEQLREkqvmiqllKRGDVQRVEEEKRDLEDIRESLLKVKEARSegeenceelekaqhs 824
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEE--------LRERFGDAPVDLGNAEDFLEELREERDELR--------------- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 825 fiefkkkqlEQLTILEKDLvqqmDHLEKDIAHEKETLEYLK-------LAEEEHVNLKKDDEnfgDAVFK-AEEFDMVKL 896
Cdd:PRK02224 426 ---------EREAELEATL----RTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDR---ERVEElEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 897 TEYRLQSKVRQLEYLKN--NHLPALLEEKQRATEVLDrgllgldntlyQIEKEIEDKEEQLAQYRASTNQLQQLQETFEF 974
Cdd:PRK02224 490 EVEEVEERLERAEDLVEaeDRIERLEERREDLEELIA-----------ERRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 975 TANVARQEEKVRKKEKEILQSRekqqREALEQAVAKLERRHSALQRRSTIDFEIE---EQKQKLATLNNSCSEQ------ 1045
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIErlrEKREALAELNDERRERlaekre 634
|
490 500 510
....*....|....*....|....*....|....*..
gi 2024393536 1046 --AGLQASLEAEQ-KALEQDRERLDQEIQQLKQKIYE 1079
Cdd:PRK02224 635 rkRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDE 671
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
1220-1285 |
1.13e-05 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 49.80 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 1220 TVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNK-----DERVIAERRSHLETYLRSFFTAMLQSPSS 1285
Cdd:COG5391 174 VVRRRYSDFESLHSILIKLLPLCAIPPLPSKKSNSEYygdrfSDEFIEERRQSLQNFLRRVSTHPLLSNYK 244
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
471-551 |
1.54e-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: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 471 YHLKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENLNGTVNLIPL---NGAQcsVNGIQITEATHLNQGAVILLGRTn 547
Cdd:COG1716 16 FPLDGGPLTIGRAP---DNDIVLDDPTVSRRHARIRRDGGGWVLEDLgstNGTF--VNGQRVTEPAPLRDGDVIRLGKT- 89
|
....
gi 2024393536 548 MFRF 551
Cdd:COG1716 90 ELRF 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
998-1132 |
1.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 998 KQQREALEQAVAKLERRHSALQRRSTIDF----------EIEEQKQKLATLNNSCSEQAGLQ---ASLEAEQKALEQDRE 1064
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWdeidvasaerEIAELEAELERLDASSDDLAALEeqlEELEAELEELEEELD 709
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 1065 RLDQEIQQLKQKIYESDGGQKGNHGMLEEKlshsnsptnPTKPQPPSAPLVDDRINAFIEQEVQRRLQ 1132
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAA---------EDLARLELRALLEERFAAALGDAVERELR 768
|
|
| PX_SNX20 |
cd07300 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ... |
1223-1277 |
3.70e-05 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.
Pssm-ID: 132833 Cd Length: 114 Bit Score: 44.42 E-value: 3.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 1223 RRYSRFREMHRTLKLKY-PEVATLEFPPKKLFGNKDERVIAERRSHLETYLRSFFT 1277
Cdd:cd07300 40 RRYSDFLKLHQELLSDFsEELEDVVFPKKKLTGNFSEEIIAERRVALRDYLTLLYS 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
600-809 |
4.19e-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: 48.14 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKF 679
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 680 EEERLREQQEIELQKKKQQeEIFARVKEELQRLQELNHKekaekmqifreLEKLKKEKDEqyikLESEKKRIEEqEREQV 759
Cdd:TIGR02169 888 KKERDELEAQLRELERKIE-ELEAQIEKKRKRLSELKAK-----------LEALEEELSE----IEDPKGEDEE-IPEEE 950
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024393536 760 MLVAHLEEQLREKQVMIQLLkrGDV-----QRVEEEKRDLEDIRESLLKVKEARS 809
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERK 1003
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
993-1113 |
4.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 993 LQSREKQQREALEQAVAKLERRHSALQR-RSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQ 1071
Cdd:COG3883 127 IADADADLLEELKADKAELEAKKAELEAkLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2024393536 1072 QLKQKIYESDGGQKGNHGMLEEKLSHSNSPTNPTKPQPPSAP 1113
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-758 |
4.47e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESkrkqieEMEEKQRSDKAELVRMQQEVEsQRKEteivqlQIRKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:PRK12704 57 EALLEAKEEIHKLRN------EFEKELRERRNELQKLEKRLL-QKEE------NLDRKLELLEKREEELEKKEKELEQKQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEeerlreqqeielQKKKQQEEIFARVKEELQRLQELNhKEKAEKMQIFRELEKLKKEKDEQYiklesekKRIEEQER 756
Cdd:PRK12704 124 QELE------------KKEEELEELIEEQLQELERISGLT-AEEAKEILLEKVEEEARHEAAVLI-------KEIEEEAK 183
|
..
gi 2024393536 757 EQ 758
Cdd:PRK12704 184 EE 185
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
602-808 |
5.60e-05 |
|
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: 46.95 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 602 QREELEKLESKRKQIEEmEEKQRSDKAELVRMQQEVESQRKEteiVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKFEE 681
Cdd:pfam15558 33 AWEELRRRDQKRQETLE-RERRLLLQQSQEQWQAEKEQRKAR---LGREERRRADRREKQVIEKESRWREQAEDQENQRQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 682 ERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMl 761
Cdd:pfam15558 109 EKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLV- 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024393536 762 vahlEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEAR 808
Cdd:pfam15558 188 ----DCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQK 230
|
|
| PX_SNX16 |
cd07276 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ... |
1211-1274 |
6.12e-05 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.
Pssm-ID: 132809 Cd Length: 110 Bit Score: 43.55 E-value: 6.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 1211 KITVL---DETWTVFRRYSRFREMHRTLKLKYPEVaTLEFPPKKLFG-NKDERVIAERRSHLETYLRS 1274
Cdd:cd07276 24 KIRVEnkvGDSWFVFRRYTDFVRLNDKLKQMFPGF-RLSLPPKRWFKdNFDPDFLEERQLGLQAFVNN 90
|
|
| PX_SNX27 |
cd06886 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ... |
1185-1277 |
6.21e-05 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.
Pssm-ID: 132796 Cd Length: 106 Bit Score: 43.55 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1185 KDPIKISIPRYvlcgqgkdEHYEFEikitvlDETWTVF-----------RRYSRFREMHRTLKLKYPEVATLEFPPKKLF 1253
Cdd:cd06886 1 KRSVPISIPDY--------KHVEQN------GEKFVVYniymagrqlcsRRYREFANLHQNLKKEFPDFQFPKLPGKWPF 66
|
90 100
....*....|....*....|....
gi 2024393536 1254 GNKDERVIAeRRSHLETYLRSFFT 1277
Cdd:cd06886 67 SLSEQQLDA-RRRGLEQYLEKVCS 89
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
584-755 |
7.74e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 584 ENLSAVMLyNPGLEFERQQREELEKLESKRKQieEMEEKQRSDKAELVRMQQEVESQR-KETEIVQLQIRKQEESlkrrs 662
Cdd:PRK09510 48 SVIDAVMV-DPGAVVEQYNRQQQQQKSAKRAE--EQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQ----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 663 vHIESRLKDLLAEKEKfeeerlreqqeiELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMqifreleklKKEKDEQYI 742
Cdd:PRK09510 120 -AEEAAKQAALKQKQA------------EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK---------KKAEAEAAK 177
|
170
....*....|...
gi 2024393536 743 KLESEKKRIEEQE 755
Cdd:PRK09510 178 KAAAEAKKKAEAE 190
|
|
| PX_p40phox |
cd06882 |
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ... |
1200-1274 |
8.62e-05 |
|
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.
Pssm-ID: 132792 Cd Length: 123 Bit Score: 43.58 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1200 QGKDEHYEFEIKITVLD-ETWTVFRRYSRFREMHRTLKLKYPEVA-------TL-EFPPKKLFGNKDErvIAERR-SHLE 1269
Cdd:cd06882 15 RGFTNYYVFVIEVKTKGgSKYLIYRRYRQFFALQSKLEERFGPEAgssaydcTLpTLPGKIYVGRKAE--IAERRiPLLN 92
|
....*
gi 2024393536 1270 TYLRS 1274
Cdd:cd06882 93 RYMKE 97
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
600-772 |
9.99e-05 |
|
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: 45.30 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRrsvhIESRLKDLLAEKEKF 679
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 680 EEERLREQQE---------IELQKKKQQ--EEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEK 748
Cdd:COG1579 79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|....
gi 2024393536 749 KRIEEQEREqvmLVAHLEEQLREK 772
Cdd:COG1579 159 EELEAEREE---LAAKIPPELLAL 179
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
747-1077 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 747 EKKRIEEQEREQVmlvahlEEQLREKQVMIQLlKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFI 826
Cdd:TIGR02169 170 RKKEKALEELEEV------EENIERLDLIIDE-KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 827 EF----KKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEylKLAEEEHVNLKKDDENfgdavfkaeefdmvklteyrLQ 902
Cdd:TIGR02169 243 ERqlasLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGE--------------------LE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 903 SKVRQLEylknnhlpALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQE 982
Cdd:TIGR02169 301 AEIASLE--------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 983 EKVRKKEKEILQSREKQQREALEqavaKLERRHSALQR-RSTIDFEIEEQKQKLATLNNSCseqaglqASLEAEQKALEQ 1061
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLE----KLKREINELKReLDRLQEELQRLSEELADLNAAI-------AGIEAKINELEE 441
|
330
....*....|....*.
gi 2024393536 1062 DRERLDQEIQQLKQKI 1077
Cdd:TIGR02169 442 EKEDKALEIKKQEWKL 457
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
600-805 |
1.53e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 600 RQQREELEKLESKRKQIEEMEEKQRsdkaELVRMQQ-EVESQRKETEIVQlQIRKQEESLKRRSVHIESR--LKDLLAEK 676
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLRKEIE----RLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAKKALEKNekLKELRAEL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EkfeeerlreqqeielQKKKQQEEIFARVKEELQRLQELnhkeKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:COG1340 170 K---------------ELRKEAEEIHKKIKELAEEAQEL----HEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024393536 757 EQVMLVAHLEEqlREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVK 805
Cdd:COG1340 231 EIIELQKELRE--LRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-1003 |
1.55e-04 |
|
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: 46.50 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 354 RAKNIINKPTINEDPNVKLIRELRAEIARLKALLAQGNQIALLDSPTALSMEEKLQQNEARVQELTKEWT--NKWNETQN 431
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEqlELLLSRQK 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 432 ILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHC--IFENLN 509
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvrALTELP 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 510 GTVNLIPLNGAQCSVNGIQITEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAV 589
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 590 M-------LYNPGLEFERQQREELEKLESKRKQIEEMEEK-QRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRR 661
Cdd:pfam02463 655 EeglaeksEVKASLSELTKELLEIQELQEKAESELAKEEIlRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 662 SVHIESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQY 741
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 742 IKLESEKKRIEEQEREQvmlvahlEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKA 821
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIK-------EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 822 QHSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENfgdavfkaeefdmvklteyrl 901
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAD--------------------- 946
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 902 qskvrqLEYLKNNHLPALLEEKQRATEVLDrgLLGLDNtlyqiekeiedkeeqlaqyrastnqlqqLQETFEFTANVARQ 981
Cdd:pfam02463 947 ------EKEKEENNKEEEEERNKRLLLAKE--ELGKVN----------------------------LMAIEEFEEKEERY 990
|
650 660
....*....|....*....|..
gi 2024393536 982 EEKVRKKEKEILQSREKQQREA 1003
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAII 1012
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
601-851 |
1.86e-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: 46.12 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 601 QQREELEKLESKRKQIEEMEEKQRsDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSV-HIESRLKDLLAEKEKF 679
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVR-EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLaQCQTLLRELETHIEEY 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 680 EEERLREQQEIELQKKK--QQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQERE 757
Cdd:TIGR00618 717 DREFNEIENASSSLGSDlaAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 758 QVMLVAHLEEQLREK-QVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSegeenceelekaQHSFIEFKKKQLEQL 836
Cdd:TIGR00618 797 DTHLLKTLEAEIGQEiPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH------------QLLKYEECSKQLAQL 864
|
250
....*....|....*
gi 2024393536 837 TILEKDLVQQMDHLE 851
Cdd:TIGR00618 865 TQEQAKIIQLSDKLN 879
|
|
| PX_FISH |
cd06888 |
The phosphoinositide binding Phox Homology domain of Five SH protein; The PX domain is a ... |
1205-1265 |
2.00e-04 |
|
The phosphoinositide binding Phox Homology domain of Five SH protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Five SH (FISH), also called Tks5, is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. FISH contains an N-terminal PX domain and five Src homology 3 (SH3) domains. FISH binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. This subfamily also includes proteins with a different number of SH3 domains than FISH, such as Tks4, which contains four SH3 domains instead of five. The Tks4 adaptor protein is required for the formation of functional podosomes. It has overlapping, but not identical, functions as FISH. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.
Pssm-ID: 132798 Cd Length: 119 Bit Score: 42.41 E-value: 2.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 1205 HYEFEIKITVLDET-WTVFRRYSRFREMHRTLKLKYPEVA--------TLEF-PPKKLFGNKDERVIAERR 1265
Cdd:cd06888 18 HYVYIINVTWSDGSsNVIYRRYSKFFDLQMQLLDKFPIEGgqkdpsqrIIPFlPGKILFRRSHIRDVAVKR 88
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
599-862 |
2.09e-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: 45.29 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 678
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 679 FEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELnhkekaEKMQIFRELEKLKKEKDEQyiklesEKKRIEEQEREQ 758
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER------DELRAKLYQEEQERKERQK------EREEAEKKARQR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 759 VMLVAHLEEQLREKQVMIQLLKRgdvQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTI 838
Cdd:pfam13868 235 QELQQAREEQIELKERRLAEEAE---REEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAERE 311
|
250 260
....*....|....*....|....
gi 2024393536 839 LEkdlVQQMDHLEKDIAHEKETLE 862
Cdd:pfam13868 312 EE---LEEGERLREEEAERRERIE 332
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
854-1079 |
2.11e-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: 45.88 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 854 IAHEKE-TLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQ-LEYLKNNHLpaLLEEKQRATEvld 931
Cdd:pfam17380 342 MAMERErELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKVKI--LEEERQRKIQ--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 932 rgllgldntlyqiEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEIL-QSREKQQREALEQAVAK 1010
Cdd:pfam17380 417 -------------QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1011 LERRHSALQRRSTIDFEIEEQKQKLATLNNscsEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1079
Cdd:pfam17380 484 RDRKRAEEQRRKILEKELEERKQAMIEEER---KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| PX_SNX1_2_like |
cd06859 |
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ... |
1220-1273 |
2.28e-04 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.
Pssm-ID: 132769 [Multi-domain] Cd Length: 114 Bit Score: 42.18 E-value: 2.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 1220 TVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERV--IAERRSHLETYLR 1273
Cdd:cd06859 38 SVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKVKFefIEKRRAALERFLR 93
|
|
| PX_UP2_fungi |
cd06869 |
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ... |
1205-1274 |
2.36e-04 |
|
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.
Pssm-ID: 132779 Cd Length: 119 Bit Score: 42.27 E-value: 2.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 1205 HYEFEIKITVLDETWT---VFRRYSRFREMHRTLKLKYP--EVATLefPPKklfgNKDERviaER-RSHLETYLRS 1274
Cdd:cd06869 33 HYEFIIRVRREGEEYRtiyVARRYSDFKKLHHDLKKEFPgkKLPKL--PHK----DKLPR---EKlRLSLRQYLRS 99
|
|
| PX_Vps5p |
cd06861 |
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ... |
1217-1273 |
2.56e-04 |
|
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1.
Pssm-ID: 132771 Cd Length: 112 Bit Score: 41.95 E-value: 2.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393536 1217 ETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSHLETYLR 1273
Cdd:cd06861 35 SSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRFDDNFVEQRRAALEKMLR 91
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
471-555 |
2.57e-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: 41.48 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 471 YHLKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENLNGTVNLIPLN-GAQCSVNGIQITEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87
|
....*..
gi 2024393536 549 FRFNHPK 555
Cdd:pfam16697 88 FCLVPAD 94
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
677-926 |
3.18e-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: 45.11 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEErlreqqeielqKKKQQEEIFARvkeELQRLQELNHKEKAEKMQIFRElEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:pfam17380 294 EKMEQE-----------RLRQEKEEKAR---EVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 757 EQVMlvahleEQLREKQVMIQLLKRGDVQRVE-EEKRDLEDIRESLlkvKEARSEGEENCEELEKAQHSFIEFKKKQLEQ 835
Cdd:pfam17380 359 KREL------ERIRQEEIAMEISRMRELERLQmERQQKNERVRQEL---EAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 836 -------LTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMvKLTEYRLQSKVRQL 908
Cdd:pfam17380 430 eearqreVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRR-KILEKELEERKQAM 508
|
250 260
....*....|....*....|
gi 2024393536 909 --EYLKNNHLPALLEEKQRA 926
Cdd:pfam17380 509 ieEERKRKLLEKEMEERQKA 528
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
597-909 |
3.39e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQ------QREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESL--------KRRS 662
Cdd:pfam15921 445 QMERQmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIeatnaeitKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 663 vHIESRLKDL--LAEKEKFEEERLREQQEIELQKKkQQEEIFARVKEELQRLQEL--NHKEKAEKMQIFR---------- 728
Cdd:pfam15921 525 -RVDLKLQELqhLKNEGDHLRNVQTECEALKLQMA-EKDKVIEILRQQIENMTQLvgQHGRTAGAMQVEKaqlekeindr 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 729 --ELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLRE----KQVMIQLLK-----RGDVQRVEEekrDLEDI 797
Cdd:pfam15921 603 rlELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNELNSLSE---DYEVL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 798 RESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYL----KLAEEEHVN 873
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALqskiQFLEEAMTN 759
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 874 LKKDDENFGDAVFK---------------AEEFDMVKLTEYRLQSKVRQLE 909
Cdd:pfam15921 760 ANKEKHFLKEEKNKlsqelstvateknkmAGELEVLRSQERRLKEKVANME 810
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
697-793 |
3.75e-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: 43.27 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 697 QQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQEREqvmlvahLEEQLREKQVMI 776
Cdd:pfam06785 80 LDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLE-------SEEQLAEKQLLI 152
|
90
....*....|....*...
gi 2024393536 777 QLLKRGDV-QRVEEEKRD 793
Cdd:pfam06785 153 NEYQQTIEeQRSVLEKRQ 170
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
604-836 |
3.90e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 604 EELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQE---------ESLKRRSVHIESRLKDLLA 674
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGgldeeeaflDRTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 675 EKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ 754
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 755 EREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDL--------EDIRESLLKVKEARSEGEENCEELEKAQHSFI 826
Cdd:pfam02029 165 EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHpevksqngEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL 244
|
250
....*....|
gi 2024393536 827 EFKKKqLEQL 836
Cdd:pfam02029 245 EAEQK-LEEL 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
599-909 |
4.93e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEk 678
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 679 feeerlreqqeielQKKKQQEEIfARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEE----- 753
Cdd:COG4372 109 --------------EAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAleqel 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 754 QEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQL 833
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024393536 834 EQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEYRLQSKVRQLE 909
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
604-807 |
5.14e-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: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 604 EELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKFEEER 683
Cdd:pfam15709 326 EKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 684 LREQQEIELQ----KKKQQEEIFARVKEELQRLQELNHKEKAEkmqifrELEKLKKEKDEQyikLESEKKRIEEQEREQV 759
Cdd:pfam15709 406 EERKQRLQLQaaqeRARQQQEEFRRKLQELQRKKQQEEAERAE------AEKQRQKELEMQ---LAEEQKRLMEMAEEER 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024393536 760 MlvahleEQLREKQvmiqllkrgdvqrvEEEKRDLEDIRESLLKVKEA 807
Cdd:pfam15709 477 L------EYQRQKQ--------------EAEEKARLEAEERRQKEEEA 504
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
602-1073 |
5.23e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 602 QREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRK-----ETEIVQLQIRKQEESLKRRSVHiesRLKDLLAEK 676
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREivksyENELDPLKNRLKEIEHNLSKIM---KLDNEIKAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIELQKkkqqEEIFARVKEELQRLQELNHKEKAEK----MQIFRELEKLKKEKDEqyikLESEKKRIE 752
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKM----EKVFQGTDEQLNDLYHNHQRTVREKerelVDCQRELEKLNKERRL----LNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 753 -EQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKK 831
Cdd:TIGR00606 347 vEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 832 QLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEfDMVKLTEYRL-QSKVRQLEY 910
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAER-ELSKAEKNSLtETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 911 LKNNHLPalleekqratevLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETfEFTANVARQEEKVRKKEK 990
Cdd:TIGR00606 506 LQNEKAD------------LDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI-KSRHSDELTSLLGYFPNK 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 991 EILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEI 1070
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSS 652
|
...
gi 2024393536 1071 QQL 1073
Cdd:TIGR00606 653 KQR 655
|
|
| PX_SNX17_31 |
cd06885 |
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ... |
1224-1284 |
5.28e-04 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.
Pssm-ID: 132795 Cd Length: 104 Bit Score: 40.78 E-value: 5.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 1224 RYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERvIAERRSHLETYLRsfftAMLQSPS 1284
Cdd:cd06885 34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQ-LEERRLQLEKYLQ----AVVQDPR 89
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
597-1077 |
5.68e-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: 44.57 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKaELVRMQQEVESQRKETEIVQLQIRKQEESLK-----RRSVHIESRLKD 671
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLK-QLRARIEELRAQEAVLEETQERINRARKAAPlaahiKAVTQIEQQAQR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 672 LLAE-KEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEkAEKMQIFRElEKLKKEKDEQYIKLESEKKR 750
Cdd:TIGR00618 312 IHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-HEVATSIRE-ISCQQHTLTQHIHTLQQQKT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 751 IEEQereQVMLVAHLEEQLREkqvmiqllkrgdvqrvEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKK 830
Cdd:TIGR00618 390 TLTQ---KLQSLCKELDILQR----------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 831 KQLEQLTILEKDLVQQMDHLEKDIAHEKETLeYLKLAEEEHVNLKKDDEnfgdavfKAEEFDMVKLTEYRLQSKVRQLEY 910
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQI-HLQETRKKAVVLARLLE-------LQEEPCPLCGSCIHPNPARQDIDN 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 911 LKNNHLPALLEEKQRATevLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEK 990
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQ--LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 991 EILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATL-----NNSCSEQAGLQASLEAEQKALEQDRER 1065
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALhalqlTLTQERVREHALSIRVLPKELLASRQL 680
|
490
....*....|..
gi 2024393536 1066 LDQEIQQLKQKI 1077
Cdd:TIGR00618 681 ALQKMQSEKEQL 692
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
703-1077 |
5.98e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 703 ARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEqyikLESEKKRIEEQereqvmlVAHLEEQLREKqvmiqllkRG 782
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQ----WERQRRELESR-------VAELKEELRQS--------RE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 783 DVQRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIE-FKKKQLEQLTILE--KDLVQQMDHLEKDIAHEKE 859
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKtLTQRVLERETELErmKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 860 TLEY-LKLAEEEHVNLKKD--------DENFGDAVFKAEEFDMVKLTEYRLQSKVRQLEYLKNN--HLPALLEEKQRATE 928
Cdd:pfam07888 175 QLQAkLQQTEEELRSLSKEfqelrnslAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrSLQERLNASERKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 929 VLDRGLLGLDNTLYQIEKEIEDKEEQLAQyraSTNQLQQLQETF-EFTANVARQEEKvrkkekeILQSREKQqREALEQA 1007
Cdd:pfam07888 255 GLGEELSSMAAQRDRTQAELHQARLQAAQ---LTLQLADASLALrEGRARWAQERET-------LQQSAEAD-KDRIEKL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 1008 VAKLERRHSALQ--RRSTIDFEIE---EQKQKLATLNNSCSEQAGLQASLEAEQKALEQ---DRERLDQEIQQLKQKI 1077
Cdd:pfam07888 324 SAELQRLEERLQeeRMEREKLEVElgrEKDCNRVQLSESRRELQELKASLRVAQKEKEQlqaEKQELLEYIRQLEQRL 401
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
632-758 |
6.76e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 632 RMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKfeeerlreqqeiELQKKKQQEEifarvKEELQR 711
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLA------------AQEQKKQAEE-----AAKQAA 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2024393536 712 LQELNHKEKAEKmqifrELEKLKKEKDEQYIKLESEKKRIEEQEREQ 758
Cdd:PRK09510 129 LKQKQAEEAAAK-----AAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
597-753 |
6.97e-04 |
|
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: 41.56 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEME---EKQRSDKAELVRMQQEVESQRKETEivqlqiRKQEESLKRRSVhIESRLKDLL 673
Cdd:pfam05672 18 EKRRQAREQREREEQERLEKEEEErlrKEELRRRAEEERARREEEARRLEEE------RRREEEERQRKA-EEEAEEREQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 674 AEKEKfeeerlreqqEIELQKKKQQEEIFARvkeelqrlqelnhkEKAEKMQIFRELEKLKKEKDEQyikleSEKKRIEE 753
Cdd:pfam05672 91 REQEE----------QERLQKQKEEAEAKAR--------------EEAERQRQEREKIMQQEEQERL-----ERKKRIEE 141
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
452-554 |
7.39e-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: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDAMTEQDIVLHGLDLESEHCIFENLNGT-------VNLIPLNGAQCSV 524
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 2024393536 525 NGIQITEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| PX_UP1_plant |
cd06879 |
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ... |
1203-1287 |
8.50e-04 |
|
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.
Pssm-ID: 132789 Cd Length: 138 Bit Score: 41.16 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1203 DEHYEFEIKITVLDETWT---VFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGNKDERVIAERRSHLETYLRSFFTAM 1279
Cdd:cd06879 44 DKFYRVQVGVQSPEGITTmrgVLRRFNDFLKLHTDLKKLFPKKKLPAAPPKGLLRMKNRALLEERRHSLEEWMGKLLSDI 123
|
....*...
gi 2024393536 1280 LQSPSSPL 1287
Cdd:cd06879 124 DLSRSVPV 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
917-1079 |
8.70e-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: 43.21 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 917 PALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSR 996
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 997 EKQQREALEQAVAKLER--RHSALQ-------------RRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQ 1061
Cdd:COG4942 99 LEAQKEELAELLRALYRlgRQPPLAlllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170
....*....|....*...
gi 2024393536 1062 DRERLDQEIQQLKQKIYE 1079
Cdd:COG4942 179 LLAELEEERAALEALKAE 196
|
|
| PX_PI3K_C2_alpha |
cd07289 |
The phosphoinositide binding Phox Homology Domain of the Alpha Isoform of Class II ... |
1203-1278 |
9.12e-04 |
|
The phosphoinositide binding Phox Homology Domain of the Alpha Isoform of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. The class II alpha isoform, PI3K-C2alpha, plays key roles in clathrin assembly and clathrin-mediated membrane trafficking, insulin signaling, vascular smooth muscle contraction, and the priming of neurosecretory granule exocytosis. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.
Pssm-ID: 132822 Cd Length: 109 Bit Score: 40.30 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1203 DEHYEFEIKITV--LDETWTVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFGN---KDerVIAERRSHLETYLRSFFT 1277
Cdd:cd07289 14 DKHYIYVVRILRegQIEPSFVFRTFDEFQELHNKLSILFPLWKLPGFPNKMVLGRthiKD--VAAKRKVELNSYIQSLMN 91
|
.
gi 2024393536 1278 A 1278
Cdd:cd07289 92 S 92
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
743-1077 |
9.84e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 743 KLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRgdvqRVEEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQ 822
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK----ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 823 HSFIEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEfdmvklteyRLQ 902
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE---------RLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 903 SKVRQLEYLKNnHLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEFTANVARQE 982
Cdd:TIGR02168 828 SLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 983 -EKVRKkekeilqsrEKQQREALEQAVAKLERRhsalqrrstidfeIEEQKQKLATLNNSCSEQAGLQAS-LEAEQKALE 1060
Cdd:TIGR02168 907 eSKRSE---------LRRELEELREKLAQLELR-------------LEGLEVRIDNLQERLSEEYSLTLEeAEALENKIE 964
|
330
....*....|....*..
gi 2024393536 1061 QDRERLDQEIQQLKQKI 1077
Cdd:TIGR02168 965 DDEEEARRRLKRLENKI 981
|
|
| PX_SNX14 |
cd06877 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ... |
1189-1273 |
1.04e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.
Pssm-ID: 132787 Cd Length: 119 Bit Score: 40.44 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1189 KISIPRY--VLCGQGKDEHYEFEIKI--------TVLDETWTVFRRY-------SRFREMHRTLklkypEVATLefPPKK 1251
Cdd:cd06877 4 RVSIPYVemRRDPSNGERIYVFCIEVerndrrakGHEPQHWSVLRRYnefyvleSKLTEFHGEF-----PDAPL--PSRR 76
|
90 100
....*....|....*....|..
gi 2024393536 1252 LFGNKDERVIAERRSHLETYLR 1273
Cdd:cd06877 77 IFGPKSYEFLESKREIFEEFLQ 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
955-1077 |
1.08e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 955 LAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQK 1034
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024393536 1035 LATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKI 1077
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
|
| PX_HS1BP3 |
cd06868 |
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ... |
1220-1273 |
1.13e-03 |
|
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.
Pssm-ID: 132778 Cd Length: 120 Bit Score: 40.09 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2024393536 1220 TVFRRYSRFREMHRTLKLKYPEVATLEFPPKKLFgnKDERVIAERRSHLETYLR 1273
Cdd:cd06868 48 MVSKKYSEFEELYKKLSEKYPGTILPPLPRKALF--VSESDIRERRAAFNDFMR 99
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
597-799 |
1.25e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIR----KQEESLkrrsvhiESRLKDL 672
Cdd:pfam03528 97 EVKSQWQEEVASLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRRlsegQEEENL-------EDEMKKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 673 LAEKEKFEEERLREQQEIELQKKKQQEEIfARVKE-ELQRLQELNHKEKAEK---------MQIFRELEKLKKEKDEQYI 742
Cdd:pfam03528 170 QEDAEKLRSVVMPMEKEIAALKAKLTEAE-DKIKElEASKMKELNHYLEAEKscrtdlemyVAVLNTQKSVLQEDAEKLR 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024393536 743 KLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVE-----EEKRDLEDIRE 799
Cdd:pfam03528 249 KELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEsvltsEQLRQVEEIKK 310
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
599-773 |
1.40e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEE--SLKRRSVHIESR------LK 670
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESkvFLDQKRGHPEVKsqngeeEV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 671 DLLAEKEKFEEERLREQQEIELQKKKQQEEifARVKEELQRLQELNHKEKAEKMQIFR-----ELEKLKKEKDEQYIKLE 745
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSQEREEEAEVFLEA--EQKLEELRRRRQEKESEEFEKLRQKQqeaelELEELKKKREERRKLLE 294
|
170 180
....*....|....*....|....*...
gi 2024393536 746 SEKKRIEEQEREQvmLVAHLEEQLREKQ 773
Cdd:pfam02029 295 EEEQRRKQEEAER--KLREEEEKRRMKE 320
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
833-1077 |
1.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 833 LEQLTILEKDLVQQMDHLEKdiahEKET-LEYLKLAEEehvnlkkddenfgdavfkaeefdmvkLTEYRLQSKVRQLEYL 911
Cdd:COG1196 188 LERLEDILGELERQLEPLER----QAEKaERYRELKEE--------------------------LKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 912 KnnhlpallEEKQRATEVLDRgllgLDNTLYQIEKEIEDKEEQLAQYRAstnQLQQLQETFEFTANVARQEEKVRKKEKE 991
Cdd:COG1196 238 E--------AELEELEAELEE----LEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 992 ILQSREKQQREALEQAVAKLERRHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQ 1071
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
....*.
gi 2024393536 1072 QLKQKI 1077
Cdd:COG1196 383 ELAEEL 388
|
|
| PX_Bem1p |
cd06890 |
The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a ... |
1188-1276 |
1.56e-03 |
|
The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of Bem1p specifically binds phosphatidylinositol-4-phosphate (PI4P).
Pssm-ID: 132800 Cd Length: 112 Bit Score: 39.58 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1188 IKISIPRYVLcgqgKDEHYEFEIKITVLD-ETWTVFRRYSRFREMHRTLKLKYPEVA-------TLEFPPKKLFGNKDER 1259
Cdd:cd06890 1 VSASVESVLL----EDNRYWYRVRATLSDgKTRYLCRYYQDFYKLHIALLDLFPAEAgrnsskrILPYLPGPVTDVVNDS 76
|
90
....*....|....*..
gi 2024393536 1260 VIAERRSHLETYLRSFF 1276
Cdd:cd06890 77 ISLKRLNDLNEYLNELI 93
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
599-779 |
1.59e-03 |
|
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: 42.33 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKL----------ESKRKQIEEMEEKQRSDKAELVRMQQEvesQRKETEIVQLQIRKQEESLKRRSVHIESR 668
Cdd:pfam15558 72 ARLGREERRRAdrrekqviekESRWREQAEDQENQRQEKLERARQEAE---QRKQCQEQRLKEKEEELQALREQNSLQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 669 LKDLLAEKEKfeeerlrEQQEIELQKKKQQEEIFARVKEELqRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLES-- 746
Cdd:pfam15558 149 ERLEEACHKR-------QLKEREEQKKVQENNLSELLNHQA-RKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEer 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024393536 747 -----EKKRIEEQEREQVMLVAhlEEQLREKQVMIQLL 779
Cdd:pfam15558 221 hrelrEKAQKEEEQFQRAKWRA--EEKEEERQEHKEAL 256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
640-808 |
1.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 640 QRKETEIVQlqIRKQEESLKRRSVHIESRLKDLLAEKEKfeeerlreqqeIELQKKKQQEEIfARVKEELQRLQELNHKE 719
Cdd:COG1579 13 QELDSELDR--LEHRLKELPAELAELEDELAALEARLEA-----------AKTELEDLEKEI-KRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 720 KAEKMQIF--RELEKLKKEKDeqyiKLESEKKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEDI 797
Cdd:COG1579 79 EEQLGNVRnnKEYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|.
gi 2024393536 798 RESLLKVKEAR 808
Cdd:COG1579 155 EAELEELEAER 165
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
592-1085 |
1.75e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 592 YNPGLEFERQQREEL--------EKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQ---LQIRKQEESLKR 660
Cdd:TIGR02168 321 LEAQLEELESKLDELaeelaeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 661 RSVHIESRLKDLLAEKEKFEEERLREQQEIELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQ 740
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 741 YIKLESEKKRIEEQEReqvMLVAHLEEQLREKQVM--------------------------------------------- 775
Cdd:TIGR02168 481 ERELAQLQARLDSLER---LQENLEGFSEGVKALLknqsglsgilgvlselisvdegyeaaieaalggrlqavvvenlna 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 776 ----IQLLKRGDVQRV-------EEEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSF----------------IEF 828
Cdd:TIGR02168 558 akkaIAFLKQNELGRVtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnaLEL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 829 KKKQLEQLTI--LEKDLV---------------------QQMDHLEKDIAHEKETLEYLKLAEEEhvnLKKDDENFGDAV 885
Cdd:TIGR02168 638 AKKLRPGYRIvtLDGDLVrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEEL 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 886 FKAEEfdmvklteyRLQSKVRQLEYLKNNhLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQL 965
Cdd:TIGR02168 715 EQLRK---------ELEELSRQISALRKD-LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 966 QQLQEtfefTANVARQEEKVRKKEKEILQSREKQQREA---LEQAVAKLERRHSALQRRST-IDFEIEEQKQKLATLNNS 1041
Cdd:TIGR02168 785 EELEA----QIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAAE 860
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2024393536 1042 CSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYESDGGQK 1085
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
|
| wall_bind_EntB |
NF040676 |
cell wall-binding protein EntB; This HMM describes the cell wall-binding protein EntB, as ... |
607-822 |
2.21e-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: 42.08 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 607 EKLESKRKQIEEMeekQRSDKAELVRMQQEVeSQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEKfeeerlre 686
Cdd:NF040676 149 KKADEKTKQVAKV---QKSVKAKEEAKTQKV-AKAKETTKAQEIVKPKEEVKVQEVVKPKEEPKVQEIVKPK-------- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 687 qqeielQKKKQQEEifARVKEElQRLQELNHKEKAEKMQifrELEKLKKEKDEQYIKLESEKKRIE------EQEREQVM 760
Cdd:NF040676 217 ------EEVKVQEE--VKPKEE-EKVQEIVKPKEEAKVQ---EEVKVKEEAKVQEIAKAKEEAKAQeiakakEEAKAQEI 284
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024393536 761 LVAHLEEQLREKQVMIQLLKRGDVQRVEEEKRDLEdiresLLKVK-EARSEGEENCEELEKAQ 822
Cdd:NF040676 285 AKAKEEAKAQEIAKAKEEEKAQEIAKAKEEAKARE-----IAKAKeEEKAREIAKAKEEAKAR 342
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
596-803 |
2.32e-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: 41.83 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 596 LEFERQQREELEKLESKRKQIEEMEEKQRsdkAELVRMQQEVESQRKETEivQLQIRKQEESLKRrsvhiesrlKDLLAE 675
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREI---ARLRAQQEKAQDEKAERD--ELRAKLYQEEQER---------KERQKE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 676 KEKfeeerlreqqeiELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQE 755
Cdd:pfam13868 224 REE------------AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024393536 756 REQV--MLVAHLEEQLREKQVMIQLLKRGDvQRVEEEKRDLEDIRESLLK 803
Cdd:pfam13868 292 RRELekQIEEREEQRAAEREEELEEGERLR-EEEAERRERIEEERQKKLK 340
|
|
| PX_SNX21 |
cd07301 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ... |
1223-1272 |
2.33e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.
Pssm-ID: 132834 Cd Length: 112 Bit Score: 39.02 E-value: 2.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2024393536 1223 RRYSRFREMHRTLKLKYP-EVATLEFPPKKLFGNKDERVIAERRSHLETYL 1272
Cdd:cd07301 40 RRYSDFERLHRRLRRLFGgEMAGVSFPRKRLRKNFTAETIAKRSRAFEQFL 90
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
696-1076 |
2.87e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 696 KQQEEIFARvKEELQRLQELNHKekaekmqifreLEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEqLRekqvm 775
Cdd:pfam01576 2 RQEEEMQAK-EEELQKVKERQQK-----------AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEE-MR----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 776 iqllkrgdvQRVEEEKRDLEDI---RESLLKVKEARSEGEENCeelekaqhsfiefKKKQLEQLTILEKDLVQQMDHLEK 852
Cdd:pfam01576 64 ---------ARLAARKQELEEIlheLESRLEEEEERSQQLQNE-------------KKKMQQHIQDLEEQLDEEEAARQK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 853 dIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVFKAEEFDMVKLTEY--RLQSKVRQLEYLKNNH--LPALLEEKQRATE 928
Cdd:pfam01576 122 -LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNlaEEEEKAKSLSKLKNKHeaMISDLEERLKKEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 929 V----LDRGLLGLDNTLYQIEKEIEDKEEQLAQYRAstnQLQQLQEtfEFTANVARQEEKVRKKEKEILQSREKQQREAL 1004
Cdd:pfam01576 201 KgrqeLEKAKRKLEGESTDLQEQIAELQAQIAELRA---QLAKKEE--ELQAALARLEEETAQKNNALKKIRELEAQISE 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 1005 EQAVAKLER--RHSALQRRSTIDFEIEEQKQKLATLNNSCSEQAGLQASLEAE----QKALEQDRERLDQEIQQLKQK 1076
Cdd:pfam01576 276 LQEDLESERaaRNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEvtelKKALEEETRSHEAQLQEMRQK 353
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
599-1079 |
2.97e-03 |
|
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: 41.98 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEKEK 678
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 679 FEEERLREQQEIELQKKK--QQEEIFARVKEELQRLQELNH--KEKAEKM-QIFRELEKLKKEK---DEQYIKLESEKKR 750
Cdd:TIGR02169 401 INELKRELDRLQEELQRLseELADLNAAIAGIEAKINELEEekEDKALEIkKQEWKLEQLAADLskyEQELYDLKEEYDR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 751 IEEQEREQVMLVAHLEEQLREKQ------VMIQLLKRGDVQRVEEEKRDLEDIRESLLKVKE----ARSEGEENCEELEK 820
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEervrggRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagNRLNNVVVEDDAVA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 821 AQHsfIEF-KKKQLEQLTILEKDLVQQMdHLEKDIAHEKETLEYLklaeeehVNLKKDDENFGDAVFKA-------EEFD 892
Cdd:TIGR02169 561 KEA--IELlKRRKAGRATFLPLNKMRDE-RRDLSILSEDGVIGFA-------VDLVEFDPKYEPAFKYVfgdtlvvEDIE 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 893 MVK--LTEYRL----------------QSKVRQLEYLKNNHLPALLEEKQRATEVLDRGLLGLDNTLYQIEKEIEDKEEQ 954
Cdd:TIGR02169 631 AARrlMGKYRMvtlegelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 955 LAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQR---------RSTID 1025
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKleealndleARLSH 790
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2024393536 1026 FEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQKIYE 1079
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
999-1077 |
3.18e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 999 QQREALEQAVAKLERRHSALQR----------RSTIDFEIEEQKQKLAtlnnscSEQAGLQASLEAEQKALEQDRERLDQ 1068
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRaerllaefckRLGKNLDDEDELEQLQ------EELEARLESLSESVSEARERRMALRQ 586
|
....*....
gi 2024393536 1069 EIQQLKQKI 1077
Cdd:PRK04863 587 QLEQLQARI 595
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
604-1065 |
3.71e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 604 EELEKLESKRKQIEEMEEKQRSDKAELVRMQqevesqrKETEIVQLQIRKQEESLKRRsvhiesrlKDLLAEKEKFEEER 683
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLT-------LRSQLLTLCTPCMPDTYHER--------KQVLEKELKHLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 684 LREQQEIELQKKKQQEEIFARVKEElQRLQELNHKEKAEKMQIfRELEKLKKEKDE--QYIKLESEKKRIEEQEREQVML 761
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEELRAQE-AVLEETQERINRarKAAPLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 762 VAHLEEQLREKQVMIQLLKRGDVQRVE-EEKRDLEDIRESLLKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTIL- 839
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLt 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 840 --------------------------EKDLVQQMDHLEKDIAHEKETLEYLKLAEEEHVNLKKDDENFGDAVF---KAEE 890
Cdd:TIGR00618 393 qklqslckeldilqreqatidtrtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAqslKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 891 FDMVKLTEYRLQ----SKVRQLEYLKNNHLPALLEEKQR--ATEVLDRGLLGLDNTLYQIEKEIEDKEEQL-----AQYR 959
Cdd:TIGR00618 473 QQLQTKEQIHLQetrkKAVVLARLLELQEEPCPLCGSCIhpNPARQDIDNPGPLTRRMQRGEQTYAQLETSeedvyHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 960 ASTNQLQ----QLQETFEFTANVARQEEKVRKKEKEILQSREKQQREAleQAVAKLERRHSALQRRSTIDFEIEEQKQKL 1035
Cdd:TIGR00618 553 SERKQRAslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT--EKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
490 500 510
....*....|....*....|....*....|.
gi 2024393536 1036 ATLNNSCS-EQAGLQASLEAEQKALEQDRER 1065
Cdd:TIGR00618 631 RLHLQQCSqELALKLTALHALQLTLTQERVR 661
|
|
| PX_SNX15 |
cd07288 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ... |
1221-1283 |
3.87e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.
Pssm-ID: 132821 Cd Length: 118 Bit Score: 38.80 E-value: 3.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024393536 1221 VFRRYSRFREMHRTLKLKYPEV--ATLEFPP---KKLFGNKDERVIAERRSHLETYLRsfFT----AMLQSP 1283
Cdd:cd07288 40 VWKRYSDLKKLHGELAYTHRNLfrRQEEFPPfprAQVFGRFEAAVIEERRNAAEAMLL--FTvnipALYNSP 109
|
|
| PX_RPK118_like |
cd07287 |
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ... |
1220-1273 |
4.41e-03 |
|
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.
Pssm-ID: 132820 Cd Length: 118 Bit Score: 38.41 E-value: 4.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024393536 1220 TVFRRYSRFREMHRTLKLKYPEVA--TLEFPP---KKLFGNKDERVIAERRSHLETYLR 1273
Cdd:cd07287 39 VVWKRYSDFKKLHKDLWQIHKNLCrqSELFPPfakAKVFGRFDESVIEERRQCAEDLLQ 97
|
|
| PX_YPT35 |
cd07280 |
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ... |
1208-1272 |
4.79e-03 |
|
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.
Pssm-ID: 132813 Cd Length: 120 Bit Score: 38.46 E-value: 4.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024393536 1208 FEIKITVLDETWT---VFRRYSRFREMHRTLKLKYPEVATLE---FPPKKLFGNKDERV----IAERRSHLETYL 1272
Cdd:cd07280 25 WKITIETKDLIGSsivAYKRYSEFVQLREALLDEFPRHKRNEipqLPPKVPWYDSRVNLnkawLEKRRRGLQYFL 99
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
599-758 |
5.06e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 599 ERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEI--VQLQIRKQEESLKRRsvHIESRLKDLLAEK 676
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAakQAEEKQKQAEEAKAK--QAAEAKAKAEAEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 677 EKFEEERLREQQEIELQKK------KQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYiKLESEKKR 750
Cdd:TIGR02794 141 ERKAKEEAAKQAEEEAKAKaaaeakKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAA 219
|
....*...
gi 2024393536 751 IEEQEREQ 758
Cdd:TIGR02794 220 AAAAEAER 227
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
691-1031 |
5.09e-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: 41.36 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 691 ELQKKKQQEEIFARVKEELQRLQELNHKekAEKMQI-FRELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQL 769
Cdd:pfam12128 215 KSRLNRQQVEHWIRDIQAIAGIMKIRPE--FTKLQQeFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 770 REKQVMIQllkrgdvQRVEEEKRDLEDIREsllKVKEARSEGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQMDH 849
Cdd:pfam12128 293 RTLDDQWK-------EKRDELNGELSAADA---AVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 850 LE------KDIAHEKETLEylklaeeehvnLKKDDENfgdavfKAEEFDMVKLTEYRLQSKVRQLEYLKNnHLPALleeK 923
Cdd:pfam12128 363 LKaltgkhQDVTAKYNRRR-----------SKIKEQN------NRDIAGIKDKLAKIREARDRQLAVAED-DLQAL---E 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 924 QRATEVLDRGLLGLDNTLYQIEKEIEDKEEQLAQYRASTNQLQQlQETFEFTANVARQEEKVRKKEKEILQSREKQQREA 1003
Cdd:pfam12128 422 SELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ-LENFDERIERAREEQEAANAEVERLQSELRQARKR 500
|
330 340
....*....|....*....|....*...
gi 2024393536 1004 LEQAVAKLERRHSALQRRSTIDFEIEEQ 1031
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQ 528
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
595-1076 |
5.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 595 GLEFERQQReeleKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQIR----KQEESLKRRSVHIESRLK 670
Cdd:COG4913 280 ALRLWFAQR----RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 671 DLLAEKEKFEEERLREQQEIELQkkkqqEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKR 750
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPAS-----AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 751 IEEQ----EREQVMLVAHLEEQL--REKQVMI--QLLkrgDVQRVEEEKRD-----LEDIRESLL-------KVKEA-RS 809
Cdd:COG4913 431 LERRksniPARLLALRDALAEALglDEAELPFvgELI---EVRPEEERWRGaiervLGGFALTLLvppehyaAALRWvNR 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 810 EGEENCEELEKAQHSFIEFKKKQLEQLTILEKDLVQQ-------MDHLEKDIAHEK-ETLEYLK----------LAEEEH 871
Cdd:COG4913 508 LHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPhpfrawlEAELGRRFDYVCvDSPEELRrhpraitragQVKGNG 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 872 VNLKKDDENFGDAV----FKAEEfdmvklteyRLQSKVRQLEYLKNNHLPAL-----LEEKQRATEVLDRGLLGLDNT-- 940
Cdd:COG4913 588 TRHEKDDRRRIRSRyvlgFDNRA---------KLAALEAELAELEEELAEAEerleaLEAELDALQERREALQRLAEYsw 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 941 ----LYQIEKEIEDKEEQLAQYRASTNQLQQLQETFEfTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHS 1016
Cdd:COG4913 659 deidVASAEREIAELEAELERLDASSDDLAALEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024393536 1017 ALQRRSTID--FEIEEQKQKLATLNNSCSEQAGLQASLEAEQKALEQDRERLDQEIQQLKQK 1076
Cdd:COG4913 738 AAEDLARLElrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
632-756 |
5.24e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 632 RMQQEVESQRKETEIVQLQIRKQEESLKRRSVHIESRLKDLLAEK---------EKFEEERLREQQEIELQKKKQQEEIF 702
Cdd:TIGR02794 54 RIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAaaekaakqaEQAAKQAEEKQKQAEEAKAKQAAEAK 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2024393536 703 ARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQER 756
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA 187
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
708-793 |
5.26e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 41.26 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 708 ELQRLQELNHKEKAEKMQIfreLEKLKKEKDEQYIKLESEKKRIEEQEREQVMlvahlEEQLREKQVMIQLLKRGDVQRV 787
Cdd:PTZ00266 436 ERARIEKENAHRKALEMKI---LEKKRIERLEREERERLERERMERIERERLE-----RERLERERLERDRLERDRLDRL 507
|
....*.
gi 2024393536 788 EEEKRD 793
Cdd:PTZ00266 508 ERERVD 513
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
655-808 |
5.54e-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: 41.36 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 655 EESLKRRSVHIESRLKDLLAEKEKFEEERLREQQEIELQKKkqqEEIFAR--VKEELQRLQELNHKEKAEKMQIFRELEK 732
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR---EETFARtaLKNARLDLRRLFDEKQSEKDKKNKALAE 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024393536 733 LKKEKDEQYIKLESEKKRIeeqEREQVMLVAHLEEQLREKQVMIQllkrGDVQRVEEEKRDLED-IRESLLKVKEAR 808
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQL---DKKHQAWLEEQKEQKREARTEKQ----AYWQVVEGALDAQLAlLKAAIAARRSGA 745
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
473-551 |
5.76e-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: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 473 LKEGQTYVGREDamtEQDIVLHGLDLESEHCIFENL-NGTVNLIPL---NGAQcsVNGIQITEATHLNQGAVILLGrTNM 548
Cdd:cd22673 18 LTKKSCTFGRDL---SCDIRIQLPGVSREHCRIEVDeNGKAYLENLsttNPTL--VNGKAIEKSAELKDGDVITIG-GRS 91
|
...
gi 2024393536 549 FRF 551
Cdd:cd22673 92 FRF 94
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
597-754 |
5.91e-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: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 597 EFERQQREELEKLESKRKQIEEMEEKQRSDKAELVRMQQEVESQRKETEIVQLQirKQEESLKRRSVHIESRLKDLLAEK 676
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ--KEIESLKRRISDLEDEILELMERI 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 677 EkfeeerlreqqeielqkkkQQEEIFARVKEELQRLQElnhKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQ 754
Cdd:COG1579 120 E-------------------ELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
955-1115 |
6.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 955 LAQYRASTNQLQQLQETFEFTANVARQEEKVRKKEKEILQSREKQQREALEQAVAKLERRHSALQRrstidfEIEEQKQK 1034
Cdd:COG3206 269 RAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA------QLAQLEAR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1035 LATLNNscseqaglqasLEAEQKALEQDRERLDQEIQQLKQKIYESD---GGQKGNHGMLEEklshsnsPTNPTKPQPPS 1111
Cdd:COG3206 343 LAELPE-----------LEAELRRLEREVEVARELYESLLQRLEEARlaeALTVGNVRVIDP-------AVVPLKPVSPK 404
|
....
gi 2024393536 1112 APLV 1115
Cdd:COG3206 405 KLLI 408
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-929 |
6.10e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 642 KETEIVQLQIRKQEESLKRRSVHIES--RLKDLLAEKEKFEEERLREQQEIELQKKKQQE---------EIFARVKEELQ 710
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQdeGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEakktetgkaEEARKAEEAKK 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 711 RLQELNHKEKAEKMQIFRELEKLKKEKDEQYIKLEsekKRIEEQEREQVMLVAHLEEQLREKQVMIQLLKRGDVQRVEEE 790
Cdd:PTZ00121 1123 KAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA---RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDA 1199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 791 KRDLEDIR-ESLLKVKEARSEGEENCEELEKAQHsfiEFKKKQLEQLTILEKDLVQQMDHLEKDIAHEKETLEYLKLAEE 869
Cdd:PTZ00121 1200 RKAEAARKaEEERKAEEARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE 1276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 870 EhvnlKKDDEnfgdaVFKAEEfdMVKLTEYRLQSKVRQLEYLKNNhlpalLEEKQRATEV 929
Cdd:PTZ00121 1277 A----RKADE-----LKKAEE--KKKADEAKKAEEKKKADEAKKK-----AEEAKKADEA 1320
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
579-795 |
6.12e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 579 LSKSCENlsAVMLYNPGLEFERQQREELEKLESKRKQIEE----MEEKQRSDKAelvrMQQEVESQRKETEIVQLQIRKQ 654
Cdd:pfam05483 568 LDKSEEN--ARSIEYEVLKKEKQMKILENKCNNLKKQIENknknIEELHQENKA----LKKKGSAENKQLNAYEIKVNKL 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 655 EESLKrrsvhiesrlkdllAEKEKFEEERLREQQEIELQKKKQQ------EEIFARVKEELQRLQELNHKEKAEKMQIFR 728
Cdd:pfam05483 642 ELELA--------------SAKQKFEEIIDNYQKEIEDKKISEEklleevEKAKAIADEAVKLQKEIDKRCQHKIAEMVA 707
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024393536 729 ELEKLKKEKDEQYIKLESEKKRIEEQEREQVMLVAHLEEQLRE-KQVMIQLLKRGDVQRVEEEKRDLE 795
Cdd:pfam05483 708 LMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
993-1077 |
6.54e-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: 40.52 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 993 LQSREKQQREALEQAVAKLERRHSALQRrstidfEIEEQKQKLATLNNScseqaglQASLEAEQKALEQDRERLDQEIQQ 1072
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEA------LKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALIAR 231
|
....*
gi 2024393536 1073 LKQKI 1077
Cdd:COG4942 232 LEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
889-1076 |
7.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 889 EEFDMVKLTEYRLQSKVRQLEYLKnnHLPALLEEKQRATE---VLDRGLLGLDntLYQIEKEIEDKEEQLAQYRASTNQL 965
Cdd:COG4913 232 EHFDDLERAHEALEDAREQIELLE--PIRELAERYAAARErlaELEYLRAALR--LWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 966 QQLQETFEftANVARQEEKVRKKEKEILQS------REKQQREALEQAVAKLERRHSALQRR-STIDFEI-------EEQ 1031
Cdd:COG4913 308 EAELERLE--ARLDALREELDELEAQIRGNggdrleQLEREIERLERELEERERRRARLEALlAALGLPLpasaeefAAL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024393536 1032 KQKLATLNNSCSEQAGL----QASLEAEQKALEQDRERLDQEIQQLKQK 1076
Cdd:COG4913 386 RAEAAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
634-1093 |
9.14e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 634 QQEVESQRKETEIVQLQIRKQEesLKRRSVHIESRLKDLLAEKEKfeeerlreqqeieLQKKKQQE-EIFARVKEELQRL 712
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQK--AESELKELEKKHQQLCEEKNA-------------LQEQLQAEtELCAEAEEMRARL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 713 QelnhKEKAEKMQIFRELEKLKKEKDEQYIKLESEKKRIEEQereqvmlVAHLEEQLREKQVMIQLLK------RGDVQR 786
Cdd:pfam01576 67 A----ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQH-------IQDLEEQLDEEEAARQKLQlekvttEAKIKK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 787 VEEEKRDLEDIRESLLKVK----EARSEGEENCEELEKAQHSFIEFKKKQLEQLTILE----------KDLVQQMDHLEK 852
Cdd:pfam01576 136 LEEDILLLEDQNSKLSKERklleERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEerlkkeekgrQELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 853 DIAHEKETLEYLKL-AEEEHVNLKKDDENFGDAVFKAEEFDMVKLTeyrLQSKVRQLEylknNHLPALLEEKQRatEVLD 931
Cdd:pfam01576 216 ESTDLQEQIAELQAqIAELRAQLAKKEEELQAALARLEEETAQKNN---ALKKIRELE----AQISELQEDLES--ERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 932 RGllgldntlyQIEKEIEDKEEQLAQYRAstnqlqQLQETFEFTAnvARQEekvrkkekeiLQSREKQQREALEQAVAKL 1011
Cdd:pfam01576 287 RN---------KAEKQRRDLGEELEALKT------ELEDTLDTTA--AQQE----------LRSKREQEVTELKKALEEE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 1012 ERRHSAlqrrstidfEIEEQKQKLATLNNSCSEQ----AGLQASLEAEQKALEQDRERLDQEIQQLKQKIYESDGGQKGN 1087
Cdd:pfam01576 340 TRSHEA---------QLQEMRQKHTQALEELTEQleqaKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL 410
|
....*.
gi 2024393536 1088 HGMLEE 1093
Cdd:pfam01576 411 EGQLQE 416
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
691-809 |
9.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024393536 691 ELQKKKQQEEIFARVKEELQRLQELNHKEKAEKMQIFRELEKLKKEKDEQYIK----LESEKKRIEEQEREqvmlVAHLE 766
Cdd:PRK12704 48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRklelLEKREEELEKKEKE----LEQKQ 123
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024393536 767 EQLREKQVMIQLLkrgdvqrVEEEKRDLEDIreSLLKVKEARS 809
Cdd:PRK12704 124 QELEKKEEELEEL-------IEEQLQELERI--SGLTAEEAKE 157
|
|
| PX_SNX19 |
cd06893 |
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ... |
1218-1273 |
9.97e-03 |
|
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.
Pssm-ID: 132803 [Multi-domain] Cd Length: 132 Bit Score: 37.91 E-value: 9.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024393536 1218 TWTVFRRYSRFREMHRTL--KLKYPEVATLEFPPKKL----FGNKDERVIAERRSHLETYLR 1273
Cdd:cd06893 50 THTVNRRFREFLTLQTRLeeNPKFRKIMNVKGPPKRLfdlpFGNMDKDKIEARRGLLETFLR 111
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