|
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: 564.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365 159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365 239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2287254621 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365 315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
3-365 |
1.18e-149 |
|
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: 463.97 E-value: 1.18e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129 68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129 146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2287254621 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
9-358 |
3.28e-148 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 459.73 E-value: 3.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225 68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225 146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225 226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
|
330 340 350
....*....|....*....|....*....|..
gi 2287254621 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 |
5.08e-139 |
|
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: 434.38 E-value: 5.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106 145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 2287254621 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 |
2.14e-118 |
|
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: 377.57 E-value: 2.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371 148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371 226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2287254621 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 |
3.23e-114 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 365.89 E-value: 3.23e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372 62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372 140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372 220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2287254621 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 |
1.44e-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: 338.55 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370 76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370 154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370 231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2287254621 315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370 302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
3-358 |
4.94e-102 |
|
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: 330.45 E-value: 4.94e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374 138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374 215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 2287254621 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 |
1.01e-101 |
|
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: 330.62 E-value: 1.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373 144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373 221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2287254621 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373 293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
1-358 |
1.99e-99 |
|
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: 323.13 E-value: 1.99e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYsADTkspdyvSQEMVF 79
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFD-PNT------TQEDVY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369 62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369 140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369 215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2287254621 317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369 284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-360 |
1.70e-98 |
|
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: 320.70 E-value: 1.70e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366 9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366 71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfds 238
Cdd:cd01366 148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWL 318
Cdd:cd01366 225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2287254621 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366 288 LQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
1-367 |
2.43e-89 |
|
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: 295.39 E-value: 2.43e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364 145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364 225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2287254621 305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364 291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-508 |
9.14e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 290.10 E-value: 9.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059 18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059 91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059 244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQ--------------- 392
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSqsslsgifaymqslk 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 393 --IALLDSPTALSMEEKLQQNEARVQEL-TKEWTNKwnETQNILKEQTLALrkegiGVVLDSELPHLIGIDDDLLSTGII 469
Cdd:COG5059 394 keTETLKSRIDLIMKSIISGTFERKKLLkEEGWKYK--STLQFLRIEIDRL-----LLLREEELSKKKTKIHKLNKLRHD 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2287254621 470 LYHLKEGQT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059 467 LSSLLSSIPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
446-562 |
4.97e-79 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438784 [Multi-domain] Cd Length: 117 Bit Score: 256.01 E-value: 4.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2287254621 526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
4-392 |
1.68e-74 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 274.12 E-value: 1.68e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188 100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188 154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188 232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188 309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188 380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454
|
410 420
....*....|....*....|
gi 2287254621 373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188 455 IRQLRDELQRVK---ANGNN 471
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
4-356 |
5.64e-73 |
|
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: 248.08 E-value: 5.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368 78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368 150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368 230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2287254621 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368 303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
3-356 |
3.66e-72 |
|
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: 245.18 E-value: 3.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375 1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375 68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375 145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375 225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2287254621 316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375 294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
4-356 |
3.16e-68 |
|
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: 233.16 E-value: 3.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376 66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376 142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376 219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 2287254621 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376 286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
4-356 |
4.03e-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: 233.34 E-value: 4.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367 63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367 141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367 217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2287254621 309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367 280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| FHA_KIF16 |
cd22708 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ... |
446-554 |
5.03e-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: 215.60 E-value: 5.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 2287254621 526 GVQIVEATHLNQGAVILLGRTNMFRFNHP 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 |
3.48e-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: 170.73 E-value: 3.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2287254621 526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKR 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 |
2.46e-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: 128.21 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTeqdIVLHGLDLESEHCIFENIGGTVTLIPL 517
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2287254621 518 sGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713 78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
|
|
| FHA_KIF1 |
cd22705 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
453-553 |
9.23e-32 |
|
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: 120.03 E-value: 9.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEA 532
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 2287254621 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 |
1.07e-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: 105.81 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQI 529
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 2287254621 530 VEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707 84 SEPTVLHHGDRVILGGDHYFRFNHP 108
|
|
| FHA_KIF1A |
cd22726 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
454-562 |
3.76e-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: 104.63 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-----VTLIPLSGSQCSVNGVQ 528
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 2287254621 529 IVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 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 |
2.01e-25 |
|
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: 102.42 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIF-----ENIGGTVTLIPLSGSQCSVNGVQ 528
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 2287254621 529 IVEATHLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727 83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
454-554 |
3.43e-25 |
|
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: 101.52 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLS-GSQCSVNGVQIVEA 532
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 2287254621 533 THLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709 81 TELHHLDRVILGSNHLYVFVGP 102
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
6-288 |
7.41e-24 |
|
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: 100.11 E-value: 7.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363 1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363 42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363 100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2287254621 243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363 137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| FHA_KIF13 |
cd22706 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ... |
471-554 |
2.30e-20 |
|
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: 87.73 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 471 YHLKEgQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 2287254621 551 FNHP 554
Cdd:cd22706 98 LNCP 101
|
|
| FHA_KIF1C |
cd22728 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
454-553 |
2.77e-18 |
|
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: 81.84 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDAsteqDIVLHGLDLESEHCIFENIGG-----TVTLIPLSGSQCSVNGVQ 528
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 2287254621 529 IVEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-1095 |
2.85e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG1196 279 LELELEEAQAEEYELLAELARL-EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKfeEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:COG1196 358 AELAE--AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 765 QEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQL 844
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHD--KESRLLEKHDESVTD-----VTEVPQDFEKIKPVEYRLQYKE 917
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAakagrATFLPLDKIRARAALAAALARG 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 918 RQLQ-YLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEK 996
Cdd:COG1196 596 AIGAaVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 997 VRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
490
....*....|....*....
gi 2287254621 1077 RINAYIEEEVQRRLQDLHR 1095
Cdd:COG1196 756 LPEPPDLEELERELERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
611-1099 |
3.48e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaeke 688
Cdd:COG1196 216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 689 kfeeerlreqqeielqkkRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 768
Cdd:COG1196 291 ------------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 769 QVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQLRffEFKRRQLVKL 847
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLE--EELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 848 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 927
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 928 LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ---------LAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 999 KKEKEI--------------LESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASL 1064
Cdd:COG1196 591 ALARGAigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510
....*....|....*....|....*....|....*
gi 2287254621 1065 EAEQEALEKDQERINAYIEEEVQRRLQDLHRVISE 1099
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
3-162 |
2.09e-15 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 74.95 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796 21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEGLFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796 77 SQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
453-554 |
8.20e-15 |
|
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: 71.97 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--RDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSG-SQCSV 524
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 2287254621 525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
624-937 |
1.42e-14 |
|
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: 79.40 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 624 RKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLReqqeiEL 703
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERER-----EL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 704 QKKRQEEEtflrvQEELQRLKElnnNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKR----LEEQEKEQVMLVAHLE 777
Cdd:pfam17380 351 ERIRQEER-----KRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVrqELEAARkvkiLEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 778 EQLREKQEMIqllRRGEVQWVEEEK-RDLEGIREsllrvkearaggdedgEELEKAQ----LRFFEFKRRQlvKLVNLEK 852
Cdd:pfam17380 423 EQIRAEQEEA---RQREVRRLEEERaREMERVRL----------------EEQERQQqverLRQQEEERKR--KKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 853 DLVQQKD-------ILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQYKERQLQYLLQ 925
Cdd:pfam17380 482 EKRDRKRaeeqrrkILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
330
....*....|..
gi 2287254621 926 NHLPTLLEEKQR 937
Cdd:pfam17380 556 EQMRKATEERSR 567
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
610-902 |
5.84e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 681
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 682 dLLAEKEKFEEerlreqqeiELQKKRQEE----ETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLEL 757
Cdd:PTZ00121 1600 -LYEEEKKMKA---------EEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 758 EKKRlEEQEKEQVMLVAHLEEQLREKQEmiQLLRRGE--------VQWVEEEKRDLEGIR----ESLLRVKEARAGGDED 825
Cdd:PTZ00121 1666 EAKK-AEEDKKKAEEAKKAEEDEKKAAE--ALKKEAEeakkaeelKKKEAEEKKKAEELKkaeeENKIKAEEAKKEAEED 1742
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254621 826 GEELEKAQLRFFEFKrrqlvKLVNLEKDLVQQKDILKKEvqEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 902
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKE--KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
610-919 |
3.29e-13 |
|
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: 74.77 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESKR------KLIEEMEEKQKSDKAELERmQQEVETQ--------------RKETEIVQLQIRKQE-ES 668
Cdd:pfam17380 286 ERQQQEKFEKMEQERlrqekeEKAREVERRRKLEEAEKAR-QAEMDRQaaiyaeqermamerERELERIRQEERKRElER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 669 LKRRSFHIE-NKLKDLlaEKEKFEEERLREQQEIELQKKR----QEEETFLRVQEELQRLKELNNnEKAEKFQIfqELDQ 743
Cdd:pfam17380 365 IRQEEIAMEiSRMREL--ERLQMERQQKNERVRQELEAARkvkiLEEERQRKIQQQKVEMEQIRA-EQEEARQR--EVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 744 LQKEKDEqyaklELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR-----DLEGIRESLLRVKEA 818
Cdd:pfam17380 440 LEEERAR-----EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 819 RAGGDEDGEELEKA-----QLRFFEFKRRQLVKLVnlEKDLVQQKdilKKEVQEEQEILECLKCEHDKESRLLEkhDESV 893
Cdd:pfam17380 515 RKLLEKEMEERQKAiyeeeRRREAEEERRKQQEME--ERRRIQEQ---MRKATEERSRLEAMEREREMMRQIVE--SEKA 587
|
330 340
....*....|....*....|....*.
gi 2287254621 894 TDVTEVPQDFEKIKPVeYRLQYKERQ 919
Cdd:pfam17380 588 RAEYEATTPITTIKPI-YRPRISEYQ 612
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-944 |
5.79e-13 |
|
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: 74.33 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 613 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLAEKEKFEE 692
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL-------KRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 693 ERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRLEE--QEK 767
Cdd:TIGR02169 738 RLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArlREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 768 EQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE---------KAQ 833
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkkerdelEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 913
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977
|
330 340 350
....*....|....*....|....*....|....
gi 2287254621 914 --QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 944
Cdd:TIGR02169 978 iqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-1092 |
6.16e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 690 FEEERLREQQEIE--LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1196 419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 768 EQVM--------LVAHLEEQLREKQEMIQLLRRGE---------------VQWVEEEKRDLEGIRESLLRVKEARAGGdE 824
Cdd:COG1196 499 AEADyegflegvKAALLLAGLRGLAGAVAVLIGVEaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATF-L 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 825 DGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFE 904
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 905 kIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRgplSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATF 984
Cdd:COG1196 658 -AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE---EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 985 EFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRhsaLQRhstLG-------MEIEEQRQKLASLNsgsrEQ 1057
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE---IEA---LGpvnllaiEEYEELEERYDFLS----EQ 803
|
490 500 510
....*....|....*....|....*....|....*
gi 2287254621 1058 sglQASLEAEQEALEkdqERINAyIEEEVQRRLQD 1092
Cdd:COG1196 804 ---REDLEEARETLE---EAIEE-IDRETRERFLE 831
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1197 |
8.63e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 686 EKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQ 765
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEA 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 766 EKEQvmlvaHLEEQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFE 838
Cdd:PTZ00121 1457 KKAE-----EAKKKAEEAKKADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAE 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 839 FKRR--QLVKLVNLEK-DLVQQKDILKKeVQEEQEILECLKCEHDKESRL-----LEKHDES-VTDVTEVPQDFEKIKPV 909
Cdd:PTZ00121 1532 EAKKadEAKKAEEKKKaDELKKAEELKK-AEEKKKAEEAKKAEEDKNMALrkaeeAKKAEEArIEEVMKLYEEEKKMKAE 1610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 910 EYRLQYKERQLQYLLQNHlptllEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQY-------QANANQLQKLQA 982
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakkaeedKKKAEEAKKAEE 1685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 983 TFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQrhstLGMEIEEQRQKLASLNSGSREQSGLQA 1062
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1063 SLEAEQEALEKDQERINAYIEEEVQRrlQDLHRVIsEGCSTSADTMKDNEKLHNGTIQRKL--KYEKRQFCPAwyldpll 1140
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDE--EDEKRRM-EVDKKIKDIFDNFANIIEGGKEGNLviNDSKEMEDSA------- 1831
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 1141 PRDATDTSSLIKEERREVDQNDHWDHpmlwSVSGPKTTSSA--SQERTHQQRDQSSVPE 1197
Cdd:PTZ00121 1832 IKEVADSKNMQLEEADAFEKHKFNKN----NENGEDGNKEAdfNKEKDLKEDDEEEIEE 1886
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-905 |
1.06e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLA 685
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 686 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 766 EKEQVMLVAHLE----EQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARaggdEDGEELEKAQLRFFEFKR 841
Cdd:TIGR02168 399 NNEIERLEARLErledRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL----ERLEEALEELREELEEAE 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287254621 842 RQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 905
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
456-564 |
1.59e-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: 65.68 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 456 LIGIDDDLLSTGIILYHLKeGQTYVGRDdasTEQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVGAD---TSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 2287254621 535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
611-1083 |
3.39e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 680
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 681 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:PRK03918 348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 761 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 840
Cdd:PRK03918 413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 841 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 916
Cdd:PRK03918 483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 917 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 992
Cdd:PRK03918 562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 993 QEEKVRKKEKEILESREK---QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQE 1069
Cdd:PRK03918 638 TEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
490
....*....|....
gi 2287254621 1070 ALEKDQERINAYIE 1083
Cdd:PRK03918 715 KLEKALERVEELRE 728
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-946 |
5.13e-12 |
|
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: 71.54 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENK 679
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 680 LKDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 754
Cdd:pfam02463 243 QELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 755 LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 834
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 835 RFFEFKRRQLVKLVNLEKDLVQQKDILKKE--VQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpQDFEKIKPVEYR 912
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDE--LELKKSEDLLKE 476
|
330 340 350
....*....|....*....|....*....|....
gi 2287254621 913 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGP 946
Cdd:pfam02463 477 TQLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
610-870 |
5.38e-12 |
|
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: 69.18 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI--RKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:pfam13868 30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEETFLRVQE---ELQRLKELNNNEKAEKFqifqeldqlQKEKDEQYAKLELEKKRL-E 763
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAewkELEKEEEREEDERILEY---------LKEKAEREEEREAEREEIeE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 764 EQEKEQVMLVAHLEEQLREKQEMIQLLRRG-----EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR--- 835
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEree 260
|
250 260 270
....*....|....*....|....*....|....*.
gi 2287254621 836 -FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQE 870
Cdd:pfam13868 261 eEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
364-476 |
1.05e-11 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 65.25 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 2287254621 463 LLSTGIILYHLKEG 476
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-1099 |
1.19e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 702 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 781
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 782 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 858
Cdd:PRK03918 242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 859 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQ-YKERQLQYllqnhlptLLEEKQR 937
Cdd:PRK03918 321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGL--------TPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 938 AFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESR 1008
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1009 EKQQREaLERALARLER---RHSALQRHSTLGMEIEEQRQKLASLN-----SGSREQSGLQ---ASLEAEQEALEKDQER 1077
Cdd:PRK03918 472 EEKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNleeleKKAEEYEKLKeklIKLKGEIKSLKKELEK 550
|
410 420 430
....*....|....*....|....*....|.
gi 2287254621 1078 INAYIEE---------EVQRRLQDLHRVISE 1099
Cdd:PRK03918 551 LEELKKKlaelekkldELEEELAELLKELEE 581
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
555-825 |
2.67e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSREN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 632
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 633 KQKSDKAELERMQQEVEtqrkETEIVQLQIRKQEESLKRrsfhienKLKDLLAEKEKfeeerlreqqeielqkKRQEEET 712
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKK-------KAEEAKKAEED----------------EKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 713 FLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvahleEQLR---EKQEMIQL 789
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEK----KKAEELKKAEEENKIKAE-EAKKEAEEDKKKA-------EEAKkdeEEKKKIAH 1761
|
250 260 270
....*....|....*....|....*....|....*.
gi 2287254621 790 LRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDED 825
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
612-925 |
4.40e-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: 68.16 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 612 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEN--------- 678
Cdd:TIGR02168 674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeriaqls 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 679 -KLKDLLAEKEKFEEERLREQQEIE--LQKKRQEEETFLRVQEELQ----RLKELN---NNEKAEKFQIFQELDQLQKEK 748
Cdd:TIGR02168 754 kELTELEAEIEELEERLEEAEEELAeaEAEIEELEAQIEQLKEELKalreALDELRaelTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 749 DEQYAKLELEKKRLEEQEKEQVML---VAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLE----GIRESLLRVKEA 818
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALlneRASLEEALALLRSELEelseELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 819 RAGGDEDGEELEKAQLRffefkrrqlvkLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHdesvtdVTE 898
Cdd:TIGR02168 914 RRELEELREKLAQLELR-----------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR------LKR 976
|
330 340 350
....*....|....*....|....*....|...
gi 2287254621 899 VPQDFEKIKPV------EYRlQYKERqLQYLLQ 925
Cdd:TIGR02168 977 LENKIKELGPVnlaaieEYE-ELKER-YDFLTA 1007
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
605-1095 |
6.42e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKlieemeEKQKSDKAELERMQQEVETQRKETEIVQlQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKFEEERLREQQEIELQKKRQEEETF-LRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEK---- 759
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELpERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATeeel 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 760 KRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIR-----ESLLRVKEARAGGDEDGEELEKAQL 834
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEErlkeaRLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 835 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH----DESVTDVTEVPQDFEKIKPVE 910
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 911 YRLQYKERQLQyllqnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQatfeftANI 990
Cdd:COG4717 354 REAEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELE------EQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 991 ARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSR--EQSGLQASLEAEQ 1068
Cdd:COG4717 412 EELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE------ELAELEAELEQLEEDGElaELLQELEELKAEL 485
|
490 500
....*....|....*....|....*....
gi 2287254621 1069 EALEKDQERINAYIE--EEVQRRLQDLHR 1095
Cdd:COG4717 486 RELAEEWAALKLALEllEEAREEYREERL 514
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
456-554 |
6.91e-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: 60.70 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 456 LIGIDDDLLSTGIILYHLKEgQTYVGRDDAsteQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 2287254621 535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
706-1100 |
7.03e-11 |
|
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: 67.79 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 782
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 783 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 854
Cdd:TIGR02169 749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 855 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 934
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 935 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1012
Cdd:TIGR02169 887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1013 REALERALARLERRHSAlqrhstlgmEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALEK-----DQERINAYIE--EE 1085
Cdd:TIGR02169 960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAILErieeyEKKKREVFMEafEA 1026
|
410
....*....|....*
gi 2287254621 1086 VQRRLQDLHRVISEG 1100
Cdd:TIGR02169 1027 INENFNEIFAELSGG 1041
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
612-1106 |
8.89e-11 |
|
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: 67.05 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 612 QQREELEKLESKRKL----IEEMEEKQKSDKAELE----RMQQEVETQRKETEIVQLQIR-----------KQEESLKRR 672
Cdd:pfam05483 265 ESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 673 SFH--IENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtFLRVQEELQRLKELNNNEKAEkfqiFQELDQLQKEKDe 750
Cdd:pfam05483 345 AAHsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVE----LEELKKILAEDE- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 751 qyaKLELEKKRLEEqekeqvmlvahLEEQLREK-QEMIQLLrrgevQWVEEEKRDLEgIRESLLRVKEARAGGD--EDGE 827
Cdd:pfam05483 419 ---KLLDEKKQFEK-----------IAEELKGKeQELIFLL-----QAREKEIHDLE-IQLTAIKTSEEHYLKEveDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 828 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQEEQE-ILECLKCEHD--KESRLLEKHDESVTDVTE-VPQDF 903
Cdd:pfam05483 479 ELEKEKLKNIELTAHC-DKLLLENKELTQEASDMTLELKKHQEdIINCKKQEERmlKQIENLEEKEMNLRDELEsVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 904 ---------------EKIKPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQ 966
Cdd:pfam05483 558 iqkgdevkckldkseENARSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQ 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 967 LAQYQANANQLQ-KLQATF----EFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQ 1031
Cdd:pfam05483 631 LNAYEIKVNKLElELASAKqkfeEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALME 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2287254621 1032 RHS-TLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQRRlQDLHRVISEGCSTSAD 1106
Cdd:pfam05483 711 KHKhQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK-EKLKMEAKENTAILKD 785
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
606-785 |
8.93e-11 |
|
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: 66.51 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetqrKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:pfam15709 347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ------RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 686 EKEKFEEERLREQQEI-ELQKKRQEEETfLRVQEELQRLKELnNNEKAEKFQIFQELD-------QLQKEKDEQYAKLEL 757
Cdd:pfam15709 417 AQERARQQQEEFRRKLqELQRKKQQEEA-ERAEAEKQRQKEL-EMQLAEEQKRLMEMAeeerleyQRQKQEAEEKARLEA 494
|
170 180
....*....|....*....|....*...
gi 2287254621 758 EKKRleEQEKEQVMLVahLEEQLREKQE 785
Cdd:pfam15709 495 EERR--QKEEEAARLA--LEEAMKQAQE 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-927 |
9.65e-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: 67.39 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQqreeLEKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQL-QIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:TIGR02168 197 ELERQ----LKSLERQAEKAERYKEL----KAELRELELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 687 KEkfeeerlreqqeiELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ 765
Cdd:TIGR02168 269 LE-------------ELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 766 EKEQVML----------VAHLEEQLREKQEMIQLLRRGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:TIGR02168 336 AEELAELeekleelkeeLESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 833 QLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpVEYR 912
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQA------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQ 486
|
330
....*....|....*
gi 2287254621 913 LQYKERQLQYLLQNH 927
Cdd:TIGR02168 487 LQARLDSLERLQENL 501
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
611-1093 |
9.67e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 690
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 691 EEERLREQQEIELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIF----QELDQLQKEKDEQYAKLELEKKRLEEQE 766
Cdd:COG4717 152 EERLEELRELEEELEELEAELA--ELQEELEELLEQLSLATEEELQDLaeelEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 767 K--EQVMLVAHLEEQLREKQEMIQLLRRGEVqwveeekrdLEGIRESLLRVKEARAGgdedgeeLEKAQLRFFefkrrQL 844
Cdd:COG4717 230 EqlENELEAAALEERLKEARLLLLIAAALLA---------LLGLGGSLLSLILTIAG-------VLFLVLGLL-----AL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 845 VKLVNLEKDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 924
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 925 QNHLptlleEKQRAfEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEI 1004
Cdd:COG4717 365 LEEL-----EQEIA-ALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1005 LESRE--------KQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:COG4717 432 EELEEleeeleelEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
490
....*....|....*..
gi 2287254621 1077 RINAYIEEEVQRRLQDL 1093
Cdd:COG4717 512 ERLPPVLERASEYFSRL 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-920 |
1.22e-10 |
|
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: 67.02 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQREELEKLEskrklieemEEKQKSDKAELERMQQEVETQRKeteivqlQIRKQEESLKRrsfHIEnKLKDLLA 685
Cdd:TIGR02169 202 RLRREREKAERYQALL---------KEKREYEGYELLKEKEALERQKE-------AIERQLASLEE---ELE-KLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 686 EKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLK-ELNNNEK--AEKFQIFQELDQLQKEKDEQYAKLELEKKRL 762
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLegiRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRR 842
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRA-ELEEVDKEFAET---RDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 843 QLVKLVNLE---KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpqdfEKIKPVEYRLQYKERQ 919
Cdd:TIGR02169 418 LSEELADLNaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK------EEYDRVEKELSKLQRE 491
|
.
gi 2287254621 920 L 920
Cdd:TIGR02169 492 L 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
623-1042 |
1.86e-10 |
|
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: 66.24 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 623 KRKLIEEM-------EEKQKSdKAELErmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKFeeerl 695
Cdd:TIGR02169 155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY----- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 696 reqqeielqkkrqeeetflrvqEELQRLKELNNNEKaEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvah 775
Cdd:TIGR02169 224 ----------------------EGYELLKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEE----------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 776 LEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLV 855
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 856 QQ---KDILKKEVQEEQEILECLKCEHDKESrllEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLL 932
Cdd:TIGR02169 347 EErkrRDKLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 933 EEKQRAFEILDRgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftaniARQEEKVRKKEKEILESRekqq 1012
Cdd:TIGR02169 424 DLNAAIAGIEAK--------INELEEEKEDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKE---- 484
|
410 420 430
....*....|....*....|....*....|
gi 2287254621 1013 REALERALARLERRHSALQRHSTLGMEIEE 1042
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
607-1099 |
2.18e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAE 686
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 687 KEKFEEERLREQQEIElQKKRQEEEtflRVQEELQRLKELNNNEKaekfqifqELDQLqKEKDEQYAKLELE----KKRL 762
Cdd:PRK03918 243 LEKELESLEGSKRKLE-EKIRELEE---RIEELKKEIEELEEKVK--------ELKEL-KEKAEEYIKLSEFyeeyLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 763 EEQEKEqvmlVAHLEEQLREKQEMIQLL--RRGEVQWVEEE----KRDLEGIRESLLRVKEARAGGDE--------DGEE 828
Cdd:PRK03918 310 REIEKR----LSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEAKAKKEElerlkkrlTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 829 LEKAQLRFFEFKRRQLvKLVNLEKDLVQQKDILKKEVQEEQEILECLK-----C--------EHDKEsRLLEKHDESVTD 895
Cdd:PRK03918 386 PEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKkakgkCpvcgreltEEHRK-ELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 896 VTEvpqDFEKIKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFEIldrgpLSLDNTLYQVekemeekeeqlaqyqaNAN 975
Cdd:PRK03918 464 IEK---ELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQL-----KELEEKLKKY----------------NLE 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 976 QLQKLQATFEFTANIARQEEKVRKKEKEILESRE--KQQREALERALARLERRHSALQRH-STLGME-IEEQRQKLASLN 1051
Cdd:PRK03918 519 ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKElEELGFEsVEELEERLKELE 598
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1052 SGSREQSGLQAS---LEAEQEALEKDQERINAYIE---------EEVQRRLQDLHRVISE 1099
Cdd:PRK03918 599 PFYNEYLELKDAekeLEREEKELKKLEEELDKAFEelaetekrlEELRKELEELEKKYSE 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
706-1077 |
3.99e-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: 65.08 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 706 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 761
Cdd:TIGR02168 171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 762 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 841
Cdd:TIGR02168 251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 842 RQLV-KLVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 917
Cdd:TIGR02168 312 ANLErQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 918 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 997
Cdd:TIGR02168 379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 998 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1076
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
.
gi 2287254621 1077 R 1077
Cdd:TIGR02168 500 N 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
608-1131 |
8.82e-10 |
|
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: 63.83 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETQRKETEIVQLQirkqeeslkRRSF 674
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHI---------KAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 675 HIENKLKDLLAE-KEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQlQKEKDEQYA 753
Cdd:TIGR00618 304 QIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ-QHTLTQHIH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 754 KLELEKKRLEEQEKeqvmLVAHLEEQLREkqemiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:TIGR00618 383 TLQQQKTTLTQKLQ----SLCKELDILQR----------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 834 LRFFEFKRRQLVKLVNL-----------EKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH----DESVTDVTE 898
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIhlqesaqslkeREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpNPARQDIDN 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 899 VPQDFEKIKPVEYRLQYKERQLQYL------LQNHLPTLLEEKQRafEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQA 972
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVyhqltsERKQRASLKEQMQE--IQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 973 NANQLQKLQATFEFTANIaRQEEKVRKKEKEILESREKQQREALEraLARLERRHSAL----QRHSTLGMEIEEQRQKLA 1048
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALL-RKLQPEQDLQDVRLHLQQCSQELALK--LTALHALQLTLtqerVREHALSIRVLPKELLAS 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1049 SLNSGSREQSGLQaSLEAEQEALEKDQERINAyiEEEVQRRLQDLHRVISEGCSTSADTMKDNEKLHNGTIQRKLKYEKR 1128
Cdd:TIGR00618 678 RQLALQKMQSEKE-QLTYWKEMLAQCQTLLRE--LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
...
gi 2287254621 1129 QFC 1131
Cdd:TIGR00618 755 VLK 757
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
611-820 |
1.01e-09 |
|
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: 62.47 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG4942 26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 690 FEEERlreqqeIELQKKRQEE--------ETFLRVQEELQRLKELNNNEKAEKFQIFQELDQL----------QKEKDEQ 751
Cdd:COG4942 106 LAELL------RALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalraeleaeRAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 752 YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveeEKRDLEGIRESLLRVKEARA 820
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLEAEAAAAA 240
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
455-551 |
1.31e-09 |
|
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: 56.51 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 455 HLIGIDDDllsTGIILYHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQ-CSVNGVQIVEAT 533
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGRSPDC---DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNgTFVNGKRITPPV 74
|
90
....*....|....*...
gi 2287254621 534 HLNQGAVILLGRTNmFRF 551
Cdd:cd00060 75 PLQDGDVIRLGDTT-FRF 91
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-891 |
2.00e-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: 63.07 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLL 684
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEEL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRL 762
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKI-----KEEELEELALELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEE 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 763 EEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ---------WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekeneieeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEE 958
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 834 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
606-1025 |
2.28e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRketEIVQLQIRKQEESLKRRSFHIEnKLKDLL 684
Cdd:PRK03918 318 RLEEEINGiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPE-KLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKFEEERLREQQEI-----ELQKKRQEEETFLrvqEELQRLK--------ELNNNEKAEKFQIF-QELDQLQKEK-- 748
Cdd:PRK03918 394 EELEKAKEEIEEEISKItarigELKKEIKELKKAI---EELKKAKgkcpvcgrELTEEHRKELLEEYtAELKRIEKELke 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 749 -DEQYAKLELEKKRLEEQEKEQVMLVAHLE--EQLREKQEMiqlLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDED 825
Cdd:PRK03918 471 iEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEK---LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 826 GEELE--KAQLRFFEFKRRQL-VKLVNLEKDL----VQQKDILKKEVQEEQEI----LECLKCEHDKESRLLEKHDESvt 894
Cdd:PRK03918 548 LEKLEelKKKLAELEKKLDELeEELAELLKELeelgFESVEELEERLKELEPFyneyLELKDAEKELEREEKELKKLE-- 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 895 dvTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDntlyqvekemeekeeqlAQYQANA 974
Cdd:PRK03918 626 --EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-----------------AELEELE 686
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2287254621 975 NQLQKLQATFEftaNIARQeekvrkkekeiLESREKQQRE--ALERALARLER 1025
Cdd:PRK03918 687 KRREEIKKTLE---KLKEE-----------LEEREKAKKEleKLEKALERVEE 725
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1127 |
2.62e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQREELEKLESKRKLIE----------EMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRR 672
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEirkfeearmaHFARRQAAIKAEEARKADELkkaEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 673 SfhiENKLKdllaeKEKFEEERLREQQEIELQKKRQEEEtflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEkdEQY 752
Cdd:PTZ00121 1311 A---EEAKK-----ADEAKKKAEEAKKKADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE--EAK 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 753 AKLELEKKRLEEQEKeqvmlvahlEEQLREKQEMIQlLRRGEVQWVEEEKRDLEGIRESLLRVKEARAgGDEDGEELEKA 832
Cdd:PTZ00121 1378 KKADAAKKKAEEKKK---------ADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 833 QlrffEFKRR--QLVKLVNLEKDLVQQK--DILKKEVQEEQEILECLKC--EHDKESRLLEKHDESVTDVTEVPQDFEKI 906
Cdd:PTZ00121 1447 D----EAKKKaeEAKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 907 KPVEYRLQYKERQLQYLLQnhlptlLEEKQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEF 986
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKK------AEEKKKADEL---------KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 987 TANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEA 1066
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254621 1067 EQEALEKDQERINAYIEEEVQRRLQDLHRVISEGCST------SADTMKDNEKLHNGTIQRKLKYEK 1127
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeelkkkEAEEKKKAEELKKAEEENKIKAEE 1734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
605-1160 |
2.68e-09 |
|
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: 62.39 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQR--EELEK-LESKRKLIEEMEEKQKSDKAELERMQ---QEVETQRKETEIVQLQIRKQEESLKRRSFHIEN 678
Cdd:TIGR02169 327 LEAEIDKLLAeiEELEReIEEERKRRDKLTEEYAELKEELEDLRaelEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 679 KLKDLLAEKEKFEEERLREQQEIE--LQKKRQEEETFLRVQEE-------LQRLKELNNNEKAEKFQIFQELDQLQKE-- 747
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEKEDKALEikkqewkLEQLAADLSKYEQELYDLKEEYDRVEKEls 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 748 -KDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEKRDLEGIrE 810
Cdd:TIGR02169 487 kLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAVAKEAI-E 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 811 SLLRVKEARAG----------------GDEDG------------EELEKA---------QLRFFEFKRRQL--VKLVNLE 851
Cdd:TIGR02169 566 LLKRRKAGRATflplnkmrderrdlsiLSEDGvigfavdlvefdPKYEPAfkyvfgdtlVVEDIEAARRLMgkYRMVTLE 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 852 KDLVQQ-----------------KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESvtdVTEVPQDFEKIKPVEYRLQ 914
Cdd:TIGR02169 646 GELFEKsgamtggsraprggilfSRSEPAELQRLRERLEGLKRE---LSSLQSELRRI---ENRLDELSQELSDASRKIG 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 915 YKERQLQYLLQNH--LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQAT 983
Cdd:TIGR02169 720 EIEKEIEQLEQEEekLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAE 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 984 FEFTANIARQEEKVRKKEKEILESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQA 1062
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1063 SLEAEQEALEKDQERINAYIeEEVQRRLQDLhrvisegcSTSADTMKDNEKLHNGTIQrKLKYEKRQfcpawyLDPLLPR 1142
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQL-RELERKIEEL--------EAQIEKKRKRLSELKAKLE-ALEEELSE------IEDPKGE 942
|
650 660
....*....|....*....|...
gi 2287254621 1143 DATDTSSL-----IKEERREVDQ 1160
Cdd:TIGR02169 943 DEEIPEEElsledVQAELQRVEE 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
605-1093 |
3.89e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKrklIEEMEEKQKSDKAELERMQQEVETQRKETEivqlqirkqeeslkrrsfHIENKLKDLL 684
Cdd:PRK02224 241 EVLEEHEERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLE------------------ELEEERDDLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKFEEERLREQQEIELQKKRqEEETFLRVQEELQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:PRK02224 300 AEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAELESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 765 QEKEQVMLVAHLEEQLREKqemiqllrRGEVQWVEEEKRDLEGIRESLLrvkEARAGGDEDGEELEkaqlrffefkrrql 844
Cdd:PRK02224 378 AVEDRREEIEELEEEIEEL--------RERFGDAPVDLGNAEDFLEELR---EERDELREREAELE-------------- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 845 VKLVNLEKDlvqqkdilkkeVQEEQEILE---CLKCEHD-KESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQL 920
Cdd:PRK02224 433 ATLRTARER-----------VEEAEALLEagkCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 921 QYL--LQNHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekEEQLAQYQANANQLQKLQATFEFTANIARQEEKVR 998
Cdd:PRK02224 502 EDLveAEDRIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 999 KKEKEILESRE---KQQREALERALARLERRHSALQRHSTLgmeiEEQRQKLASLNSGSREQ--------SGLQASLEAE 1067
Cdd:PRK02224 571 REEVAELNSKLaelKERIESLERIRTLLAAIADAEDEIERL----REKREALAELNDERRERlaekrerkRELEAEFDEA 646
|
490 500
....*....|....*....|....*..
gi 2287254621 1068 Q-EALEKDQERINAYIeEEVQRRLQDL 1093
Cdd:PRK02224 647 RiEEAREDKERAEEYL-EQVEEKLDEL 672
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
615-1090 |
4.87e-09 |
|
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: 61.52 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 615 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKD-------LLAEK 687
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQtqqshayLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQrlKELNNNEKAEKFQIFQE-LDQLQKEKDEQYAKLElEKKRLEEQE 766
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ--ERINRARKAAPLAAHIKaVTQIEQQAQRIHTELQ-SKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 767 KEQVMLVAHLEEQLREKQEMIQLLRRGEV---QWVEEEK----------------RDLEGIRESLLRvKEARAGGDEDGE 827
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIhirDAHEVATsireiscqqhtltqhiHTLQQQKTTLTQ-KLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 828 ELEKAQLRFFEFKRRQL-VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESvtdvTEVPQDFEKI 906
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER----EQQLQTKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 907 KPVEYRLQyKERQLQYLLQNHLPTLLEEK-----QRAFEILDRGPLS--LDNTLYQVEKEMEEKEEQLAQYQANANQLQK 979
Cdd:TIGR00618 482 HLQETRKK-AVVLARLLELQEEPCPLCGScihpnPARQDIDNPGPLTrrMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 980 LQATFEF---TANIARQEEKVRKKEKEILESREKQQREALErALARLERRHSALQRHSTLGMEIEEQRQKLA-SLNSGSR 1055
Cdd:TIGR00618 561 LKEQMQEiqqSFSILTQCDNRSKEDIPNLQNITVRLQDLTE-KLSEAEDMLACEQHALLRKLQPEQDLQDVRlHLQQCSQ 639
|
490 500 510
....*....|....*....|....*....|....*
gi 2287254621 1056 EQSGLQASLEAEQEALEKDQERINAYIEEEVQRRL 1090
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
607-873 |
9.00e-09 |
|
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: 59.16 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhIENKLKDLLAE 686
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 687 KEKFeeerlreqqeiELQKKRQEEEtFLRVQEELQRLKELNNNEKAEKFQIFQELdqLQKEKDEQYAKLELEKKrlEEQE 766
Cdd:pfam13868 168 EEER-----------EAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEA--EKKA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 767 KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVK 846
Cdd:pfam13868 232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAA 308
|
250 260
....*....|....*....|....*..
gi 2287254621 847 LVNLEkdlVQQKDILKKEVQEEQEILE 873
Cdd:pfam13868 309 EREEE---LEEGERLREEEAERRERIE 332
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
609-941 |
1.21e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 609 FERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEV----ETQRKETEIVQLQIRKQEESlkrRSFHIENKLKDll 684
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeEARKAEDAKRVEIARKAEDA---RKAEEARKAED-- 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKFEEERLREQQEIELQKK---RQEEETflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyAKLELEKKR 761
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAedaRKAEAA--RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE--AKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 762 LEEQEKEQVMLVAHLE--------------EQLR---EKQEMIQLLRRGEVQWVEEEKRDLEGIResllRVKEARAGGDE 824
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFArrqaaikaeearkaDELKkaeEKKKADEAKKAEEKKKADEAKKKAEEAK----KADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 825 DGEELEKAQLRFFEFKRRQLVKLVNLEKdlvqQKDILKKEvQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFE 904
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEA----AADEAEAA-EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
330 340 350
....*....|....*....|....*....|....*..
gi 2287254621 905 KIKPVEYRLQYKERQLQYllQNHLPTLLEEKQRAFEI 941
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKK--ADEAKKKAEEKKKADEA 1436
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-833 |
1.37e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 619 KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfhienKLKDLLAEKEKfeeerlreq 698
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------KLQAEIAEAEA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 699 qeiELQKKRQEEETFLRVQEE--------------------LQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELE 758
Cdd:COG3883 80 ---EIEERREELGERARALYRsggsvsyldvllgsesfsdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 759 KKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 833
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1129 |
1.52e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQrEELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDl 683
Cdd:PTZ00121 1165 KAEEARKA-EDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKD- 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 684 lAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:PTZ00121 1239 -AEEAK------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 764 EQEK--EQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEF 839
Cdd:PTZ00121 1306 EAKKkaEEAKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 840 KRRQLVKLVNLEKDLVQQK---DILKKEVQEEQEILEC-LKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQY 915
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 916 KERQLQyllQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIAR 992
Cdd:PTZ00121 1466 AEEAKK---ADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 993 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLgMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALE 1072
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 1073 KDQERinayIEEEVQRRLQDLHRVISEGCSTSADTMKDNE--KLHNGTIQRKLKYEKRQ 1129
Cdd:PTZ00121 1622 AEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenKIKAAEEAKKAEEDKKK 1676
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
611-787 |
1.66e-08 |
|
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: 57.24 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKF 690
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 691 EEERLREQQE---------IELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:COG1579 79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|....*...
gi 2287254621 760 KRLEEQEKEqvmLVAHLEEQLREKQEMI 787
Cdd:COG1579 159 EELEAEREE---LAAKIPPELLALYERI 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-818 |
3.42e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVqlqiRKQEESLKRRSFHIENKLKDLLA 685
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLER 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 686 EkekfeeerlreqqeIELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:TIGR02168 832 R--------------IAATERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 764 EQEKEqvmlVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:TIGR02168 898 ELSEE----LRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQER 944
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
613-870 |
3.81e-08 |
|
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: 57.74 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 613 QREELEKLESKRKLIEEmEEKQKSDKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSFHI---ENKLKDLLAEKEK 689
Cdd:pfam15558 33 AWEELRRRDQKRQETLE-RERRLLLQQSQEQWQAEKEQRKARLG------REERRRADRREKQViekESRWREQAEDQEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 690 FEEERLREQQEIELQKKRQEEETfLRVQEE-LQRLKELNNNEKAEKFQI---------------FQELDQ---------- 743
Cdd:pfam15558 106 QRQEKLERARQEAEQRKQCQEQR-LKEKEEeLQALREQNSLQLQERLEEachkrqlkereeqkkVQENNLsellnhqark 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 744 ----LQKEKDEQYAKLELEKKRLEEQEK-EQVMLVAHLEEQLREKQEMIQLLRrgeVQWVEEEK-RDLEGIRESLLRVKE 817
Cdd:pfam15558 185 vlvdCQAKAEELLRRLSLEQSLQRSQENyEQLVEERHRELREKAQKEEEQFQR---AKWRAEEKeEERQEHKEALAELAD 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2287254621 818 ARAGGDEDGEELEKAQlrffefkRRQLVKLVNLEKDLVQQkdILKKEVQEEQE 870
Cdd:pfam15558 262 RKIQQARQVAHKTVQD-------KAQRARELNLEREKNHH--ILKLKVEKEEK 305
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
605-1099 |
5.39e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLeskrklIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIR----KQEESLKRRSFHIENKL 680
Cdd:COG4913 281 LRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 681 KDLLAEKEKFEEERLREQQEIELqkkrqEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKK 760
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 761 RLEEQ----EKEQVMLVAHLEEQLREKQ-------EMIQLlRRGEVQW----------------VEEE----------KR 803
Cdd:COG4913 430 SLERRksniPARLLALRDALAEALGLDEaelpfvgELIEV-RPEEERWrgaiervlggfaltllVPPEhyaaalrwvnRL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 804 DL------EGIRESLLRVKEARAGGD------------------------------EDGEELE------------KAQLR 835
Cdd:COG4913 509 HLrgrlvyERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRrhpraitragqvKGNGT 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 836 FFE-----FKRRQLV-------KLVNLEKDLVQqkdiLKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDF 903
Cdd:COG4913 589 RHEkddrrRIRSRYVlgfdnraKLAALEAELAE----LEEELAEAEERLE----ALEAELDALQERREALQRLAEYSWDE 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 904 EKIKPVEYRLQYKERQLQYLLQNH--LPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQ 981
Cdd:COG4913 661 IDVASAEREIAELEAELERLDASSddLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 982 ATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGsrEQSGLQ 1061
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREWPA--ETADLD 808
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2287254621 1062 ASLEA-----------EQEALEKDQERINAYIEEEVQRRLQDLHRVISE 1099
Cdd:COG4913 809 ADLESlpeylalldrlEEDGLPEYEERFKELLNENSIEFVADLLSKLRR 857
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-1091 |
8.08e-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: 57.76 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE---ESLKRRSFHIENKLKDLL 684
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVAQLELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEkfeeerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:TIGR02168 400 NEIE-----------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 765 QEKEQVMLVAHLEEQLREKQEMIQLLRRGE---------VQWVEEEKRDLEGIRE---SLLRV----------------- 815
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQenlegfsegVKALLKNQSGLSGILGvlsELISVdegyeaaieaalggrlq 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 816 -----------------KEARAGG-------DEDGEELEKAQLRFFEFKRRQLVKLVNLEK------------------- 852
Cdd:TIGR02168 549 avvvenlnaakkaiaflKQNELGRvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 853 -DLVQQKDILKKE-------------------------------VQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVP 900
Cdd:TIGR02168 629 dDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaktnssiLERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 901 QDFEKIKPVEYRLQYKERQLQyLLQNHLPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQ----LSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 981 QATFEFTANIARQEEKVRKKEKEILESREKQQREA---LERALARLERRHSALQRHST-LGMEIEEQRQKLASLNSgsrE 1056
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAATERRLEdLEEQIEELSEDIESLAA---E 860
|
570 580 590
....*....|....*....|....*....|....*
gi 2287254621 1057 QSGLQASLEAEQEALEKDQERINAYIEEEVQRRLQ 1091
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSE 895
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
605-1084 |
9.95e-08 |
|
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: 57.29 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQ---------------RKETEIV----------- 658
Cdd:TIGR00618 366 SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsafrdlqgqlaHAKKQQElqqryaelcaa 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 659 ----QLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERlreqqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEK 734
Cdd:TIGR00618 446 aitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE---------TRKKAVVLARLLELQEEPCPLCGSCIHPNPA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 735 FQIFQELDQLQK--EKDEQ-YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgeVQWVEEEKRDLEGIRES 811
Cdd:TIGR00618 517 RQDIDNPGPLTRrmQRGEQtYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL----TQCDNRSKEDIPNLQNI 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 812 LLRVKEaraggdeDGEELEKAQLRFFEFKRRQLVKLvnlEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 891
Cdd:TIGR00618 593 TVRLQD-------LTEKLSEAEDMLACEQHALLRKL---QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 892 SVTDVTEVP-QDFEKIKPVEYRLQYKERQLQY---------LLQNHLPTLLEEKQRAFEILDRGPLSL-------DNTLY 954
Cdd:TIGR00618 663 HALSIRVLPkELLASRQLALQKMQSEKEQLTYwkemlaqcqTLLRELETHIEEYDREFNEIENASSSLgsdlaarEDALN 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 955 QVEKEMEEKEEQLAQYQANANQ---------LQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLER 1025
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFnnneevtaaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 1026 RHSALQRHSTLGMEIEEQRQKLASLnsgsREQSGLQASLEAEQEALEKDQERINAYIEE 1084
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATLGEI----THQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
612-1091 |
1.60e-07 |
|
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: 56.72 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 612 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQEEslkrrsfhienklkdLLAEKEKFe 691
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLC---EEKNALQEQLQAETE---------------LCAEAEEM- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 692 eerlreqqEIELQKKRQEEETFL-----RVQEELQRLKELnNNEKAEKFQIFQELDQ-----------LQKEK------- 748
Cdd:pfam01576 63 --------RARLAARKQELEEILhelesRLEEEEERSQQL-QNEKKKMQQHIQDLEEqldeeeaarqkLQLEKvtteaki 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 749 ----------DEQYAKLELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMI-----QLLRRGEVQWVEEEK--RDL 805
Cdd:pfam01576 134 kkleedilllEDQNSKLSKERKLLEERISEFTSNLAEEEEkakslsKLKNKHEAMisdleERLKKEEKGRQELEKakRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 806 EG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFE--FKRRQLVK--------LVNLEKDLVQQKDILKKEVQE 867
Cdd:pfam01576 214 EGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEetAQKNNALKkireleaqISELQEDLESERAARNKAEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 868 EQ---EILECLKCE----HDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFE 940
Cdd:pfam01576 294 RRdlgEELEALKTEledtLDTTAAQQELRSKREQEVTELK------KALEEETRSHEAQLQEMRQKH-TQALEELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 941 ILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN-----------QLQKLQATFEFTANIARQEEKVRKKEKEILESRE 1009
Cdd:pfam01576 367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehkrkklegQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1010 KQQREAlERALARLERRHSAL--QRHSTLGMEIEEQRQKLA---SLNSGSREQSGLQASLEAEQEA-------------- 1070
Cdd:pfam01576 447 SLLNEA-EGKNIKLSKDVSSLesQLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEAkrnverqlstlqaq 525
|
570 580
....*....|....*....|....*.
gi 2287254621 1071 ---LEKDQERINAYIE--EEVQRRLQ 1091
Cdd:pfam01576 526 lsdMKKKLEEDAGTLEalEEGKKRLQ 551
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-1024 |
2.15e-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: 56.13 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 354 RAKNIINKPTINEDANVKLIRELRAEIARLKtlLAQGNQIALLDSPTALSMEEKLQQNEARVQELTK----EWTNKWNET 429
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGK--LTEEKEELEKQELKLLKDELELKKSEDLLKETQLvklqEQLELLLSR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 430 QNILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIG 509
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 510 GTVTLIPLSG--SQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSKSRENLS 587
Cdd:pfam02463 573 LPLGARKLRLliPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 588 AVMlynPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEE 667
Cdd:pfam02463 653 SLE---EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 668 SLKRRSFHIENKLKDLLAEKEKfeeerlreqQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE 747
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEE---------EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 748 KDEQyAKLELEKKRLEEQEKEQVmlvahLEEQLREKQEmiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGE 827
Cdd:pfam02463 801 EELR-ALEEELKEEAELLEEEQL-----LIEQEEKIKE-------------EELEELALELKEEQKLEKLAEEELERLEE 861
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 828 ELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKEsrLLEKHDESVTDVTEVPQDFEKIK 907
Cdd:pfam02463 862 EITKEEL-----LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL--LEEKENEIEERIKEEAEILLKYE 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 908 PVEYRLQYKERQLQYLLQNHLPTLLEEkqrafeildrgplsldntlyqvekemeekeEQLAQYQANANQLQKLQATFEFT 987
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEEER------------------------------NKRLLLAKEELGKVNLMAIEEFE 984
|
650 660 670
....*....|....*....|....*....|....*..
gi 2287254621 988 ANIARQEEKVRKKEKEILESREKQQREALERALARLE 1024
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
608-806 |
2.18e-07 |
|
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: 55.73 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETQRKETEivqLQIRKQEESLKRrsfhiENKLKDLLaEK 687
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLER-----AEKMREEL-EL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKfeeerLREQQEIELQKKRQEEETFLRVQEEL-QRLKELNNNEKAEKFQ--IFQELDQLQKEKDEQYA-KLELEKKRLE 763
Cdd:pfam15709 381 EQ-----QRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRKKQQEEAeRAEAEKQRQK 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2287254621 764 EQE----KEQVMLVAHLEEQ----LREKQEMIQllrrgEVQWVEEEKRDLE 806
Cdd:pfam15709 456 ELEmqlaEEQKRLMEMAEEErleyQRQKQEAEE-----KARLEAEERRQKE 501
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
611-988 |
3.24e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ------------EVETQRKETEIVQLQIRKQEESLKRrsfhIEN 678
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQ----LNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 679 KLKDLlaEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE-LQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLEL 757
Cdd:TIGR04523 343 QISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 758 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQlRF 836
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------ELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQ-KE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 837 FEFKRRQLVKLVNLEKDLVQQKDILKKEVQE---EQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrL 913
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---I 563
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 914 QYKERQLQYLLQNHlpTLLEEKQRAFEILdrgplsldntlyqvekemeekeeqLAQYQANANQLQKLQATFEFTA 988
Cdd:TIGR04523 564 DEKNKEIEELKQTQ--KSLKKKQEEKQEL------------------------IDQKEKEKKDLIKEIEEKEKKI 612
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
611-803 |
4.62e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETQRKETEIVQlQIRKQEESLKRR--SFHIENKLKDLLAEk 687
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 ekfeeerlreqqeieLQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG1340 169 ---------------LKELRKEAEEI---HKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
170 180 190
....*....|....*....|....*....|....*.
gi 2287254621 768 EQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
471-551 |
4.86e-07 |
|
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
Pssm-ID: 441322 [Multi-domain] Cd Length: 96 Bit Score: 49.57 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716 16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90
|
...
gi 2287254621 549 FRF 551
Cdd:COG1716 91 LRF 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
611-803 |
5.54e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETE----IVQLQIRKQEESLKRRSFHIENKLK----- 681
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelaELEKEIAELRAELEAQKEELAELLRalyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 682 ------DLLAEKEKFEEERLREQQEIELQKKRQEE-ETFLRVQEELQRLKELNNNEKAEKFQIFQE-------LDQLQKE 747
Cdd:COG4942 117 grqpplALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAEleeeraaLEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2287254621 748 KDEQYAKLELEKKRLEEQekeqvmlvahLEEQLREKQEMIQLLRRGEVQWVEEEKR 803
Cdd:COG4942 197 RQKLLARLEKELAELAAE----------LAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-1095 |
9.19e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrketeivqLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-----------AQLELQIASLNNEIERLEARLERLEDRR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFeeerlreQQEIELQKKRQEEETFLRVQEELQRLKelnnnekaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:TIGR02168 417 ERL-------QQEIEELLKKLEEAELKELQAELEELE--------------EELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 768 EQVMLVAHLeEQLREKQEMIQ-LLRRGE-----VQWVEEEKRDLEGIRE---SLLRVK-------EARAGGDED---GEE 828
Cdd:TIGR02168 476 ALDAAEREL-AQLQARLDSLErLQENLEgfsegVKALLKNQSGLSGILGvlsELISVDegyeaaiEAALGGRLQavvVEN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 829 LEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDkesrlLEKHDESVTDVtevpqdfekikp 908
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD-----LVKFDPKLRKA------------ 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 909 VEYRL----------QYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ 978
Cdd:TIGR02168 618 LSYLLggvlvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 979 KLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERrhsALQRHSTLGMEIEEQRQKLASLNSGSREQS 1058
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLEEAE 774
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2287254621 1059 GLQASLEAEQEALEKDQERINAYIE------EEVQRRLQDLHR 1095
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKalrealDELRAELTLLNE 817
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
451-554 |
9.60e-07 |
|
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: 49.61 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGRDDASTEQ-DIVLHGLDLESEHCI-----------FENIGGT-- 511
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2287254621 512 --VTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712 76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
720-1206 |
1.38e-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: 53.20 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 720 LQRLKELNNNEKAEKFQIFQElDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvAHLEEQ--LREKQEMIQLLRRGEVQW 797
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVE-RRRKLEEAEKARQ---AEMDRQaaIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 798 V--EEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEqeilecl 875
Cdd:pfam17380 353 IrqEERKRELERIRQEEIAMEISRM------RELERLQM-----ERQQKNERVRQELEAARKVKILEEERQRK------- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 876 kcehdkesrllekhdesvtdVTEVPQDFEKIKpveyRLQYKERQLQyllqnhLPTLLEEKQRAFEILDRgplsldntlyq 955
Cdd:pfam17380 415 --------------------IQQQKVEMEQIR----AEQEEARQRE------VRRLEEERAREMERVRL----------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 956 vekemeekeeqlaQYQANANQLQKLqatfeftaniaRQEEKVRKKEKEILESREKQQREALEralarlerrhsalQRHST 1035
Cdd:pfam17380 454 -------------EEQERQQQVERL-----------RQQEEERKRKKLELEKEKRDRKRAEE-------------QRRKI 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1036 LGMEIEEQRQKLAslnSGSREQSGLQASLEAEQEALEKDQERINA------YIEEEVQRRLQDLHRVISEGCSTSADTMK 1109
Cdd:pfam17380 497 LEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAeeerrkQQEMEERRRIQEQMRKATEERSRLEAMER 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1110 DNEKLHNGTIQRKLKYEKRQFCPAWYLDPLLPRDATDTSSLIKEER--REVDQNDHW--DHPMLWSvsgPKTTSSASQER 1185
Cdd:pfam17380 574 EREMMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHmiRFTTQSPEWatPSPATWN---PEWNTVTAEEE 650
|
490 500
....*....|....*....|.
gi 2287254621 1186 THQQRDQSSVPEVFQDSENKY 1206
Cdd:pfam17380 651 TPGIPIIHSQCQVNGECELKY 671
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
627-800 |
1.44e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.32 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 627 IEEMEEKQKSDkaELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKfeeerLREQQEIELQKK 706
Cdd:COG2433 382 LEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDE-----RIERLERELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 707 RQEEETFLRVQEELQRLKELNNNEKAEkfqifqeLDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLE----EQLRE 782
Cdd:COG2433 454 RSEERREIRKDREISRLDREIERLERE-------LEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEkftkEAIRR 526
|
170
....*....|....*...
gi 2287254621 783 KQEMIqLLRRGEVQWVEE 800
Cdd:COG2433 527 LEEEY-GLKEGDVVYLRD 543
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
605-764 |
2.35e-06 |
|
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: 49.27 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSfHIENKLKDLL 684
Cdd:pfam05672 23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE------RRREEEERQRK-AEEEAEEREQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKfeeerlreqqEIELQKKRQEEETFLRVQEELQRLkelnnnekaEKFQIFQELDQLQKEKdeqyakleleKKRLEE 764
Cdd:pfam05672 91 REQEE----------QERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER----------KKRIEE 141
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
611-940 |
3.66e-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: 51.07 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE-ESLKRRSFHIENK 679
Cdd:pfam13868 2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 680 LKDLLAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnnNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 759
Cdd:pfam13868 82 IEEREQKRQE------------EYEEKLQEREQMDEIVERIQE------EDQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 760 KRLEEQEKEQVMLVahlEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLrffEF 839
Cdd:pfam13868 144 ELEKEEEREEDERI---LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ---ER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 840 KRRQlvklvnLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESvtdvtEVPQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam13868 218 KERQ------KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFE-----RMLRKQAEDEEIEQEEAEKRRM 286
|
330 340
....*....|....*....|.
gi 2287254621 920 LQYLLQNHLPTLLEEKQRAFE 940
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRA 307
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
624-1094 |
5.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 624 RKLIEEMEEkqksdkaeLERMQQEVETQRKETEIVQlQIRKQEESLKRrsfhienkLKDLLAEKEKFEEERLREQQEIEL 703
Cdd:COG4913 228 DALVEHFDD--------LERAHEALEDAREQIELLE-PIRELAERYAA--------ARERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 704 QKKRQEEEtflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE----QYAKLELEKKRLEEQEKEQVMLVAHLEEQ 779
Cdd:COG4913 291 ELLEAELE---ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 780 LR-------EKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRffEFKRRQlvklVNLEK 852
Cdd:COG4913 368 LAalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIA--SLERRK----SNIPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 853 DLVQQKDILKK----------------EVQEEQEI----LEclKCEHDKESRLL--EKHDESVTD--------------- 895
Cdd:COG4913 441 RLLALRDALAEalgldeaelpfvgeliEVRPEEERwrgaIE--RVLGGFALTLLvpPEHYAAALRwvnrlhlrgrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 896 VTEVPQDFEKIKPVE----YRLQYKERQLQYLLQNHL-----------PTLLEEKQRA-------------FEILDRGPL 947
Cdd:COG4913 519 VRTGLPDPERPRLDPdslaGKLDFKPHPFRAWLEAELgrrfdyvcvdsPEELRRHPRAitragqvkgngtrHEKDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 948 S------LDNTlyqvekemeekeEQLAQYQANANQLQ----KLQATFEFTANIARQEEKVRKKEKEILESREKQQR-EAL 1016
Cdd:COG4913 599 RsryvlgFDNR------------AKLAALEAELAELEeelaEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1017 ERALARLERRHSALQRHS----TLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQRRLQD 1092
Cdd:COG4913 667 EREIAELEAELERLDASSddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
..
gi 2287254621 1093 LH 1094
Cdd:COG4913 747 LR 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
615-831 |
6.72e-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: 51.22 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 615 EELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 694
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 695 LREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyaklelekkrlEEQEKEQVMLVA 774
Cdd:TIGR02169 892 DELEAQLRELERKIEE-----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE------------DEEIPEEELSLE 954
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2287254621 775 HLEEQLREKQEMIQLLrrGEV-----QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK 831
Cdd:TIGR02169 955 DVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
610-873 |
7.36e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.81 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETQRKETEIVQLQIRKQEeslkrrsfhienKLKDLLAEKEK 689
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 690 feeerlreqqeielqKKRQEEETFLRVQEELQRlKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQ 769
Cdd:COG3064 78 ---------------KLAEAEKAAAEAEKKAAA-EKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 770 VMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVN 849
Cdd:COG3064 142 KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
250 260
....*....|....*....|....
gi 2287254621 850 LEKDLVQQKDILKKEVQEEQEILE 873
Cdd:COG3064 222 AARAAAASREAALAAVEATEEAAL 245
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
608-912 |
7.49e-06 |
|
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: 51.20 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEK----------QKSDKAELERMQQEVETQRKET-EIVQLQIRKQEESLKRRSFHI 676
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKimkldneikaLKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 677 ENKLKDLLAEKEKFEEERLreqqeiELQKKRQE---EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKD---E 750
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERR------LLNQEKTEllvEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFserQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 751 QYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEKRDLEGIRESLLRVKearaggdEDGE 827
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekKGLGRTIELKKEILEKKQEELKFVI-------KELQ 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 828 ELEKAQLRFFEFK---RRQLVKLVNLEKD-LVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD- 902
Cdd:TIGR00606 465 QLEGSSDRILELDqelRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDk 544
|
330
....*....|...
gi 2287254621 903 ---FEKIKPVEYR 912
Cdd:TIGR00606 545 mdkDEQIRKIKSR 557
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
605-1094 |
9.57e-06 |
|
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: 50.99 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQ-RKETEIVQLQIRKQEESLKRRSFHIENKLKDL 683
Cdd:pfam12128 380 RRSKIKEQNNRDIAGIKDKLAKIREARDRQL---AVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 684 LAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam12128 457 TATPE-------------LLLQLENFDERIERAREEQEA-----ANAEVERLQ--SELRQARKRRDQASEALRQASRRLE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 764 EQEKEqvmlVAHLEEQLREKQ-EMIQLLRRGEVQWVEEEKRDLEgiRESLLR---VKEARAGGDEDGEELEKAQLRffeF 839
Cdd:pfam12128 517 ERQSA----LDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVIS--PELLHRtdlDPEVWDGSVGGELNLYGVKLD---L 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 840 KRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpQDFEKIKPVEYRLQYKERQ 919
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQS 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 920 LQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNT----LYQVEKEMEEKEEQLAQY-----QANANQLQKLQATFE-FTAN 989
Cdd:pfam12128 665 EKDKKNKALAERKDSANERLNSLEAQLKQLDKKhqawLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAaRRSG 744
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 990 IARQEEKVRKKEKEILESRE---------KQQREALERALARLE-RRHSALQRH------------------STLGMEIE 1041
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGvdpdviaklKREIRTLERKIERIAvRRQEVLRYFdwyqetwlqrrprlatqlSNIERAIS 824
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 1042 EQRQKLASLNSGSREQsglQASLEAEQEALEKDQERINAYIE--EEVQRRLQDLH 1094
Cdd:pfam12128 825 ELQQQLARLIADTKLR---RAKLEMERKASEKQQVRLSENLRglRCEMSKLATLK 876
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
610-844 |
1.02e-05 |
|
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: 49.92 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESK-RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhiENKLKDLLAEKE 688
Cdd:pfam13868 108 ERIQEEDQAEAEEKlEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER----EAEREEIEEEKE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 689 KfEEERLREQQEIELQKKRQEEE-TFLRVQEELQ---RLKELNNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLEE 764
Cdd:pfam13868 184 R-EIARLRAQQEKAQDEKAERDElRAKLYQEEQErkeRQKEREEAEKKARQR--QELQQAREEQIELKERRLAEEAEREE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 765 QEKEQVMLV----AHLEEQLREKQEMIQLLRRGEVQWVEEEKRdlegiRESLLRVKEARAGGDEDGEELEKAQLRFFEFK 840
Cdd:pfam13868 261 EEFERMLRKqaedEEIEQEEAEKRRMKRLEHRRELEKQIEERE-----EQRAAEREEELEEGERLREEEAERRERIEEER 335
|
....
gi 2287254621 841 RRQL 844
Cdd:pfam13868 336 QKKL 339
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
576-1109 |
1.18e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 576 MTDLSKSRENL-SAVMLYNPGLFPIKGPICLRLEFERQQ---------REELEKLESK-RKLIEEMEEKQKSDKAELERM 644
Cdd:pfam05483 25 KSNLSKNGENIdSDPAFQKLNFLPMLEQVANSGDCHYQEglkdsdfenSEGLSRLYSKlYKEAEKIKKWKVSIEAELKQK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 645 QQEVETQRKETE-----IVQLQIRKQEESLKRRSFHIENklKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRvQEE 719
Cdd:pfam05483 105 ENKLQENRKIIEaqrkaIQELQFENEKVSLKLEEEIQEN--KDLIKENNATRHLCNLLKETCARSAEKTKKYEYER-EET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 720 LQRLKELNNNekAEKFQI-FQELdQLQKEKdeqyAKLELEKKRLEEQEKEQvmlvaHLEE----QLREKQEMIQLLRrge 794
Cdd:pfam05483 182 RQVYMDLNNN--IEKMILaFEEL-RVQAEN----ARLEMHFKLKEDHEKIQ-----HLEEeykkEINDKEKQVSLLL--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 795 VQWVEEEKRdlegIRESLLRVKEAR--AGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 872
Cdd:pfam05483 247 IQITEKENK----MKDLTFLLEESRdkANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 873 ECLKCE--HDKESRLLE------KHDESVTDVTEVPQDFEKIKPVE-YRLQYKERQLQYLlqnhlptLLEEKQRAFEild 943
Cdd:pfam05483 323 TKTICQltEEKEAQMEElnkakaAHSFVVTEFEATTCSLEELLRTEqQRLEKNEDQLKII-------TMELQKKSSE--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 944 rgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARL 1023
Cdd:pfam05483 393 ---------LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1024 ERRHSALQRHSTLGMEIEEQRQKLASLNSGS-----------REQSGLQASLEAEQEAL---EKDQERINAYIE--EEVQ 1087
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIELTAHCdklllenkeltQEASDMTLELKKHQEDIincKKQEERMLKQIEnlEEKE 543
|
570 580
....*....|....*....|..
gi 2287254621 1088 RRLQDLHRVISEGCSTSADTMK 1109
Cdd:pfam05483 544 MNLRDELESVREEFIQKGDEVK 565
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
613-768 |
1.22e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 613 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 692
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 693 ERLreqqeiELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:PRK12704 122 KQQ------ELEKKEEELEE--LIEEQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLikEIEEEAKEEADKK 189
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
706-1100 |
1.38e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 706 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQ-------ELDQLQKEKDeqyAKLELEKKRLEEQE--KEQVMLVAH- 775
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlqtKLQEMQMERD---AMADIRRRESQSQEdlRNQLQNTVHe 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 776 -------LEEQLREKQEMIQLLRRGEVQwveeEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLV 848
Cdd:pfam15921 154 leaakclKEDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 849 NLEKDLVQ--------QKDILKKEVQEEQEILecLKCEHDKESRLLEKHDESVTDVTEVPQDFE-KIKPVEYRLQYKERQ 919
Cdd:pfam15921 230 DTEISYLKgrifpvedQLEALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEKASSARsQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 920 LQ-----YLLQ--------NHLPTLLEEKQRAFEI----LDRGPLSLDNTLYQVEKEMEekeeQLAQYQANAN-QLQKLQ 981
Cdd:pfam15921 308 ARnqnsmYMRQlsdlestvSQLRSELREAKRMYEDkieeLEKQLVLANSELTEARTERD----QFSQESGNLDdQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 982 ATFE------------------------FTANIARQEEKVRKKEKEILESREKQQRE----ALERALARLERRHSALQRH 1033
Cdd:pfam15921 384 ADLHkrekelslekeqnkrlwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKV 463
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 1034 STLGMEIEEQRQKL-----------ASLNSGSREQSGLQASLEAEQEALEKDQERINAyIEEEVQRRLQDLHRVISEG 1100
Cdd:pfam15921 464 SSLTAQLESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEKERAIEATNAEITK-LRSRVDLKLQELQHLKNEG 540
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
605-938 |
1.46e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQEVETQ-------RKETEIVQLQIR---KQEESLKRRSF 674
Cdd:pfam10174 350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkinvlQKKIENLQEQLRdkdKQLAGLKERVK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 675 HIEN----------KLKDLLAEKEKFEEERLREqQEIELQKKRQEEETFlrvQEELQRLKELNNNEKAEKFQIFQELDQL 744
Cdd:pfam10174 426 SLQTdssntdtaltTLEEALSEKERIIERLKEQ-REREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 745 QK----------EKDEQYAKLE--LEKKRLEEQEKEQVMLVAH-LEEQLREKQEM---IQLLRRgEVQWVEEEKR----D 804
Cdd:pfam10174 502 KEhasslassglKKDSKLKSLEiaVEQKKEECSKLENQLKKAHnAEEAVRTNPEIndrIRLLEQ-EVARYKEESGkaqaE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 805 LEGIRESLLRVKEARAGGDEDGEELEKAQLRFFefkRRQLVKLVNLEkdLVQQKDiLKKEVQEEQEILECLKCEHDKESR 884
Cdd:pfam10174 581 VERLLGILREVENEKNDKDKKIAELESLTLRQM---KEQNKKVANIK--HGQQEM-KKKGAQLLEEARRREDNLADNSQQ 654
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2287254621 885 LleKHDESVTDVTEVPQDFEKIK----PVEYRLQYKERQLQYLLQN---HLPTLLEEKQRA 938
Cdd:pfam10174 655 L--QLEELMGALEKTRQELDATKarlsSTQQSLAEKDGHLTNLRAErrkQLEEILEMKQEA 713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
598-898 |
1.49e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 598 PIKG-PICLRLEFERQQREELE-KLESKRKLIEEMEEK--QKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRS 673
Cdd:PRK02224 460 PVEGsPHVETIEEDRERVEELEaELEDLEEEVEEVEERleRAEDLVEAED---RIERLEERREDLEELIAERRETIEEKR 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 674 FHIENKLK---DLLAEKEkfeeerlreqqeielQKKRQEEETFLRVQEELQRLKELNnnekAEKFQIFQELDQLQKEKDE 750
Cdd:PRK02224 537 ERAEELREraaELEAEAE---------------EKREAAAEAEEEAEEAREEVAELN----SKLAELKERIESLERIRTL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 751 QYAKLELEKKRLEEQEKEqvmlvAHLEEQLREKQEMIQLLRrgevqwveEEKRDLEG-IRESllRVKEARaggdEDGEEL 829
Cdd:PRK02224 598 LAAIADAEDEIERLREKR-----EALAELNDERRERLAEKR--------ERKRELEAeFDEA--RIEEAR----EDKERA 658
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287254621 830 EKAQLRFFEfkrrqlvKLvnleKDLVQQKDILKKE---VQEEQEILECLKCEHDkesRLLEKHD--ESVTDVTE 898
Cdd:PRK02224 659 EEYLEQVEE-------KL----DELREERDDLQAEigaVENELEELEELRERRE---ALENRVEalEALYDEAE 718
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
471-555 |
1.58e-05 |
|
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: 45.33 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87
|
....*..
gi 2287254621 549 FRFNHPK 555
Cdd:pfam16697 88 FCLVPAD 94
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
605-926 |
1.72e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKL--ESKRKLIEEMEEKQKsdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhienkLKD 682
Cdd:COG4372 13 LSLFGLRPKTGILIAAlsEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQ--------LEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 683 LLAEKEKfeeerlreqqeiELQKKRQEEEtflRVQEELQRLKElnnnekaEKFQIFQELDQLQKEK---DEQYAKLELEK 759
Cdd:COG4372 81 ELEELNE------------QLQAAQAELA---QAQEELESLQE-------EAEELQEELEELQKERqdlEQQRKQLEAQI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 760 KRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFE 838
Cdd:COG4372 139 AELQSEIAEREEELKELEEQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 839 FKRRQLVKL-----VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 913
Cdd:COG4372 219 ELLEAKDSLeaklgLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLL 298
|
330
....*....|...
gi 2287254621 914 QYKERQLQYLLQN 926
Cdd:COG4372 299 ALLLNLAALSLIG 311
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
607-940 |
2.28e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 607 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAE 686
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL----LEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 687 KEKFEEERLREQQEI--------ELQKKRQEEETFLRV---------------QEEL-QRLKELN--NNEKAEKFQIFQE 740
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDsvkeliikNLDNTRESLETQLKVlsrsinkikqnleqkQKELkSKEKELKklNEEKKELEEKVKD 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 741 LDQLQKEKDEQYAKLELEKKRLEEQ---------EKEQVMLVAHLEEQLREKQEMIqllrrgeVQWVEEEKRDLEGIRES 811
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKisdledelnKDDFELKKENLEKEIDEKNKEI-------EELKQTQKSLKKKQEEK 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 812 LLRVKEARAGGDEDGEELEK-----AQL-RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKcehDKESRL 885
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEkekkiSSLeKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR---NKWPEI 664
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 886 LEKHDESVTDVTEVPQDFEKIKPvEYRLQYKERQLQYLLQNHLPtLLEEKQRAFE 940
Cdd:TIGR04523 665 IKKIKESKTKIDDIIELMKDWLK-ELSLHYKKYITRMIRIKDLP-KLEEKYKEIE 717
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
614-924 |
2.39e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 614 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQrkETEIVQLQIR-----KQEESLKRRSFHIEN------KLKD 682
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT--NAEITKLRSRvdlklQELQHLKNEGDHLRNvqteceALKL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 683 LLAEKEKFeeerlreqqeIELQKKRQEEETFLRVQ----------EELQRLKELNNNEkaekfqifQELDQLQKEKDEQY 752
Cdd:pfam15921 556 QMAEKDKV----------IEILRQQIENMTQLVGQhgrtagamqvEKAQLEKEINDRR--------LELQEFKILKDKKD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 753 AKLELEKKRLEEQEKEQVMLVAHLEEQLRE----KQEMIQLLR-----RGEVQWVEEE----KRDLEGIRESL------- 812
Cdd:pfam15921 618 AKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNELNSLSEDyevlKRNFRNKSEEMetttnkl 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 813 -LRVKEARAggdedgeELEKAQ--LRFFEFKRRQLVKL-VNLEKDLVQQK---DILKKEVQ-EEQEILECLKCEH---DK 881
Cdd:pfam15921 698 kMQLKSAQS-------ELEQTRntLKSMEGSDGHAMKVaMGMQKQITAKRgqiDALQSKIQfLEEAMTNANKEKHflkEE 770
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2287254621 882 ESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 924
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
753-1084 |
2.51e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 753 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 833 QLRFFEFK---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpv 909
Cdd:TIGR02168 756 LTELEAEIeelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER---- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 910 eyRLQYKERQLQYLLQNhlptlLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTAN 989
Cdd:TIGR02168 832 --RIAATERRLEDLEEQ-----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 990 IARQEEKVrkKEKEILESREKQqrEALERALARLErrhsalqrhstlgMEIEEQRQKLASLNSGS-REQSGLQASLEAEQ 1068
Cdd:TIGR02168 905 ELESKRSE--LRRELEELREKL--AQLELRLEGLE-------------VRIDNLQERLSEEYSLTlEEAEALENKIEDDE 967
|
330
....*....|....*.
gi 2287254621 1069 EALEKDQERINAYIEE 1084
Cdd:TIGR02168 968 EEARRRLKRLENKIKE 983
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
608-835 |
3.71e-05 |
|
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: 49.02 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKL-------IEEMEEKQKsdKAELERMQQEVETQRKETEIVQLQ-----IRKQEESLKRRSFH 675
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLknkheamISDLEERLK--KEEKGRQELEKAKRKLEGESTDLQeqiaeLQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 676 IENKLKDLLAEKEKfeeerlREQQEIELQKK-RQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE----KDE 750
Cdd:pfam01576 241 KEEELQAALARLEE------ETAQKNNALKKiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtLDT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 751 QYAKLELEKKRleeqEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELe 830
Cdd:pfam01576 315 TAAQQELRSKR----EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL- 389
|
....*
gi 2287254621 831 KAQLR 835
Cdd:pfam01576 390 QAELR 394
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
604-1129 |
4.75e-05 |
|
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: 48.50 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 604 CLRLEFERQQREELEKLESKRKLIEEMEEKqksDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRS----FHIENK 679
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQL---NHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyFPNKKQ 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 680 LKDLLAEKEKfeeerlreqqeielqKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE-------KDEQy 752
Cdd:TIGR00606 575 LEDWLHSKSK---------------EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsQDEE- 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 753 AKLELEKKRLEEQEKEQVMLVA-------HLEEQLREKQEMIQLLRRgeVQWVEEEKRDLEGIRESLLRVKEARAggded 825
Cdd:TIGR00606 639 SDLERLKEEIEKSSKQRAMLAGatavysqFITQLTDENQSCCPVCQR--VFQTEAELQEFISDLQSKLRLAPDKL----- 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 826 gEELEKaQLRFFEFKRRQLVKLVNLEKDLVQQKDilkKEVQEEQEILECLKCEHDKESRLLEKHDESV------------ 893
Cdd:TIGR00606 712 -KSTES-ELKKKEKRRDEMLGLAPGRQSIIDLKE---KEIPELRNKLQKVNRDIQRLKNDIEEQETLLgtimpeeesakv 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 894 --TDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlptlleekqrafeildrgPLSLDNTLYQVEKEMEEKEEQLAQYQ 971
Cdd:TIGR00606 787 clTDVTIMERFQMELKDVERKIAQQAAKLQ------------------------GSDLDRTVQQVNQEKQEKQHELDTVV 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 972 ANANQLQKLQATfeftaniARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLN 1051
Cdd:TIGR00606 843 SKIELNRKLIQD-------QQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1052 SGSRE-QSGLQASLEAEQEALEKDQERINAyIEEEVQRR---LQDLHRVISEGCStsaDTMKDNEKLHNGTIQRKLKYEK 1127
Cdd:TIGR00606 916 TFLEKdQQEKEELISSKETSNKKAQDKVND-IKEKVKNIhgyMKDIENKIQDGKD---DYLKQKETELNTVNAQLEECEK 991
|
..
gi 2287254621 1128 RQ 1129
Cdd:TIGR00606 992 HQ 993
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
605-782 |
4.89e-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: 48.53 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLL 684
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-KKRKRL 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKFEEERLREQQEIELQKKRQEE------------ETFLRVQEELQRLKELNNneKAEkfQIFQELDQLQKEKDEQY 752
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRALEPVNM--LAI--QEYEEVLKRLDELKEKR 995
|
170 180 190
....*....|....*....|....*....|
gi 2287254621 753 AKLELEKKRLEEqekeqvmLVAHLEEQLRE 782
Cdd:TIGR02169 996 AKLEEERKAILE-------RIEEYEKKKRE 1018
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
602-891 |
5.04e-05 |
|
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: 48.50 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 602 PICLR-LEFERQQREELEKLESKRKL----IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHI 676
Cdd:TIGR00606 681 PVCQRvFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 677 EnKLKDLLAEKEKfeeERLREQQEIELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQI-----FQELDQLQKEKDE 750
Cdd:TIGR00606 761 Q-RLKNDIEEQET---LLGTIMPEEESAKVCLTDVTIMeRFQMELKDVERKIAQQAAKLQGSdldrtVQQVNQEKQEKQH 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 751 QY----AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvQWVEEEKRDLEGIRESLLRVKEARAGGDEDG 826
Cdd:TIGR00606 837 ELdtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-QFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 827 EELEKAQLRffefkRRQLVKLVNLEKDLVQQK-DILKKEVQEEQEILECL--KCEHDKESRLLEKHDE 891
Cdd:TIGR00606 916 TFLEKDQQE-----KEELISSKETSNKKAQDKvNDIKEKVKNIHGYMKDIenKIQDGKDDYLKQKETE 978
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
607-869 |
5.11e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.20 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 607 LEFERQQREELEKleSKRKLIEEMEEKQKSDKAELERMQQevetqRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 686
Cdd:pfam05557 43 LDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRL-----KKKYLEALNKKLNEKESQLADAREVISCLKNELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 687 kekfeeerlreqqeieLQKKRQEEETFLRVQE-ELQRLKELNNNEKA------EKFQIFQELDQLQKEKDEQYAKLELEk 759
Cdd:pfam05557 116 ----------------LRRQIQRAELELQSTNsELEELQERLDLLKAkaseaeQLRQNLEKQQSSLAEAEQRIKELEFE- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 760 krLEEQE---------KEQVMLVAHLEEQLREKQEMIQLLR--RGEVQWVEEEKrdlEGIRESLLRVKEARAGGDEDGEE 828
Cdd:pfam05557 179 --IQSQEqdseivknsKSELARIPELEKELERLREHNKHLNenIENKLLLKEEV---EDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254621 829 LEKAQLRFFEFK----------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQ 869
Cdd:pfam05557 254 KEKLEQELQSWVklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLE 310
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
608-890 |
5.19e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRK----ETEIVQLQIRKQEESLKRRsfhienkLKDL 683
Cdd:pfam02029 10 ERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQggldEEEAFLDRTAKREERRQKR-------LQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 684 LAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNN--------NEKAEKFQIFQELDQLQKEKDEQYAKL 755
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRykeeeteiREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 756 ELEKKRLEEQE--KEQVMLVAHLEEqLREKQEMIQLLRRGEV------QWVEEEKRDLEGIRESLLRVKEARAGGDEDGE 827
Cdd:pfam02029 163 SEEAEEVPTENfaKEEVKDEKIKKE-KKVKYESKVFLDQKRGhpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2287254621 828 ELEKAQLRfFEFKRRQLVKLVNLEKDLVQQKdilkkevQEEQEI-LECLKCEHDKESRLLEKHD 890
Cdd:pfam02029 242 VFLEAEQK-LEELRRRRQEKESEEFEKLRQK-------QQEAELeLEELKKKREERRKLLEEEE 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
676-820 |
6.05e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 676 IENKLKDLLAEKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQ--LQKEK--DEQ 751
Cdd:PRK12704 36 AEEEAKRILEEAKK------------EAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKEEnlDRK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 752 YAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLrrgevqwVEEEKRDLEGIreSLLRVKEARA 820
Cdd:PRK12704 102 LELLEKREEELEKKEKE----LEQKQQELEKKEEELEEL-------IEEQLQELERI--SGLTAEEAKE 157
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
703-908 |
6.28e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlvahLEEQLR 781
Cdd:pfam05262 183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 782 EKQemiQLLRRGEVQWVEEEKRDLEgiresllrvkearaggdEDGEELEKAQLrffEFKRrqlvKLVNLEKDLVQQKDIL 861
Cdd:pfam05262 256 EAK---NLPKPADTSSPKEDKQVAE-----------------NQKREIEKAQI---EIKK----NDEEALKAKDHKAFDL 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2287254621 862 KKEVQEEQEILEclkcehdkesrllEKHDESVTDVTEVPQDFEKIKP 908
Cdd:pfam05262 309 KQESKASEKEAE-------------DKELEAQKKREPVAEDLQKTKP 342
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
799-1130 |
6.31e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 799 EEEKRDLEGIRESLLRVKEARaggdedgEELEKaQLRFFEFKRRQLVKLVNLEKDLVQ-QKDILKKEVQEEQEILECLKc 877
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDIL-------NELER-QLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQ- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 878 ehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLpTLLEEKQRAFEILDRGPLSLDNTLYQVE 957
Cdd:TIGR02168 246 --EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-NEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 958 KEMEEKEEQLAQYQANANQLQKLQATfeftaniarqeekvrkkekeiLESREKQQREALERALARLERRHSALQrhstlg 1037
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEE---------------------LKEELESLEAELEELEAELEELESRLE------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1038 mEIEEQRQKLASLNSGSREQsglQASLEAEQEALEKDQERINAYIE------EEVQRRLQDLHRVISEGCSTSADTMKDN 1111
Cdd:TIGR02168 376 -ELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRErlqqeiEELLKKLEEAELKELQAELEELEEELEE 451
|
330
....*....|....*....
gi 2287254621 1112 EKLHNGTIQRKLKYEKRQF 1130
Cdd:TIGR02168 452 LQEELERLEEALEELREEL 470
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
605-914 |
6.88e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLEsKRKLIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRSFHIEN----- 678
Cdd:COG5185 213 GNLGSESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDKLEkLVEQNTDLRLEKLGENAESSKRLNENANNlikqf 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 679 -KLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE----LQRLKELNNNE-----------KAEKFQIFQELD 742
Cdd:COG5185 292 eNTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKREtetgIQNLTAEIEQGqesltenleaiKEEIENIVGEVE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 743 QLQKEKDEQYAKLELEKKRLE------EQEKEQVMLVAHLEEQLREKQEMIQLLRR---GEVQWVEEEKRDLEGIRESLL 813
Cdd:COG5185 372 LSKSSEELDSFKDTIESTKESldeipqNQRGYAQEILATLEDTLKAADRQIEELQRqieQATSSNEEVSKLLNELISELN 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 814 RVKEaraggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQqkdiLKKEVQEEQEILECLKcehDKESRLLEKHDESV 893
Cdd:COG5185 452 KVMR-----EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQ----IESRVSTLKATLEKLR---AKLERQLEGVRSKL 519
|
330 340
....*....|....*....|.
gi 2287254621 894 TDVTEVPQDFEKIKPVEYRLQ 914
Cdd:COG5185 520 DQVAESLKDFMRARGYAHILA 540
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
611-867 |
8.88e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELekleskRKLIEEMEEKQKSDKAELERMQ-QEVETQRKETEIVQ-----LQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:COG5022 806 LGSRKEY------RSYLACIIKLQKTIKREKKLREtEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 685 AEKEKF-------------EEERLREQQEIELQKKRQE---EETFLRVqEELQRLKELNNNEKAEkfqifqELDQLQKEK 748
Cdd:COG5022 880 AERQLQelkidvksisslkLVNLELESEIIELKKSLSSdliENLEFKT-ELIARLKKLLNNIDLE------EGPSIEYVK 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 749 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDedgeE 828
Cdd:COG5022 953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQESTKQLKELPVEVA----E 1027
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2287254621 829 LEKAQLRFFE--FKRRQLVKLVNLEKDLVQQKDILKKEVQE 867
Cdd:COG5022 1028 LQSASKIISSesTELSILKPLQKLKGLLLLENNQLQARYKA 1068
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
606-895 |
1.00e-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: 47.20 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE------------ 666
Cdd:pfam07888 68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvle 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 667 -----ESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEI-----ELQKKR----QEEETFLRVQEELQRLKELNNN--- 729
Cdd:pfam07888 148 retelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslskEFQELRnslaQRDTQVLQLQDTITTLTQKLTTahr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 730 EKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE-QLREKQEMIQL------LRRGEVQW----- 797
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQLTLQLadaslaLREGRARWaqere 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 798 -----VEEEKRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKeVQEEQEIL 872
Cdd:pfam07888 308 tlqqsAEADKDRIEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV-AQKEKEQL 383
|
330 340
....*....|....*....|...
gi 2287254621 873 ECLKCEHDKESRLLEKHDESVTD 895
Cdd:pfam07888 384 QAEKQELLEYIRQLEQRLETVAD 406
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
623-768 |
1.34e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 44.88 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 623 KRKLIEEMEEKQKSdKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKlKDLLAEKEKfeeerlrEQQEIE 702
Cdd:pfam12072 52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKK-EESLEKKEK-------ELEAQQ 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 768
Cdd:pfam12072 120 QQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL--LDEVEEELRHEAAVMikEIEEEAKEEADKK 185
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
622-894 |
1.42e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 622 SKRKLIEEMEEKQKSDKAELERMQQEVETQRKEteivqlqIRKQEESLKRRSFHIENKLKDLLAEKEkfeeerlreqqei 701
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQ------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 702 ELQKKRQEeetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE------QYAKLELEKKRLE----------EQ 765
Cdd:COG1340 61 ELREKRDE------LNEKVKELKEERDELNEKLNELREELDELRKELAElnkaggSIDKLRKEIERLEwrqqtevlspEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 766 EKEQVMLVAHLEEQLREKQEMiqllrrgevqwvEEEKRDLEGIRESLLRVK-EARAGGDEDGEELEKAQLrffefKRRQL 844
Cdd:COG1340 135 EKELVEKIKELEKELEKAKKA------------LEKNEKLKELRAELKELRkEAEEIHKKIKELAEEAQE-----LHEEM 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2287254621 845 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT 894
Cdd:COG1340 198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
608-763 |
1.63e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetqRKETEIVQLQIRKQE-ESLKRRSFHIENKLKDLLAE 686
Cdd:pfam17380 447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKE 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 687 KEKFEEERLREQQEIELQKKR---QEEETFLRVQEELQRLKElnnnEKAekfqifqELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERrkqQEMEERRRIQEQMRKATE----ERS-------RLEAMEREREMMRQIVESEKARAE 590
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
614-941 |
1.81e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 614 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKFEEe 693
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN----TQTQLNQLKDEQNKIKK- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 694 rlreqqeiELQKKRQEeetflrVQEELQRLKELNNNEKaekfQIFQELDQLQKEKDEQYAKlELeKKRLEEQEKEqvmlV 773
Cdd:TIGR04523 268 --------QLSEKQKE------LEQNNKKIKELEKQLN----QLKSEISDLNNQKEQDWNK-EL-KSELKNQEKK----L 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 774 AHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRrqlv 845
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNE-QISQLKKELTNSESensekqreLEEKQNEIEKLKKENQSYKQEIKNLESQINDLES---- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 846 KLVNLEKdLVQQKDILKKEVQEEQEILEclkCEHDKESRLLEKHDESVTDVTEVPQDFE-KIKPVEYRLQYKERQLQYLL 924
Cdd:TIGR04523 399 KIQNQEK-LNQQKDEQIKKLQQEKELLE---KEIERLKETIIKNNSEIKDLTNQDSVKElIIKNLDNTRESLETQLKVLS 474
|
330
....*....|....*....
gi 2287254621 925 Q--NHLPTLLEEKQRAFEI 941
Cdd:TIGR04523 475 RsiNKIKQNLEQKQKELKS 493
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
716-1092 |
1.97e-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: 45.68 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 716 VQEELQRLKELN--------NNEKAEKFQIFQELDQLQKEKDEQYAKLeLEKKRLEEQEKEQVMLVAHLEEQLREKQEMI 787
Cdd:pfam13868 1 LRENSDELRELNskllaakcNKERDAQIAEKKRIKAEEKEEERRLDEM-MEEERERALEEEEEKEEERKEERKRYRQELE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 788 QLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLRFFEFKR-RQLVKLVNLEKDLVQQKDIlKKEVQ 866
Cdd:pfam13868 80 EQIEEREQKRQEEYEEKLQEREQMDEIVERIQE------EDQAEAEEKLEKQRQlREEIDEFNEEQAEWKELEK-EEERE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 867 EEQEILECLKcehDKESRLLEKHDESvtdvtevpqdfekikpveyRLQYKERQLqylLQNHLPTLLEEKQRAFEILDRgp 946
Cdd:pfam13868 153 EDERILEYLK---EKAEREEEREAER-------------------EEIEEEKER---EIARLRAQQEKAQDEKAERDE-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 947 lsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATF-EFTANIARQEEKVRKKEKEILESREKQQREALERALARLER 1025
Cdd:pfam13868 206 --LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAReEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 1026 RHSALQRHST-LGMEIEEQRQKlaslnsgsREQSglQASLEAEQEALEKDQERINAYIEEEVQRRLQD 1092
Cdd:pfam13868 284 RRMKRLEHRReLEKQIEEREEQ--------RAAE--REEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
551-820 |
2.34e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 551 FNHPKEAAKLREKRKSgllssfslsMTDLSKSRENLSAVMLYNPGLFPIKGPICLR--LEFERQQREELEKLESKrklIE 628
Cdd:PRK05771 36 LKEELSNERLRKLRSL---------LTKLSEALDKLRSYLPKLNPLREEKKKVSVKslEELIKDVEEELEKIEKE---IK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 629 EMEEKqksdKAELERMQQEVETQRKETEI-----VQLQIRKQEESLKRRSFHI-ENKLKDLLAEKEKFEEERLREQQE-- 700
Cdd:PRK05771 104 ELEEE----ISELENEIKELEQEIERLEPwgnfdLDLSLLLGFKYVSVFVGTVpEDKLEELKLESDVENVEYISTDKGyv 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 701 --IELQKKRQEEEtflrVQEELQRLkELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE 778
Cdd:PRK05771 180 yvVVVVLKELSDE----VEEELKKL-GFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2287254621 779 QL---REKQEM-IQLLRRGEV----QWVEEEkrDLEGIRESLLRVKEARA 820
Cdd:PRK05771 255 YLeieLERAEAlSKFLKTDKTfaieGWVPED--RVKKLKELIDKATGGSA 302
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
608-786 |
2.45e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhiENKLKDLLAEK 687
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---GEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEeTFLRVQEELQRLKELNNNE----KAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEfeklRQKQQEAELELEELKKKREERRKLLEEEEQRRK 301
|
170 180
....*....|....*....|...
gi 2287254621 764 EQEKEQvmLVAHLEEQLREKQEM 786
Cdd:pfam02029 302 QEEAER--KLREEEEKRRMKEEI 322
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
703-821 |
2.66e-04 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 43.52 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 703 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAhlEEQLRE 782
Cdd:pfam11600 18 LEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLK--EEKRKE 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 2287254621 783 KQEMIQlLRRGEVQWVEEEKRdlegIRESLLRVKEARAG 821
Cdd:pfam11600 96 KQEALE-AKLEEKRKKEEEKR----LKEEEKRIKAEKAE 129
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
624-788 |
2.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 624 RKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQlqirkQEESLKRRSfHIENKLKDLLAEkekfeeerlreQQEIEl 703
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEA-----KEEIHKLRN-EFEKELRERRNE-----------LQKLE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEE-----QEKEQVMLVAHLEE 778
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERisgltAEEAKEILLEKVEE 165
|
170
....*....|.
gi 2287254621 779 QLR-EKQEMIQ 788
Cdd:PRK12704 166 EARhEAAVLIK 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
704-888 |
2.94e-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: 45.14 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 704 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE---QYAKLELEKKRLEEQEKEQVMLVAHLEEQL 780
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 781 REKQEMI--------------------------QLLRRGEV--QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkA 832
Cdd:COG4942 100 EAQKEELaellralyrlgrqpplalllspedflDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELE-A 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2287254621 833 QLRFFEFKRRQLVKLVNLEKDLVQQkdiLKKEVQEEQEILECLKCEHDKESRLLEK 888
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
615-1084 |
3.41e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 615 EELEKLESKRKLI--EEMEEKQKSDK--AELERMQQEVETQR-----KETEIVQL--QIRKQEESLKRRSFHIENKLKDL 683
Cdd:TIGR04523 75 NKIKILEQQIKDLndKLKKNKDKINKlnSDLSKINSEIKNDKeqknkLEVELNKLekQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 684 LAEKEKFEeerlreqqeiELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQKeKDEQYAKLELEKKRL 762
Cdd:TIGR04523 155 EKLNNKYN----------DLKKQKEELENELnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 763 EEQEKEqvmlvahLEEQLREKQEMIQllrrgevqwveEEKRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRr 842
Cdd:TIGR04523 224 KKQNNQ-------LKDNIEKKQQEIN-----------EKTTEISNTQTQLNQLKDEQ---NKIKKQLSEKQKELEQNNK- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 843 qlvKLVNLEKDLVQQK-DILKKEVQEEQEILECLKCEHDKESRLLE-------KHDESVTDVTEVPQDFEK-IKPVEYRL 913
Cdd:TIGR04523 282 ---KIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEeiqnqisQNNKIISQLNEQISQLKKeLTNSESEN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 914 QYKERQLQYLlQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQK----LQATFEF 986
Cdd:TIGR04523 359 SEKQRELEEK-QNEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKeierLKETIIK 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 987 TANIARQEEKVRKKEKEILESRE------KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGL 1060
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDntreslETQLKVLSRSINKIKQNLEQKQK------ELKSKEKELKKLNEEKKELEEK 511
|
490 500
....*....|....*....|....
gi 2287254621 1061 QASLEAEQEALEKDQERINAYIEE 1084
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKE 535
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
478-543 |
3.62e-04 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 40.25 E-value: 3.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498 1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
608-872 |
3.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKEteivQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE----RQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRL-KELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK-KRLEEQ 765
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELlKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDsLEAKLG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 766 EKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLV 845
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
250 260
....*....|....*....|....*..
gi 2287254621 846 KLVNLEKDLVQQKDILKKEVQEEQEIL 872
Cdd:COG4372 313 LEDALLAALLELAKKLELALAILLAEL 339
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
473-551 |
3.70e-04 |
|
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: 41.43 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 473 LKEGQTYVGRDDASteqDIVLHGLDLESEHC-IFENIGGTVTLIPLSGS-QCSVNGVQIVEATHLNQGAVILLGrTNMFR 550
Cdd:cd22673 18 LTKKSCTFGRDLSC---DIRIQLPGVSREHCrIEVDENGKAYLENLSTTnPTLVNGKAIEKSAELKDGDVITIG-GRSFR 93
|
.
gi 2287254621 551 F 551
Cdd:cd22673 94 F 94
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
623-910 |
3.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 623 KRKLIEEMEEKQKSDKA-ELERMQQEVETQRKETEivqlqIRKQEESLKRRSFHIENKLKDLLAEKEKfeeerlreqqei 701
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDfDFDAKEDNRADEATEEA-----FGKAEEAKKTETGKAEEARKAEEAKKKA------------ 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 702 elQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEEQEKEQVMLVAhleEQLR 781
Cdd:PTZ00121 1125 --EDARKAEEA--RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE---DAKKAEAARKAEEVRKA---EELR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 782 EKQEM--IQLLRRGEVQWVEEEKRDLEGIR--ESLLRVKEARaggdEDGEELEKAQ--LRFFEFKRRQLVKLVNLEKDLV 855
Cdd:PTZ00121 1195 KAEDArkAEAARKAEEERKAEEARKAEDAKkaEAVKKAEEAK----KDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQA 1270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 856 QQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVE 910
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
621-772 |
4.23e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 621 ESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEiVQLQIRKQEESLKRRSFHIENklkdllAEKEKFEEERLREQQE 700
Cdd:pfam02029 206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE-VFLEAEQKLEELRRRRQEKES------EEFEKLRQKQQEAELE 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2287254621 701 IELQKKRQEEETFLRVQEELQRlkelnNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVML 772
Cdd:pfam02029 279 LEELKKKREERRKLLEEEEQRR-----KQEEAER--------KLREEEEKRRMKEEIERRRAEAAEKRQKLP 337
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
618-861 |
5.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 618 EKLESKRKLIEEMEEKQKSDKAELERMqqeVETQRKETEivqlQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 697
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNK---YDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 698 QQEIELQKKrqeEETFLRVQEE----LQRLKElnNNEKAEKfqIFQELDQLQKekdeqyaKLELEKKRLEEQEKeqvmlv 773
Cdd:PHA02562 268 KSKIEQFQK---VIKMYEKGGVcptcTQQISE--GPDRITK--IKDKLKELQH-------SLEKLDTAIDELEE------ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 774 ahLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVK----EARAGGDEDGEELEKAQlrffefkrRQLVKLVN 849
Cdd:PHA02562 328 --IMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKaaieELQAEFVDNAEELAKLQ--------DELDKIVK 393
|
250
....*....|..
gi 2287254621 850 LEKDLVQQKDIL 861
Cdd:PHA02562 394 TKSELVKEKYHR 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
617-942 |
5.44e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 617 LEKLESKRKL----IEEMEEKQKSDKAELERMQQEV-----ETQRKETEIVQL-------------------QIRKQEES 668
Cdd:TIGR04523 206 LKKKIQKNKSlesqISELKKQNNQLKDNIEKKQQEInekttEISNTQTQLNQLkdeqnkikkqlsekqkeleQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 669 LKRRSFHIENKLKDLlaEKEKFEEERLREQQEIELQKK---------RQEEETFLRVQEELQRLK------ELNNNEKAE 733
Cdd:TIGR04523 286 LEKQLNQLKSEISDL--NNQKEQDWNKELKSELKNQEKkleeiqnqiSQNNKIISQLNEQISQLKkeltnsESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 734 KF-QIFQELDQLQKEKD---EQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQ-------EMIQLLR------RGEVQ 796
Cdd:TIGR04523 364 ELeEKQNEIEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekelleKEIERLKetiiknNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 797 WVEEEKRDLEGIRESLLRVKEARAGGDEDGE--------ELEKAQlRFFEFKRRQLVKLVNLEKDLVQQKDILKKEV--- 865
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqNLEQKQ-KELKSKEKELKKLNEEKKELEEKVKDLTKKIssl 522
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254621 866 QEEQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrLQYKERQLQYLLQNHlpTLLEEKQRAFEIL 942
Cdd:TIGR04523 523 KEKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---IDEKNKEIEELKQTQ--KSLKKKQEEKQEL 590
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
618-818 |
5.51e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 618 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 697
Cdd:cd16269 87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 698 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLv 773
Cdd:cd16269 155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQK- 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2287254621 774 ahLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 818
Cdd:cd16269 228 --LEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
608-713 |
5.93e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
90 100
....*....|....*....|....*.
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEETF 713
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGF 248
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
610-867 |
7.06e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQ--LQIRKQEESLKRRSfhieNKLKDLLAEK 687
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRaiLESYDKELTMSNYS----PQLLERIEEA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEETFLRVQE------ELQRLKElnNNEKAEKFQIFQELDQLQKEKDEqyakLELEKKR 761
Cdd:pfam05557 386 EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtlerELQALRQ--QESLADPSYSKEEVDSLRRKLET----LELERQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 762 LEEQEKEQVMLVAHLEeqLREKQEM-----IQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRF 836
Cdd:pfam05557 460 LREQKNELEMELERRC--LQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETT 537
|
250 260 270
....*....|....*....|....*....|....*
gi 2287254621 837 FEFKRRQLVKL----VNLEKDLVQQKDILKKEVQE 867
Cdd:pfam05557 538 STMNFKEVLDLrkelESAELKNQRLKEVFQAKIQE 572
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
607-790 |
8.95e-04 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 42.45 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 607 LEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESL---KRRSFHIEN 678
Cdd:pfam14988 6 LEYLAKKTEEKQKKIEKlwnqyVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALrpfAKLKESQER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 679 KLKDLLAEKEKFEEERLREQQEIELQkkRQEEETFLRVQEELQRLKEL---NNNEKAEKFQ----------------IFQ 739
Cdd:pfam14988 86 EIQDLEEEKEKVRAETAEKDREAHLQ--FLKEKALLEKQLQELRILELgerATRELKRKAQalklaakqalsefcrsIKR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2287254621 740 ELDQLQKE---KDEQYAKLELEKKRLEEQEKeqvmlvahleeQLREKQEMIQLL 790
Cdd:pfam14988 164 ENRQLQKEllqLIQETQALEAIKSKLENRKQ-----------RLKEEQWYLEAL 206
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
605-1084 |
1.12e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERM---------------------------QQEV--------- 648
Cdd:pfam10174 209 IHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNirdledevqmlktngllhtedreeeikQMEVykshskfmk 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 649 --------ETQRKETEIVQLQIR-----KQEESLKRrsfHIEnKLKDLLAEKEKfeEERLREQQEIELQKKRQEEETFL- 714
Cdd:pfam10174 289 nkidqlkqELSKKESELLALQTKletltNQNSDCKQ---HIE-VLKESLTAKEQ--RAAILQTEVDALRLRLEEKESFLn 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 715 RVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAKLELEKKRLEeqekeqvmlvaHLEEQLREKQEMIQLLRRGe 794
Cdd:pfam10174 363 KKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIE-----------NLQEQLRDKDKQLAGLKER- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 795 vqwVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQE-EQEILE 873
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEkESSLID 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 874 CLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQyKERQLQY-------------LLQNHLPTLLEEKQRAFE 940
Cdd:pfam10174 501 LKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLK-KAHNAEEavrtnpeindrirLLEQEVARYKEESGKAQA 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 941 ILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeFTANI-ARQEEKVRKKEKEILESREKQQREALERA 1019
Cdd:pfam10174 580 EVER----LLGILREVENEKNDKDKKIAELESLTLRQMKEQNK--KVANIkHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1020 LARLERRHSALQRHStlgMEIEEQRQKLASLNSGSREQSGLQASLEAE-----QEALEKDQERINAYIEE 1084
Cdd:pfam10174 654 QLQLEELMGALEKTR---QELDATKARLSSTQQSLAEKDGHLTNLRAErrkqlEEILEMKQEALLAAISE 720
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
605-807 |
1.17e-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: 43.94 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQRE---ELEKLESKRKLIEEMEEKQKSDKAELER----MQQEVETQRKETEIVQ-----LQIRKQEESLKRR 672
Cdd:pfam05483 553 VREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENkcnnLKKQIENKNKNIEELHqenkaLKKKGSAENKQLN 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 673 SFHIE-NKLK-DLLAEKEKFEEERLREQQEIELQKKRQE------EETFLRVQEELQRLKELnnnEKAEKFQIFQELDQL 744
Cdd:pfam05483 633 AYEIKvNKLElELASAKQKFEEIIDNYQKEIEDKKISEEklleevEKAKAIADEAVKLQKEI---DKRCQHKIAEMVALM 709
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2287254621 745 QKEKdEQYAKLELEKKR----LEEQEKEQVMLVAHLEEQLRE-KQEMIQLLRRGEVQWVEEEKRDLEG 807
Cdd:pfam05483 710 EKHK-HQYDKIIEERDSelglYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
608-764 |
1.30e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKEteivqlqiRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE--------LAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNN--------NEKAEkfqifQELDQLQKEKD---EQYAKLE 756
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEReiealgpvNLLAI-----EEYEELEERYDflsEQREDLE 808
|
....*...
gi 2287254621 757 LEKKRLEE 764
Cdd:COG1196 809 EARETLEE 816
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
909-1091 |
1.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 909 VEYRLQYKERQLQY---LLQNHLPTL---LEEKQRAFEILDR--GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:COG3206 162 LEQNLELRREEARKaleFLEEQLPELrkeLEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 981 QATFEftANIARQEEKVRKKEKEILESREKQQREALERALARLERR----HSALQRhstLGMEIEEQRQKLAS-----LN 1051
Cdd:COG3206 242 LAALR--AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnHPDVIA---LRAQIAALRAQLQQeaqriLA 316
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2287254621 1052 SGSREQSGLQASLEAEQEALEKDQERINAYIEEEVQ-RRLQ 1091
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAElRRLE 357
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
611-689 |
1.68e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
611-727 |
1.69e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 611 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQ-EVETQRKETE-IVQLQIRKQEESlkrrsfhIENKLKDLLAEKE 688
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFErEREEIRESYEeKLRTELERQAEA-------HEEHLKDVLVEQE 389
|
90 100 110
....*....|....*....|....*....|....*....
gi 2287254621 689 kfeeerlreqqeIELQKKRQEEETFLRVQEELQRLKELN 727
Cdd:pfam09731 390 ------------IELQREFLQDIKEKVEEERAGRLLKLN 416
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-1093 |
1.86e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKLESKRKLIEEMEEK--QKSDKAELERMQQEVETQRKETEIVQLQIRKQEES----------LKRR 672
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDllKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLkvllalikdgVGGR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 673 SFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQY 752
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 753 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 832
Cdd:pfam02463 604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 833 QLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKceHDKESRLLEKHDESVTDVTEVPQDFEKIKP-VEY 911
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV--QEAQDKINEELKLLKQKIDEEEEEEEKSRLkKEE 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 912 RLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftania 991
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK------------ 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 992 RQEEKVRKKEKEILES------REKQQREALERALARLERRHSALQRHStlgMEIEEQRQKLASLNSGSREQSGLQASLE 1065
Cdd:pfam02463 830 IKEEELEELALELKEEqkleklAEEELERLEEEITKEELLQELLLKEEE---LEEQKLKDELESKEEKEKEEKKELEEES 906
|
490 500
....*....|....*....|....*...
gi 2287254621 1066 AEQEALEKDQERINAYIEEEVQRRLQDL 1093
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYE 934
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
757-1087 |
1.91e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 757 LEKKRLEEQEKEQVMLV--------AHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESL-LRVKEARAGGDEDGE 827
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVvpraellqNRLEECLQERAELLQAQEAANRQ-REKEKERYKRDREQWeRQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 828 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQE-EQEILEClkcEHDKESrLLEKHDESVTDVTEVPQDFEKI 906
Cdd:pfam07888 88 ELRQSREKHEELEEKY-KELSASSEELSEEKDALLAQRAAhEARIREL---EEDIKT-LTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 907 KPVEYRLQYKERQLQYLLQ------NHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 980
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQqteeelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 981 QATFeftaNIARQEEKVRKKEKEILESREKQQREALERAlaRLERRHSALQRhSTLGMEIEEQRQKLAslnsgsREQSGL 1060
Cdd:pfam07888 243 QERL----NASERKVEGLGEELSSMAAQRDRTQAELHQA--RLQAAQLTLQL-ADASLALREGRARWA------QERETL 309
|
330 340
....*....|....*....|....*..
gi 2287254621 1061 QASLEAEQEALEKDQERINAyIEEEVQ 1087
Cdd:pfam07888 310 QQSAEADKDRIEKLSAELQR-LEERLQ 335
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
632-792 |
1.93e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 41.59 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 632 EKQKSDKAELERMQQEVETqrKETEIVQLQIRKQEEslkrrsfHIEN-KLKDLLAEKEKfeeeRLREQQEIELQKKRQEE 710
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEE--KELEINELKAKYEEL-------RRENlEMRKIVAEFEK----TIAQMIEEKQKQKELEH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 711 ETFLRVQEELQRLK-ELNNNEKAeKFQIFQELDQlQKEKDEQYAKLELEKK--------RLEEQEKEQVMLVAHLEEQLR 781
Cdd:pfam05010 68 AEIQKVLEEKDQALaDLNSVEKS-FSDLFKRYEK-QKEVISGYKKNEESLKkcaqdylaRIKKEEQRYQALKAHAEEKLD 145
|
170
....*....|.
gi 2287254621 782 EKQEMIQLLRR 792
Cdd:pfam05010 146 QANEEIAQVRS 156
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
624-782 |
2.25e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 624 RKLIEEMEEKQKSDKAELERMQ---------QEVETQRKETE--IVQ-----LQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4026 72 RELAEKFFEELKGMVGHVERMKlplghdveyVDVELVRKEIKnaIIRaglksLQNIPEYNELREELLELKEKIDEIAKEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 688 EKFEEERLreqqeiELQKKRQEeetflrVQEELQRLKElnnnekaekfqifqELDQLQKEKDEQYAKLELEKKRLEEQEK 767
Cdd:COG4026 152 EKLTKENE------ELESELEE------LREEYKKLRE--------------ENSILEEEFDNIKSEYSDLKSRFEELLK 205
|
170
....*....|....*
gi 2287254621 768 EQVMLVAHLEEQLRE 782
Cdd:COG4026 206 KRLLEVFSLEELWKE 220
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
605-689 |
2.48e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELEKlESKRKLIE-EMEEKQKSDKAELERMQQEvETQRKETEI-----VQLQIRK-QEESLKRRSFHIE 677
Cdd:pfam17380 497 LEKELEERKQAMIEE-ERKRKLLEkEMEERQKAIYEEERRREAE-EERRKQQEMeerrrIQEQMRKaTEERSRLEAMERE 574
|
90
....*....|..
gi 2287254621 678 NKLKDLLAEKEK 689
Cdd:pfam17380 575 REMMRQIVESEK 586
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
626-794 |
2.93e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 626 LIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRsfhIENKLKDLLAEKEKFEEErlreqqeIELQK 705
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELE----QKAEEAEALLKE---AEKLKEELEEKKEKLQEE-------EDKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 706 KRQEEEtflrVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAKLELE--KKRLEEQEKEqvmlvahLEEQLREK 783
Cdd:PRK00409 569 EEAEKE----AQQAIKEAKK-------EADEIIKELRQLQKGGYASVKAHELIeaRKRLNKANEK-------KEKKKKKQ 630
|
170
....*....|.
gi 2287254621 784 QEMIQLLRRGE 794
Cdd:PRK00409 631 KEKQEELKVGD 641
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
628-1099 |
3.31e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 628 EEMEEKQKSDKAELERMQQEVET-----QRKETEIVQLQ-----IRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 697
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNldknlNKDEEKINNSNnkikiLEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 698 QQEI-----ELQK-KRQEEET----------FLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE----------Q 751
Cdd:TIGR04523 116 KEQKnklevELNKlEKQKKENkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqknidkiknK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 752 YAKLELEKKRLEEQEKEQVMLVA---HLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEARaggDEDGEE 828
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESqisELKKQNNQLKDNIEKKQ----QEINEKTTEISNTQTQLNQLKDEQ---NKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 829 LEKAQLRFFEFKRrqlvKLVNLEKDLVQQK-DILKKEVQEEQEILECLKCEhdkesrlLEKHDESVTDV-TEVPQDFEKI 906
Cdd:TIGR04523 269 LSEKQKELEQNNK----KIKELEKQLNQLKsEISDLNNQKEQDWNKELKSE-------LKNQEKKLEEIqNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 907 KPVEYRLQYKERQLQYLLQNH--LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATF 984
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 985 EftaniaRQEEKVRKKEKEILESREKQQREaleraLARLERRHSALQ-RHSTLGMEIEEQRQKLASLnsgSREQSGLQAS 1063
Cdd:TIGR04523 418 Q------QEKELLEKEIERLKETIIKNNSE-----IKDLTNQDSVKElIIKNLDNTRESLETQLKVL---SRSINKIKQN 483
|
490 500 510
....*....|....*....|....*....|....*...
gi 2287254621 1064 LEAEQEALEKDQERINAYIEE--EVQRRLQDLHRVISE 1099
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEkkELEEKVKDLTKKISS 521
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
707-806 |
3.35e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.30 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 707 RQEEETFLRVQEEL-QRLKELNNnekaekfqifqELDQLQKekdeqyaKLELEKKRLEEQEKEQVML---VAHLEEQLRE 782
Cdd:pfam08614 63 REELAELYRSRGELaQRLVDLNE-----------ELQELEK-------KLREDERRLAALEAERAQLeekLKDREEELRE 124
|
90 100 110
....*....|....*....|....*....|
gi 2287254621 783 KQEMIQLLR------RGEVQWVEEEKRDLE 806
Cdd:pfam08614 125 KRKLNQDLQdelvalQLQLNMAEEKLRKLE 154
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
620-1078 |
3.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 620 LESKRKLIEEMEEKQKSDKA-ELERmqqEVETQRKETEIVQlQIRKQEESLKRRSfHIENKLKDLLAEKEKfeeerlreq 698
Cdd:PRK04863 479 YQLVRKIAGEVSRSEAWDVArELLR---RLREQRHLAEQLQ-QLRMRLSELEQRL-RQQQRAERLLAEFCK--------- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 699 qeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLE-LEKKRLEEQEKeqvmlVAHLE 777
Cdd:PRK04863 545 ---RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAaRAPAWLAAQDA-----LARLR 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 778 EQLREKQE--------MIQLLRR-----GEVQWVEEEKRDLEGIRESLlrvkeARAGGDEDGE----------------- 827
Cdd:PRK04863 617 EQSGEEFEdsqdvteyMQQLLERereltVERDELAARKQALDEEIERL-----SQPGGSEDPRlnalaerfggvllseiy 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 828 ---ELEKA--------QLRF------FEFKRRQLVKLVNLEKDL------------------VQQKDILKKEVQEE---- 868
Cdd:PRK04863 692 ddvSLEDApyfsalygPARHaivvpdLSDAAEQLAGLEDCPEDLyliegdpdsfddsvfsveELEKAVVVKIADRQwrys 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 869 -------------QEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEK-----------------IKPVEYRLQYKER 918
Cdd:PRK04863 772 rfpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfigshlavafeadpeaeLRQLNRRRVELER 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 919 QLQYL------LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ-------LAQYQANANQLQKLQATfe 985
Cdd:PRK04863 852 ALADHesqeqqQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEaeeakrfVQQHGNALAQLEPIVSV-- 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 986 ftaniarqeekvrkkekeiLESrEKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSR--EQSGLQAS 1063
Cdd:PRK04863 930 -------------------LQS-DPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMlaKNSDLNEK 989
|
570
....*....|....*
gi 2287254621 1064 LEAEQEALEKDQERI 1078
Cdd:PRK04863 990 LRQRLEQAEQERTRA 1004
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
612-689 |
3.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254621 612 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 689
Cdd:PRK12704 68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
452-554 |
3.99e-03 |
|
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: 39.01 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-------VTLIPLSGSQCSV 524
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 2287254621 525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
605-791 |
4.35e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 605 LRLEFERQQREELE-KLESKRKLIEEmEEKQKSD-KAELERMQQEVETQRK--ETEIVQLQIRKQEESL-----KRRSFH 675
Cdd:pfam00038 89 QKYEDELNLRTSAEnDLVGLRKDLDE-ATLARVDlEAKIESLKEELAFLKKnhEEEVRELQAQVSDTQVnvemdAARKLD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 676 IENKLKDLLAEKEKFEeerlreqqeielQKKRQE-EETFLRVQEELQRLKELNNNE-KAEKFQIFQ----------ELDQ 743
Cdd:pfam00038 168 LTSALAEIRAQYEEIA------------AKNREEaEEWYQSKLEELQQAAARNGDAlRSAKEEITElrrtiqsleiELQS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2287254621 744 LQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE-KQEMIQLLR 791
Cdd:pfam00038 236 LKKQKASLERQLAETEERYELQLADYQELISELEAELQEtRQEMARQLR 284
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
606-898 |
4.66e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 606 RLEFERQQ----REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsF------- 674
Cdd:PRK02224 329 RLEECRVAaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER-Fgdapvdl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 675 -HIENKLKDLLAEKEKFEEERLREQQEI-ELQKKRQEEETFL-------------------RVQEELQRLKELnnneKAE 733
Cdd:PRK02224 408 gNAEDFLEELREERDELREREAELEATLrTARERVEEAEALLeagkcpecgqpvegsphveTIEEDRERVEEL----EAE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 734 KFQIFQELDQLQK--EKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR-------------------- 791
Cdd:PRK02224 484 LEDLEEEVEEVEErlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaeekreaaaea 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 792 -------RGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKaqLRffeFKRRQLVKLVNLEKDLVQQKDILKKE 864
Cdd:PRK02224 564 eeeaeeaREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER--LR---EKREALAELNDERRERLAEKRERKRE 638
|
330 340 350
....*....|....*....|....*....|....*.
gi 2287254621 865 VQEE--QEILECLKCEHDKESRLLEKHDESVTDVTE 898
Cdd:PRK02224 639 LEAEfdEARIEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
707-1093 |
4.81e-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: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 707 RQEEETFLRvQEELQRLKELNnnekaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQ----LRE 782
Cdd:pfam01576 2 RQEEEMQAK-EEELQKVKERQ-----------QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMrarlAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 783 KQEMIQLLRRGEVQWVEEEKRDlegirESLLRVKEARAGGDEDGEElekaQLRFFEFKRRQLvklvNLEKDLVQQKdilK 862
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERS-----QQLQNEKKKMQQHIQDLEE----QLDEEEAARQKL----QLEKVTTEAK---I 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 863 KEVQEEQEILECLKCEHDKESRLLEkhdESVTDVT-EVPQDFEKIKPVEyRLQYKERQLQYLLQNHLPTllEEKQRafEI 941
Cdd:pfam01576 134 KKLEEDILLLEDQNSKLSKERKLLE---ERISEFTsNLAEEEEKAKSLS-KLKNKHEAMISDLEERLKK--EEKGR--QE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 942 LDRGPLSLDNTLYQVEKEMEEKEEQL----AQYQANANQLQKLQATFE-FTANIARQEEKVRKKEKEILESREKQQREAL 1016
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIaelrAQLAKKEEELQAALARLEeETAQKNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 1017 ERALARLERRhsalqrhsTLGMEIEEQRQKLASLNSGSREQSGLQASLEAE----QEALEKDQERINAYIEEEVQRRLQD 1092
Cdd:pfam01576 286 ARNKAEKQRR--------DLGEELEALKTELEDTLDTTAAQQELRSKREQEvtelKKALEEETRSHEAQLQEMRQKHTQA 357
|
.
gi 2287254621 1093 L 1093
Cdd:pfam01576 358 L 358
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
739-869 |
4.85e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 739 QELDQLqkekDEQYAKLELEKKRLE-EQEKEQVMLVAHLEEQLREKQEMIQLLRRgevQWvEEEKRDLEGIREsllrVKE 817
Cdd:COG0542 411 EELDEL----ERRLEQLEIEKEALKkEQDEASFERLAELRDELAELEEELEALKA---RW-EAEKELIEEIQE----LKE 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2287254621 818 ARAGGDEDGEELEKaqlrffefkrrqlvKLVNLEKDLVQQKDILKKEVQEEQ 869
Cdd:COG0542 479 ELEQRYGKIPELEK--------------ELAELEEELAELAPLLREEVTEED 516
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
716-919 |
5.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 716 VQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMI-------- 787
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELgeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 788 -------------------QLLRRGE-VQWVEEEKRDLegiresLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKL 847
Cdd:COG3883 97 rsggsvsyldvllgsesfsDFLDRLSaLSKIADADADL------LEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254621 848 VNLEKDLVQQKDI---LKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQ 919
Cdd:COG3883 171 AELEAQQAEQEALlaqLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
608-769 |
5.42e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREeleKLESKRKliEEMEEKQKSDKAELERMQQEVETQR-----KETEIVQLQIRKQEESLKrrsfhienklkd 682
Cdd:PRK09510 63 QYNRQQQQ---QKSAKRA--EEQRKKKEQQQAEELQQKQAAEQERlkqleKERLAAQEQKKQAEEAAK------------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 683 LLAEKEKfeeerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRL 762
Cdd:PRK09510 126 QAALKQK----------QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
....*..
gi 2287254621 763 EEQEKEQ 769
Cdd:PRK09510 195 AAAEAKK 201
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
620-791 |
5.43e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 620 LESKRKLIEEMEEKQKSD--------KAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIENklkdllaekekfe 691
Cdd:pfam09787 20 LQSKEKLIASLKEGSGVEgldsstalTLELEELRQERDLLREEIQ----KLRGQIQQLRTELQELEA------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 692 eerlreqqeielqkkrQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKdeQYAKLELEKKRleeqekeqvm 771
Cdd:pfam09787 83 ----------------QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL--RYLEEELRRSK---------- 134
|
170 180
....*....|....*....|
gi 2287254621 772 lvAHLEEQLREKQEMIQLLR 791
Cdd:pfam09787 135 --ATLQSRIKDREAEIEKLR 152
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
607-672 |
5.97e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 40.74 E-value: 5.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2287254621 607 LEFERQQREEleklESKRKLIEEmEEKQKSDKAELE------RMQQEVETQRKETEivqLQIRKQEESLKRR 672
Cdd:pfam12037 76 LKIERQRVEY----EERRKTLQE-ETKQKQQRAQYQdelarkRYQDQLEAQRRRNE---ELLRKQEESVAKQ 139
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
614-786 |
7.96e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.97 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 614 REELEKL-ESKRKLIEE---MEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKqeesLKRRSFHIENKLKDLLAEKEK 689
Cdd:pfam15066 369 KENVEELiEDKYNVILEkndINKTLQNLQEILANTQKHLQESRKEKETLQLELKK----IKVNYVHLQERYITEMQQKNK 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 690 feeerlREQQEIELQKKRQEEEtflrvqEELQRLKELNNN-EKAEKfqifQELDQLQKEKDEQyaklelEKKRLEEQEKE 768
Cdd:pfam15066 445 ------SVSQCLEMDKTLSKKE------EEVERLQQLKGElEKATT----SALDLLKREKETR------EQEFLSLQEEF 502
|
170
....*....|....*...
gi 2287254621 769 QvmlvAHLEEQLREKQEM 786
Cdd:pfam15066 503 Q----KHEKENLEERQKL 516
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
608-769 |
8.27e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 608 EFERQQREELEKLE--SKRKLIEEMEEKQKSDKAELERMQQ--EVETQRKETEIVQLqirKQEESLKRrsfhIENKLKDL 683
Cdd:PRK09510 91 ELQQKQAAEQERLKqlEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAKAAAAAKA---KAEAEAKR----AAAAAKKA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 684 LAEKEKFEEERLREQQEIELQKKrQEEETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLELEKKRLE 763
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAAEAKKK-AEAEAAAKAAAEAKKKAEAEAKKKAAA----EAKKKAAAEAKAAAAKAAAEAKAAA 238
|
....*.
gi 2287254621 764 EQEKEQ 769
Cdd:PRK09510 239 EKAAAA 244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
704-784 |
8.87e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254621 704 QKKRQEEETFLRVQEELQRLKELNNNEKAEkfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREK 783
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQERLKQLEKERLAA---------QEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
.
gi 2287254621 784 Q 784
Cdd:PRK09510 155 R 155
|
|
| |
