|
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: 563.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365 159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365 239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 530425794 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365 315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
3-365 |
2.00e-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: 463.58 E-value: 2.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129 68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129 146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530425794 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
9-358 |
5.68e-148 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 459.35 E-value: 5.68e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225 68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225 146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225 226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
|
330 340 350
....*....|....*....|....*....|..
gi 530425794 327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225 295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
3-356 |
8.70e-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: 433.99 E-value: 8.70e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106 145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 530425794 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106 292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
3-358 |
3.60e-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: 376.80 E-value: 3.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371 148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371 226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530425794 318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371 294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
3-358 |
4.20e-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: 4.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372 62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372 140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372 220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 530425794 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 |
1.80e-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: 1.80e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370 76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370 154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370 231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530425794 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 |
5.62e-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: 5.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374 138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374 215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 530425794 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 |
1.29e-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: 330.24 E-value: 1.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373 144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373 221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 530425794 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 |
2.70e-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: 322.74 E-value: 2.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYsADTkspdyvSQEMVF 79
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFD-PNT------TQEDVY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369 62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369 140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369 215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530425794 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 |
1.88e-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: 1.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366 9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366 71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfds 238
Cdd:cd01366 148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWL 318
Cdd:cd01366 225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530425794 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 |
2.95e-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: 295.00 E-value: 2.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364 145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364 225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530425794 305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364 291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-508 |
1.52e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 289.33 E-value: 1.52e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059 18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059 91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059 244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQ--------------- 392
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSqsslsgifaymqslk 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 393 --IALLDSPTALSMEEKLQQNEARVQEL-TKEWTNKwnETQNILKEQTLALrkegiGVVLDSELPHLIGIDDDLLSTGII 469
Cdd:COG5059 394 keTETLKSRIDLIMKSIISGTFERKKLLkEEGWKYK--STLQFLRIEIDRL-----LLLREEELSKKKTKIHKLNKLRHD 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 530425794 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 |
7.06e-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: 255.63 E-value: 7.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 530425794 526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
4-392 |
2.17e-74 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 274.12 E-value: 2.17e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188 100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188 154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188 232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188 309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188 380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454
|
410 420
....*....|....*....|
gi 530425794 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 |
6.37e-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: 247.69 E-value: 6.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368 78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368 150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368 230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 530425794 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 |
5.52e-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: 244.80 E-value: 5.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375 1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375 68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375 145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375 225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530425794 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 |
3.30e-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: 3.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376 66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376 142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376 219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 530425794 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 |
4.73e-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: 232.96 E-value: 4.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367 63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367 141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367 217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 530425794 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 |
5.14e-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: 5.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 530425794 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 |
3.70e-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: 3.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 530425794 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 |
2.51e-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: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTeqdIVLHGLDLESEHCIFENIGGTVTLIPL 517
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530425794 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 |
9.44e-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: 9.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEA 532
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 530425794 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 |
1.15e-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: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQI 529
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 530425794 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 |
3.88e-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: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-----VTLIPLSGSQCSVNGVQ 528
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 530425794 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 |
2.06e-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: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIF-----ENIGGTVTLIPLSGSQCSVNGVQ 528
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 530425794 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 |
3.51e-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: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLS-GSQCSVNGVQIVEA 532
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 530425794 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 |
7.58e-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: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363 1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363 42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363 100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 530425794 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 |
2.35e-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: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 471 YHLKEgQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 530425794 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 |
3.06e-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: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDAsteqDIVLHGLDLESEHCIFENIGG-----TVTLIPLSGSQCSVNGVQ 528
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 530425794 529 IVEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
595-1078 |
1.61e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 595 GLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 673
Cdd:COG1196 303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 674 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:COG1196 383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 754 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 831
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 832 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 901
Cdd:COG1196 538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 902 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 981
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 982 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1061
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759
|
490
....*....|....*..
gi 530425794 1062 KDQERLEYEIQQLKQKI 1078
Cdd:COG1196 760 PDLEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
600-1077 |
1.15e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaeke 677
Cdd:COG1196 216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 678 kfeeerlreqqeielqkkRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 757
Cdd:COG1196 291 ------------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 758 QVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQLRffEFKRRQLVKL 836
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLE--EELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 837 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 916
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 917 LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ---------LAQYQANANQLQKLQATFEFTANIARQEEKVR 987
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 988 KKEKEI--------------LESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASL 1053
Cdd:COG1196 591 ALARGAigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500
....*....|....*....|....
gi 530425794 1054 EAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELE 694
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
3-162 |
1.98e-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: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796 21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 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 |
8.38e-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: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--RDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSG-SQCSV 524
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 530425794 525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
592-926 |
9.45e-15 |
|
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: 80.17 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKD 671
Cdd:pfam17380 260 YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 672 LLAEKEKFEEERLReqqeiELQKKRQEEEtflrvQEELQRLKElnnNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKK 749
Cdd:pfam17380 335 IYAEQERMAMERER-----ELERIRQEER-----KRELERIRQ---EEIAMEISRMRELERLQMERQQKNERVrqELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 750 R----LEEQEKEQVMLVAHLEEQLREKQEMIqllRRGEVQWVEEEK-RDLEGIREsllrvkearaggdedgEELEKAQ-- 822
Cdd:pfam17380 402 RkvkiLEEERQRKIQQQKVEMEQIRAEQEEA---RQREVRRLEEERaREMERVRL----------------EEQERQQqv 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 823 --LRFFEFKRRQlvKLVNLEKDLVQQKD-------ILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFE 893
Cdd:pfam17380 463 erLRQQEEERKR--KKLELEKEKRDRKRaeeqrrkILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEER 534
|
330 340 350
....*....|....*....|....*....|...
gi 530425794 894 KIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQR 926
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
599-891 |
8.68e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 670
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 671 dLLAEKEKFEEerlreqqeiELQKKRQEE----ETFLRVQEELQRLKELNNNEKAEKfqifQELDQLQKEKDEQYAKLEL 746
Cdd:PTZ00121 1600 -LYEEEKKMKA---------EEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 747 EKKRlEEQEKEQVMLVAHLEEQLREKQEmiQLLRRGE--------VQWVEEEKRDLEGIR----ESLLRVKEARAGGDED 814
Cdd:PTZ00121 1666 EAKK-AEEDKKKAEEAKKAEEDEKKAAE--ALKKEAEeakkaeelKKKEAEEKKKAEELKkaeeENKIKAEEAKKEAEED 1742
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530425794 815 GEELEKAQLRFFEFKrrqlvKLVNLEKDLVQQKDILKKEvqEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQD 891
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKK-----KIAHLKKEEEKKAEEIRKE--KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
602-933 |
7.28e-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: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 602 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLAEKEKFEE 681
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL-------KRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 682 ERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRLEE--QEK 756
Cdd:TIGR02169 738 RLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArlREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 EQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE---------KAQ 822
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkkerdelEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 823 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 902
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977
|
330 340 350
....*....|....*....|....*....|....
gi 530425794 903 --QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 933
Cdd:TIGR02169 978 iqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
603-1136 |
7.66e-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: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 603 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRS--FHIENKLKDLLAEKEKF 679
Cdd:TIGR02169 363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEkLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 680 EEERLREQQEIELQkkrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02169 440 EEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEKRDLEGIrESLLRVKEARAG---------- 810
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAVAKEAI-ELLKRRKAGRATflplnkmrde 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 811 ------GDEDG------------EELEKA---------QLRFFEFKRRQL--VKLVNLEKDLVQQ--------------- 846
Cdd:TIGR02169 587 rrdlsiLSEDGvigfavdlvefdPKYEPAfkyvfgdtlVVEDIEAARRLMgkYRMVTLEGELFEKsgamtggsraprggi 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 847 --KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESVTDVTEVpqdFEKIKPVEYRLQYKERQLQYLLQNH--LPTLLE 922
Cdd:TIGR02169 667 lfSRSEPAELQRLRERLEGLKRE---LSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEekLKERLE 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 923 EKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIARQEEKVRKKEKEI 993
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQK 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 994 LESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQ 1072
Cdd:TIGR02169 821 LNRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425794 1073 QLKQKIYEV----------DGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRV 1136
Cdd:TIGR02169 900 ELERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
597-894 |
1.18e-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: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEK 676
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 EQVMLVAHLE----EQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARaggdEDGEELEKAQLRFFEFKRRQ 832
Cdd:TIGR02168 401 EIERLEARLErledRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL----ERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425794 833 LVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 894
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
456-564 |
1.63e-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: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 456 LIGIDDDLLSTGIILYHLKeGQTYVGRDdasTEQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVGAD---TSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 530425794 535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
600-1098 |
2.14e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 669
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 670 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 749
Cdd:PRK03918 348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 750 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 829
Cdd:PRK03918 413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 830 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 905
Cdd:PRK03918 483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 906 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 981
Cdd:PRK03918 562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 982 QEEKVRKKEKEILESREK---QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQE 1058
Cdd:PRK03918 638 TEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 530425794 1059 ALEKDQERLEyeiqQLKQKIYEVDGVQKDHHGTLEGKVAS 1098
Cdd:PRK03918 715 KLEKALERVE----ELREKVKKYKALLKERALSKVGEIAS 750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
536-1237 |
2.49e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 536 NQGAVILLGRTNMFRFNHPKEAAKLREKRKSGL--LSSFSLSMTDLSKSRENLSAvmlynpglEFERQQREELEKLESKR 613
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADElkKAEEKKKADEAKKAEEKKKA--------DEAKKKAEEAKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 614 KLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQ 693
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 694 KKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQEKEQvmlvaHLEEQLREKQ 773
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAE-----EAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 774 EMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFEFKRrqlvKLVNLEK-DLVQ 845
Cdd:PTZ00121 1471 KADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAEEAK----KADEAKKaEEKK 1546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 846 QKDILKK--EVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlpTLLEE 923
Cdd:PTZ00121 1547 KADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--------KAEEA 1618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 924 KQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftaniARQEEKVRKKEKEILESREKQQRE 1003
Cdd:PTZ00121 1619 KIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKK-----------AEEENKIKAAEEAKKAEEDKKKAE 1678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1004 ALERALARLERRHSALQRHstlgmeiEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDG 1083
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKE-------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1084 VQKDhhgtlEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISEGCSTSADTMKDNEKlhnGTIQrkL 1163
Cdd:PTZ00121 1752 DEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE---GNLV--I 1821
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530425794 1164 KYEKRQFCPAwyldpllPRDATDTSSLIKEERREVDQNDHWDHpmlwSVSGPKTTSSA--SQERTHQQRDQSSVPE 1237
Cdd:PTZ00121 1822 NDSKEMEDSA-------IKEVADSKNMQLEEADAFEKHKFNKN----NENGEDGNKEAdfNKEKDLKEDDEEEIEE 1886
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
595-935 |
4.30e-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: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 595 GLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKL 669
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 670 KDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL 744
Cdd:pfam02463 244 ELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 745 ELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR 824
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 825 FFEFKRRQLVKLVNLEKDLVQQKDILKKE--VQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpQDFEKIKPVEYRL 902
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDE--LELKKSEDLLKET 477
|
330 340 350
....*....|....*....|....*....|...
gi 530425794 903 QYKERQLQYLLQNHLPTLLEEKQRAFEILDRGP 935
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLK 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
691-1170 |
5.35e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 691 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 770
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 771 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 847
Cdd:PRK03918 242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 848 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQ-YKERQLQYllqnhlptLLEEKQR 926
Cdd:PRK03918 321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGL--------TPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 927 AFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESR 997
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 998 EKQQREaLERALARLER---RHSALQRHSTLGMEIEEQRQKLASLN-----SGSREQSGLQ---ASLEAEQEALEKDQER 1066
Cdd:PRK03918 472 EEKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNleeleKKAEEYEKLKeklIKLKGEIKSLKKELEK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1067 ---LEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMdariNAYIE--------EEVQRRLQDLHR 1135
Cdd:PRK03918 551 leeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY----NEYLElkdaekelEREEKELKKLEE 626
|
490 500 510
....*....|....*....|....*....|....*
gi 530425794 1136 VISEGCSTSADTMKDNEKLHNGTIQRKLKYEKRQF 1170
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
599-859 |
6.91e-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: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI--RKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:pfam13868 30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKFEEERLREQQEIELQKKRQEEETFLRVQE---ELQRLKELNNNEKAEKFqifqeldqlQKEKDEQYAKLELEKKRL-E 752
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAewkELEKEEEREEDERILEY---------LKEKAEREEEREAEREEIeE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 753 EQEKEQVMLVAHLEEQLREKQEMIQLLRRG-----EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR--- 824
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEree 260
|
250 260 270
....*....|....*....|....*....|....*.
gi 530425794 825 -FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQE 859
Cdd:pfam13868 261 eEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
587-1080 |
7.84e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 587 SAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIE 666
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 667 -NKLKDLLAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKElnnNEKAEKFQIFQELDQLQKEKDEQYAKLE 745
Cdd:COG4717 134 lEALEAELAELPE------------RLEELEERLEELRELEEELEELEA---ELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 746 LEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIresLLRVKEARAGGDEDGEELEKAQLRF 825
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL---LLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 826 FEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH----DESVTDVTEVPQDFEKIKPVEYR 901
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 902 LQYKERQLQyllqnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEftaniar 981
Cdd:COG4717 356 AEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLE------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 982 qeekvrKKEKEILESREKQQREALERALARLERRHSALQRhstlgmEIEEQRQKLaslnsgsreqsglqASLEAEQEALE 1061
Cdd:COG4717 413 ------ELLGELEELLEALDEEELEEELEELEEELEELEE------ELEELREEL--------------AELEAELEQLE 466
|
490 500
....*....|....*....|.
gi 530425794 1062 KDQE--RLEYEIQQLKQKIYE 1080
Cdd:COG4717 467 EDGElaELLQELEELKAELRE 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
599-1019 |
9.18e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 FEEERLREQQEIE--LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:COG1196 419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQ---WVEEEKRDLEGIRESLLRVKEARAggDEDGEELEKAQLRFFEFKRRQL 833
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATF 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 834 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVP-QDFEKIKPVEYRLQYKERQLQYL 912
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 913 LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKE 992
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 530425794 993 ILESREKQQ----------------REALERALARLERRHSAL 1019
Cdd:COG1196 737 LLEELLEEEelleeealeelpeppdLEELERELERLEREIEAL 779
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
364-476 |
1.14e-11 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 65.25 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 530425794 463 LLSTGIILYHLKEG 476
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
578-1084 |
3.90e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 578 DLSKSRENLSAVMlynpglefeRQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrKETEIVQLQIRKQEES 657
Cdd:PRK03918 159 DYENAYKNLGEVI---------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 658 LKRRSFHIEnKLKDLLAEKEKFEEERLREQQEIElQKKRQEEEtflRVQEELQRLKELNNNEKaekfqifqELDQLqKEK 737
Cdd:PRK03918 226 LEKEVKELE-ELKEEIEELEKELESLEGSKRKLE-EKIRELEE---RIEELKKEIEELEEKVK--------ELKEL-KEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 738 DEQYAKLELE----KKRLEEQEKEqvmlVAHLEEQLREKQEMIQLL--RRGEVQWVEEE----KRDLEGIRESLLRVKEA 807
Cdd:PRK03918 292 AEEYIKLSEFyeeyLDELREIEKR----LSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 808 RAGGDE--------DGEELEKAQLRFFEFKRRQLvKLVNLEKDLVQQKDILKKEVQEEQEILECLK-----C-------- 866
Cdd:PRK03918 368 KAKKEElerlkkrlTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKkakgkCpvcgrelt 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 867 EHDKEsRLLEKHDESVTDVTEvpqDFEKIKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFEIldrgpLSLDNTLYQVe 946
Cdd:PRK03918 447 EEHRK-ELLEEYTAELKRIEK---ELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQL-----KELEEKLKKY- 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 947 kemeekeeqlaqyqaNANQLQKLQATFEFTANIARQEEKVRKKEKEILESRE--KQQREALERALARLERRHSALQRH-S 1023
Cdd:PRK03918 516 ---------------NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKElE 580
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425794 1024 TLGME-IEEQRQKLASLNSGSREQSGLQASlEAEQEALEKDQERLEYEIQQLKQKIYEVDGV 1084
Cdd:PRK03918 581 ELGFEsVEELEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKR 641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
601-914 |
5.03e-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: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 601 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEN--------- 667
Cdd:TIGR02168 674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeriaqls 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 668 -KLKDLLAEKEKFEEERLREQQEIE--LQKKRQEEETFLRVQEELQ----RLKELN---NNEKAEKFQIFQELDQLQKEK 737
Cdd:TIGR02168 754 kELTELEAEIEELEERLEEAEEELAeaEAEIEELEAQIEQLKEELKalreALDELRaelTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 738 DEQYAKLELEKKRLEEQEKEQVML---VAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLE----GIRESLLRVKEA 807
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALlneRASLEEALALLRSELEelseELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 808 RAGGDEDGEELEKAQLRffefkrrqlvkLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHdesvtdVTE 887
Cdd:TIGR02168 914 RRELEELREKLAQLELR-----------LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR------LKR 976
|
330 340 350
....*....|....*....|....*....|...
gi 530425794 888 VPQDFEKIKPV------EYRlQYKERqLQYLLQ 914
Cdd:TIGR02168 977 LENKIKELGPVnlaaieEYE-ELKER-YDFLTA 1007
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
555-1077 |
6.00e-11 |
|
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: 68.07 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAE-LERM 633
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIkREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 634 QQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRlk 713
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 714 elnnnEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRD 793
Cdd:pfam02463 433 -----EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 794 LEGIRESLLRVKEARAGGDEDGeELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEI---LECLKCEHDK 870
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHG-RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELplgARKLRLLIPK 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 871 ESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLyQVEKEME 950
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGL-AEKSEVK 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 951 EKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLgmEIE 1030
Cdd:pfam02463 666 ASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--LKQ 743
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 530425794 1031 EQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
456-554 |
7.06e-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: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 456 LIGIDDDLLSTGIILYHLKEgQTYVGRDDAsteQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 530425794 535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
695-1076 |
9.33e-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: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 695 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 750
Cdd:TIGR02168 171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 751 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 830
Cdd:TIGR02168 251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 831 RQLV-KLVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 906
Cdd:TIGR02168 312 ANLErQLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 907 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 986
Cdd:TIGR02168 379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 987 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1065
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
410
....*....|.
gi 530425794 1066 RLEYEIQQLKQ 1076
Cdd:TIGR02168 500 NLEGFSEGVKA 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
695-1079 |
1.01e-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: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 695 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 771
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 772 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 843
Cdd:TIGR02169 749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 844 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 923
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 924 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1001
Cdd:TIGR02169 887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425794 1002 REALERALARLERRHSAlqrhstlgmEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALekdQERLEyEIQQLKQKIY 1079
Cdd:TIGR02169 960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAI---LERIE-EYEKKKREVF 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
556-916 |
1.05e-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: 67.00 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 556 EAA---KLREKRKSGLLSsfslsmtdLSKSRENLSAVmlYNPGLEFERQqreeLEKLESKRKLIEEMEEKqksdKAELER 632
Cdd:TIGR02168 163 EAAgisKYKERRKETERK--------LERTRENLDRL--EDILNELERQ----LKSLERQAEKAERYKEL----KAELRE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 633 MQQEVETQRKETEIVQL-QIRKQEESLKRRSFHIENKLKDLLAEKEkfeeerlreqqeiELQKKRQE-EETFLRVQEELQ 710
Cdd:TIGR02168 225 LELALLVLRLEELREELeELQEELKEAEEELEELTAELQELEEKLE-------------ELRLEVSElEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 711 RLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVML----------VAHLEEQLREKQEMIQLLR 780
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELeekleelkeeLESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 781 RGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEE 857
Cdd:TIGR02168 372 SRLEELeeqLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA------ELEEL 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 858 QEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpVEYRLQYKERQLQYLLQNH 916
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAER---ELAQLQARLDSLERLQENL 501
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
601-1087 |
1.71e-10 |
|
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: 66.28 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 601 QQREELEKLESKRKL----IEEMEEKQKSDKAELE----RMQQEVETQRKETEIVQLQIR-----------KQEESLKRR 661
Cdd:pfam05483 265 ESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 662 SFH--IENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtFLRVQEELQRLKELNNNEKAEkfqiFQELDQLQKEKDe 739
Cdd:pfam05483 345 AAHsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVE----LEELKKILAEDE- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 740 qyaKLELEKKRLEEqekeqvmlvahLEEQLREK-QEMIQLLrrgevQWVEEEKRDLEgIRESLLRVKEARAGGD--EDGE 816
Cdd:pfam05483 419 ---KLLDEKKQFEK-----------IAEELKGKeQELIFLL-----QAREKEIHDLE-IQLTAIKTSEEHYLKEveDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 817 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQEEQE-ILECLKCEHD--KESRLLEKHDESVTDVTE-VPQDF 892
Cdd:pfam05483 479 ELEKEKLKNIELTAHC-DKLLLENKELTQEASDMTLELKKHQEdIINCKKQEERmlKQIENLEEKEMNLRDELEsVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 893 ---------------EKIKPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQ 955
Cdd:pfam05483 558 iqkgdevkckldkseENARSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQ 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 956 LAQYQANANQLQ-KLQATF----EFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQ 1020
Cdd:pfam05483 631 LNAYEIKVNKLElELASAKqkfeEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALME 710
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 1021 RHS-TLGMEIEEQRQKLASLNSGSREQSGLQASLE-------AEQEALEKDQERLEYEIQQLKQKIYEVDGVQKD 1087
Cdd:pfam05483 711 KHKhQYDKIIEERDSELGLYKNKEQEQSSAKAALEielsnikAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
600-1072 |
2.23e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 679
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 680 EEERLREQQEIELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIF----QELDQLQKEKDEQYAKLELEKKRLEEQE 755
Cdd:COG4717 152 EERLEELRELEEELEELEAELA--ELQEELEELLEQLSLATEEELQDLaeelEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 756 K--EQVMLVAHLEEQLREKQEMIQLLRRGEVqwveeekrdLEGIRESLLRVKEARAGgdedgeeLEKAQLRFFefkrrQL 833
Cdd:COG4717 230 EqlENELEAAALEERLKEARLLLLIAAALLA---------LLGLGGSLLSLILTIAG-------VLFLVLGLL-----AL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 834 VKLVNLEKDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 913
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 914 QNHLptlleEKQRAfEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEI 993
Cdd:COG4717 365 LEEL-----EQEIA-ALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 994 LESRE--------KQQREALERALARLERRHSALQRhstlGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1065
Cdd:COG4717 432 EELEEleeeleelEEELEELREELAELEAELEQLEE----DGELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
....*..
gi 530425794 1066 RLEYEIQ 1072
Cdd:COG4717 508 EYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
612-1031 |
2.37e-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: 65.86 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 612 KRKLIEEM-------EEKQKSdKAELErmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKFeeerl 684
Cdd:TIGR02169 155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREY----- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 685 reqqeielqkkrqeeetflrvqEELQRLKELNNNEKaEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvah 764
Cdd:TIGR02169 224 ----------------------EGYELLKEKEALER-QKEAIERQLASLEEELEKLTEEISELEKRLEE----------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 765 LEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLV 844
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE---RELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 845 QQ---KDILKKEVQEEQEILECLKCEHDKESrllEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLL 921
Cdd:TIGR02169 347 EErkrRDKLTEEYAELKEELEDLRAELEEVD---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 922 EEKQRAFEILDRgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftaniARQEEKVRKKEKEILESRekqq 1001
Cdd:TIGR02169 424 DLNAAIAGIEAK--------INELEEEKEDKALEIKKQEWKLEQLAADLSK-------YEQELYDLKEEYDRVEKE---- 484
|
410 420 430
....*....|....*....|....*....|
gi 530425794 1002 REALERALARLERRHSALQRHSTLGMEIEE 1031
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
596-774 |
4.63e-10 |
|
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: 64.20 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 596 LEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetqrKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:pfam15709 348 LEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ------RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 676 KEKFEEERLREQQEI-ELQKKRQEEETfLRVQEELQRLKELnNNEKAEKFQIFQELD-------QLQKEKDEQYAKLELE 747
Cdd:pfam15709 418 QERARQQQEEFRRKLqELQRKKQQEEA-ERAEAEKQRQKEL-EMQLAEEQKRLMEMAeeerleyQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*..
gi 530425794 748 KKRleEQEKEQVMLVahLEEQLREKQE 774
Cdd:pfam15709 496 ERR--QKEEEAARLA--LEEAMKQAQE 518
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
555-880 |
1.05e-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: 63.84 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLynpgLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ 634
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV----QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 635 QEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKE 714
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI-----KEEELEELA 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 715 LNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ------- 785
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekenei 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 786 --WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILEC 863
Cdd:pfam02463 920 eeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
330
....*....|....*..
gi 530425794 864 LKCEHDKESRLLEKHDE 880
Cdd:pfam02463 1000 LEEEKKKLIRAIIEETC 1016
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
600-809 |
1.16e-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: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:COG4942 26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 FEEERlreqqeIELQKKRQEE--------ETFLRVQEELQRLKELNNNEKAEKFQIFQELDQL----------QKEKDEQ 740
Cdd:COG4942 106 LAELL------RALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalraeleaeRAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 741 YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveeEKRDLEGIRESLLRVKEARA 809
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLEAEAAAAA 240
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
455-551 |
1.34e-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: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 455 HLIGIDDDllsTGIILYHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQ-CSVNGVQIVEAT 533
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGRSPDC---DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNgTFVNGKRITPPV 74
|
90
....*....|....*...
gi 530425794 534 HLNQGAVILLGRTNmFRF 551
Cdd:cd00060 75 PLQDGDVIRLGDTT-FRF 91
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
742-1078 |
1.57e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 742 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 821
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 822 QLRFFEFK---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpv 898
Cdd:TIGR02168 756 LTELEAEIeelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER---- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 899 eyRLQYKERQLQYLLQNhlptlLEEKQRAFEILdrgplsldntlyqvekemeekEEQLAQYQANANqlqKLQATFEFTAN 978
Cdd:TIGR02168 832 --RIAATERRLEDLEEQ-----IEELSEDIESL---------------------AAEIEELEELIE---ELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 979 IARQEEKVRKKEKEILESREKQQREaLERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQAS-LEAE 1056
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRE-LESKRSELRRELEELReKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEAL 959
|
330 340
....*....|....*....|..
gi 530425794 1057 QEALEKDQERLEYEIQQLKQKI 1078
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
695-1083 |
2.09e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 695 KRQEEETFLR---VQEELQRLK----ELNNN--------EKAEKFQifqELDQLQKEKDEQYAKLELEKKRLEEQEKEQV 759
Cdd:COG1196 171 KERKEEAERKleaTEENLERLEdilgELERQleplerqaEKAERYR---ELKEELKELEAELLLLKLRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 760 mlVAHLEEQLREKQEMIQLLRRgevqwveeekrdlegiresllRVKEARAGGDEDGEELEKAQLRFFEFKRRQLvklvnl 839
Cdd:COG1196 248 --LEELEAELEELEAELAELEA---------------------ELEELRLELEELELELEEAQAEEYELLAELA------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 840 ekDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEvpqdfekikpvEYRLQYKErqlqyllqnhlpt 919
Cdd:COG1196 299 --RLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELE-----------ELEEELEE------------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 920 lLEEKQRAFEildrgplsldntlyqvekemeekeEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK 999
Cdd:COG1196 349 -AEEELEEAE------------------------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1000 QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIY 1079
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
....
gi 530425794 1080 EVDG 1083
Cdd:COG1196 481 ELLE 484
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
595-1080 |
2.63e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 595 GLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE----------ESLKRRSF 663
Cdd:PRK02224 210 GLESELAElDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 664 HIENKLKDLLAEKEKFEEERLREQQEIELQKKRqEEETFLRVQEELQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAK 743
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 744 LELEKKRLEEQEKEQVMLVAHLEEQLREKqemiqllrRGEVQWVEEEKRDLEGIRESLLrvkEARAGGDEDGEELEkaql 823
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEEL--------RERFGDAPVDLGNAEDFLEELR---EERDELREREAELE---- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 824 rffefkrrqlVKLVNLEKDlvqqkdilkkeVQEEQEILE---CLKCEHD-KESRLLEKHDESVTDVTEVPQDFEKIKPVE 899
Cdd:PRK02224 433 ----------ATLRTARER-----------VEEAEALLEagkCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 900 YRLQYKERQLQYL--LQNHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekEEQLAQYQANANQLQKLQATFEFTA 977
Cdd:PRK02224 492 EEVEERLERAEDLveAEDRIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 978 NIARQEEKVRKKEKEILESRE---KQQREALERALARLERRHSALQRHSTLgmeiEEQRQKLASLNSGSREQ-------- 1046
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLaelKERIESLERIRTLLAAIADAEDEIERL----REKREALAELNDERRERlaekrerk 636
|
490 500 510
....*....|....*....|....*....|....*
gi 530425794 1047 SGLQASLEAEQ-EALEKDQERLEYEIQQLKQKIYE 1080
Cdd:PRK02224 637 RELEAEFDEARiEEAREDKERAEEYLEQVEEKLDE 671
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
597-1077 |
3.21e-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: 62.29 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETQRKETEIVQLQirkqeeslkRRSF 663
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHI---------KAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 664 HIENKLKDLLAE-KEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQlQKEKDEQYA 742
Cdd:TIGR00618 304 QIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ-QHTLTQHIH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 743 KLELEKKRLEEQEKeqvmLVAHLEEQLREkqemiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 822
Cdd:TIGR00618 383 TLQQQKTTLTQKLQ----SLCKELDILQR----------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 823 LRFFEFKRRQLVKLVNLEKDLVQQKdilkkeVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRL 902
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQS------LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP------CPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 903 QYKERQLQYLLqnhlptLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQanaNQLQKLQATFEFTA----- 977
Cdd:TIGR00618 511 IHPNPARQDID------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---EQMQEIQQSFSILTqcdnr 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 978 -----NIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLnsgSREQSGLQAS 1052
Cdd:TIGR00618 582 skediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL---HALQLTLTQE 658
|
490 500
....*....|....*....|....*
gi 530425794 1053 LEAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQ 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
613-1174 |
6.41e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 613 RKLIEEMEEkqksdkaeLERMQQEVETQRKETEIVQlQIRKQEESLKRrsfhienkLKDLLAEKEKFEEERLREQQEIEL 692
Cdd:COG4913 228 DALVEHFDD--------LERAHEALEDAREQIELLE-PIRELAERYAA--------ARERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 693 QKKRQEEEtflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE----QYAKLELEKKRLEEQEKEQVMLVAHLEEQ 768
Cdd:COG4913 291 ELLEAELE---ELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 769 LR-------EKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRffEFKRRQlvklVNLEK 841
Cdd:COG4913 368 LAalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIA--SLERRK----SNIPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 842 DLVQQKDILKK----------------EVQEEQEI----LEclKCEHDKESRLL--EKHDESVTD--------------- 884
Cdd:COG4913 441 RLLALRDALAEalgldeaelpfvgeliEVRPEEERwrgaIE--RVLGGFALTLLvpPEHYAAALRwvnrlhlrgrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 885 VTEVPQDFEKIKPVE----YRLQYKERQLQYLLQNHL-----------PTLLEEKQRA-------------FEILDRGPL 936
Cdd:COG4913 519 VRTGLPDPERPRLDPdslaGKLDFKPHPFRAWLEAELgrrfdyvcvdsPEELRRHPRAitragqvkgngtrHEKDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 937 S------LDNTlyqvekemeekeEQLAQYQAnanQLQKLQATFEFTANIARQEekvrkkekeileSREKQQREALERALA 1010
Cdd:COG4913 599 RsryvlgFDNR------------AKLAALEA---ELAELEEELAEAEERLEAL------------EAELDALQERREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1011 RLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLE---AEQEALEKDQERLEYEIQQLKQKIYEVDGVQKD 1087
Cdd:COG4913 652 RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEeleAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1088 HHGTLEGKVAssslpvsAEKSHLVPLMDARINAYIEEEVQRRLQDlhrvisegcSTSADTMKDNEKLHNgtIQRKLKYEK 1167
Cdd:COG4913 732 LQDRLEAAED-------LARLELRALLEERFAAALGDAVERELRE---------NLEERIDALRARLNR--AEEELERAM 793
|
....*..
gi 530425794 1168 RQFCPAW 1174
Cdd:COG4913 794 RAFNREW 800
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
598-1169 |
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 530425794 598 FERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRrsfhIENKLKdllA 674
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaEEARKAEDAKRVEIARKAEDARK----AEEARK---A 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 675 EKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKRLE 752
Cdd:PTZ00121 1173 EDAK------------KAEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 753 EQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 832
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 833 LVKlvNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESvTDVTEVPQDFEKIKPVEYRLQYKERQLQYL 912
Cdd:PTZ00121 1319 EAK--KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 913 LQNHLPtllEEKQRAFEILDRgplsldntlyQVEKEMEEKEEQLAQYQANANQLQKlqatfefTANIARQEEKVRKKEKE 992
Cdd:PTZ00121 1396 AKKKAE---EDKKKADELKKA----------AAAKKKADEAKKKAEEKKKADEAKK-------KAEEAKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 993 ILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQ----EALEKDQERLE 1068
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEakkaDEAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1069 YEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEevqRRLQDLHRVISEGCSTSADTM 1148
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEA 1612
|
570 580
....*....|....*....|.
gi 530425794 1149 KDNEKLHNGTIQRKLKYEKRQ 1169
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKK 1633
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
596-862 |
1.23e-08 |
|
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: 58.78 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 596 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhIENKLKDLLAE 675
Cdd:pfam13868 91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 676 KEKFeeerlreqqeiELQKKRQEEEtFLRVQEELQRLKELNNNEKAEKFQIFQELdqLQKEKDEQYAKLELEKKrlEEQE 755
Cdd:pfam13868 168 EEER-----------EAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEA--EKKA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 756 KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVK 835
Cdd:pfam13868 232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAA 308
|
250 260
....*....|....*....|....*..
gi 530425794 836 LVNLEkdlVQQKDILKKEVQEEQEILE 862
Cdd:pfam13868 309 EREEE---LEEGERLREEEAERRERIE 332
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
600-776 |
1.88e-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: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKF 679
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 680 EEERLREQQE---------IELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 748
Cdd:COG1579 79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180
....*....|....*....|....*...
gi 530425794 749 KRLEEQEKEqvmLVAHLEEQLREKQEMI 776
Cdd:COG1579 159 EELEAEREE---LAAKIPPELLALYERI 183
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
601-1094 |
2.10e-08 |
|
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: 59.42 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 601 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQEEslkrrsfhienklkdLLAEKEKFe 680
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLC---EEKNALQEQLQAETE---------------LCAEAEEM- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 681 eerlreqqEIELQKKRQEEETFL-----RVQEELQRLKELnNNEKAEKFQIFQELDQ-----------LQKEK------- 737
Cdd:pfam01576 63 --------RARLAARKQELEEILhelesRLEEEEERSQQL-QNEKKKMQQHIQDLEEqldeeeaarqkLQLEKvtteaki 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 738 ----------DEQYAKLELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMI-----QLLRRGEVQWVEEEK--RDL 794
Cdd:pfam01576 134 kkleedilllEDQNSKLSKERKLLEERISEFTSNLAEEEEkakslsKLKNKHEAMisdleERLKKEEKGRQELEKakRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 795 EG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFE--FKRRQLVK--------LVNLEKDLVQQKDILKKEVQE 856
Cdd:pfam01576 214 EGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEetAQKNNALKkireleaqISELQEDLESERAARNKAEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 857 EQ---EILECLKCE----HDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFE 929
Cdd:pfam01576 294 RRdlgEELEALKTEledtLDTTAAQQELRSKREQEVTELK------KALEEETRSHEAQLQEMRQKH-TQALEELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 930 ILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN-----------QLQKLQATFEFTANIARQEEKVRKKEKEILESRE 998
Cdd:pfam01576 367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehkrkklegQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 999 KQQREAlERALARLERRHSAL--QRHSTLGMEIEEQRQKLA---SLNSGSREQSGLQASLEAEQEAlekdQERLEYEIQQ 1073
Cdd:pfam01576 447 SLLNEA-EGKNIKLSKDVSSLesQLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEA----KRNVERQLST 521
|
570 580
....*....|....*....|.
gi 530425794 1074 LKQKIYEVDGVQKDHHGTLEG 1094
Cdd:pfam01576 522 LQAQLSDMKKKLEEDAGTLEA 542
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
608-822 |
2.26e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 608 KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfhienKLKDLLAEKEKfeeerlreq 687
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------KLQAEIAEAEA--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 688 qeiELQKKRQEEETFLRVQEE--------------------LQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELE 747
Cdd:COG3883 80 ---EIEERREELGERARALYRsggsvsyldvllgsesfsdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 748 KKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 822
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
598-1078 |
4.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 598 FERQQREELEKLESKRKlieemeEKQKSDKAELERMQQEVETQRKETEIVQlQIRKQEESLKRRSFHIENKLKDLLAEKE 677
Cdd:COG4717 47 LLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 678 KFEEERLREQQEIELQKKRQEEETF-LRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAELAELpERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 EQVmlvAHLEEQLREKQEmiqllrrgEVQWVEEEKRDLEGIRESLlrvkEARAGGDEDGEELEKAQLRFFEFkrRQLVKL 836
Cdd:COG4717 199 EEL---EELQQRLAELEE--------ELEEAQEELEELEEELEQL----ENELEAAALEERLKEARLLLLIA--AALLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 837 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEkhdesvtdvtevpQDFEKIKPVEYRLQYKERQLQYLLQNH 916
Cdd:COG4717 262 LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG-------------KEAEELQALPALEELEEEELEELLAAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 917 LPTLLEEKQRAFEILDRgplsldntlyqvekemeekeeqLAQYQANANQLQKLQAtfeftaniARQEEKVRKKEKEILES 996
Cdd:COG4717 329 GLPPDLSPEELLELLDR----------------------IEELQELLREAEELEE--------ELQLEELEQEIAALLAE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 997 REKQQREALERALARLERRHSALQRHSTLGMEIEEQR-QKLASLNSGSREQSGLQ-ASLEAEQEALEKDQERLEYEIQQL 1074
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLgELEELLEALDEEELEEElEELEEELEELEEELEELREELAEL 458
|
....
gi 530425794 1075 KQKI 1078
Cdd:COG4717 459 EAEL 462
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
580-795 |
7.12e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 57.27 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 580 SKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETQRKETEivqLQIRKQEESLK 659
Cdd:pfam15709 295 GRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 660 RrsfhiENKLKDLLaEKEKfeeerLREQQEIELQKKRQEEETFLRVQEEL-QRLKELNNNEKAEKFQ--IFQELDQLQKE 736
Cdd:pfam15709 370 R-----AEKMREEL-ELEQ-----QRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRK 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425794 737 KDEQYA-KLELEKKRLEEQE----KEQVMLVAHLEEQ----LREKQEMIQllrrgEVQWVEEEKRDLE 795
Cdd:pfam15709 439 KQQEEAeRAEAEKQRQKELEmqlaEEQKRLMEMAEEErleyQRQKQEAEE-----KARLEAEERRQKE 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-807 |
7.30e-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: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 596 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVqlqiRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERR 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 676 kekfeeerlreqqeIELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:TIGR02168 833 --------------IAATERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530425794 754 QEKEqvmlVAHLEEQLREKQEMIQLLRrgevQWVEEEKRDLEGIRESLLRVKEA 807
Cdd:TIGR02168 899 LSEE----LRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
354-1013 |
8.07e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 354 RAKNIINKPTINEDANVKLIRELRAEIARLKtlLAQGNQIALLDSPTALSMEEKLQQNEARVQELTK----EWTNKWNET 429
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGK--LTEEKEELEKQELKLLKDELELKKSEDLLKETQLvklqEQLELLLSR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 430 QNILKEQTLALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHC------ 503
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLvralte 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 504 IFENIGGTVTLIPLSGSQCSVNGVQIVEAT--HLNQGAVILLGRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSMTDLSK 581
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPIlnLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 582 SRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ--EVETQRKETEIVQLQIRKQEESLK 659
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQreKEELKKLKLEAEELLADRVQEAQD 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 660 RRSFHIENKLKDLLAEKEKfeeerlreqQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE 739
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEE---------EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 740 QyAKLELEKKRLEEQEKEQVmlvahLEEQLREKQEmiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELE 819
Cdd:pfam02463 804 R-ALEEELKEEAELLEEEQL-----LIEQEEKIKE-------------EELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 820 KAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKEsrLLEKHDESVTDVTEVPQDFEKIKPVE 899
Cdd:pfam02463 865 KEEL-----LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL--LEEKENEIEERIKEEAEILLKYEEEP 937
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 900 YRLQYKERQLQYLLQNHLPTLLEEkqrafeildrgplsldntlyqvekemeekeEQLAQYQANANQLQKLQATFEFTANI 979
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEER------------------------------NKRLLLAKEELGKVNLMAIEEFEEKE 987
|
650 660 670
....*....|....*....|....*....|....
gi 530425794 980 ARQEEKVRKKEKEILESREKQQREALERALARLE 1013
Cdd:pfam02463 988 ERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
597-1078 |
1.42e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrketeivqLQIRKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-----------AQLELQIASLNNEIERLEARLERLEDRR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKFeeerlreQQEIELQKKRQEEETFLRVQEELQRLKelnnnekaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02168 417 ERL-------QQEIEELLKKLEEAELKELQAELEELE--------------EELEELQEELERLEEALEELREELEEAEQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 EQVMLVAHLeEQLREKQEMIQ-LLRRGE-----VQWVEEEKRDLEGIRE---SLLRVK-------EARAGGDED---GEE 817
Cdd:TIGR02168 476 ALDAAEREL-AQLQARLDSLErLQENLEgfsegVKALLKNQSGLSGILGvlsELISVDegyeaaiEAALGGRLQavvVEN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 818 LEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDkesrlLEKHDESVTDVtevpqdfekikp 897
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD-----LVKFDPKLRKA------------ 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 898 VEYRL----------QYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ 967
Cdd:TIGR02168 618 LSYLLggvlvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 968 KLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERrhsALQRHSTLGMEIEEQRQKLASLNSGSREQS 1047
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEELEERLEEAE 774
|
490 500 510
....*....|....*....|....*....|.
gi 530425794 1048 GLQASLEAEQEALEKDQERLEYEIQQLKQKI 1078
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
556-792 |
2.00e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 556 EAAKLREKRKSGLLSsfslsMTDLSKSRENLSAVM--LYNpglEFeRQQREELEKLESKRKLIEEMEEKQksdkAELERM 633
Cdd:COG1340 58 EAQELREKRDELNEK-----VKELKEERDELNEKLneLRE---EL-DELRKELAELNKAGGSIDKLRKEI----ERLEWR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 634 QQ-EVETQRKETEIVQlQIRKQEESLKRR--SFHIENKLKDLLAEkekfeeerlreqqeieLQKKRQEEETFlrvQEELQ 710
Cdd:COG1340 125 QQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE----------------LKELRKEAEEI---HKKIK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 711 RLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEE 790
Cdd:COG1340 185 ELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE 264
|
..
gi 530425794 791 KR 792
Cdd:COG1340 265 LE 266
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
599-1167 |
2.06e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDllAEK 676
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKD--AEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:PTZ00121 1242 AK------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 --EQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 832
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 833 LVKLVNLEKDLVQQK---DILKKEVQEEQEILEC-LKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQ 908
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 909 LQyllQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEK 985
Cdd:PTZ00121 1470 KK---ADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 986 VRKKEKEILESREKQQREALERALARLERRHSALQRHSTLgMEIEEQR-QKLASLNSGSREQSGLQASLEAEQ----EAL 1060
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA-KKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAkikaEEL 1625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1061 EKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAE--KSHLVPLMDARINAYIEEEVQRRLQDLHRVIS 1138
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
570 580
....*....|....*....|....*....
gi 530425794 1139 EGCSTSADTMKDNEKLHNGTIQRKLKYEK 1167
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
597-1015 |
2.90e-07 |
|
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: 55.50 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLI-EEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENK------L 669
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveleeL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 670 KDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQ------RLKELNNNEKAEKFQIFQELDQLQKEK------ 737
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKlkniel 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 738 DEQYAKLELEKKRLEEQEKEQVM-LVAHLEEQLREKQEMIQLLRRGE-VQWVEEEKRD-LEGIRESLLRVKEARAGGDED 814
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIEnLEEKEMNLRDeLESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 815 GEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT----DVTEVPQ 890
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNklelELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 891 DFEKIKPvEYRLQYKERQLQYllqnhlPTLLEEKQRAFEILDRGP------------------LSLDNTLYQVEKEMEEK 952
Cdd:pfam05483 651 KFEEIID-NYQKEIEDKKISE------EKLLEEVEKAKAIADEAVklqkeidkrcqhkiaemvALMEKHKHQYDKIIEER 723
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425794 953 EEQLAQYQANANQLQKLQATFEFT-ANIARQEEKVRKKEKEILESREKQQREALERALARLERR 1015
Cdd:pfam05483 724 DSELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
600-977 |
3.90e-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: 55.03 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ------------EVETQRKETEIVQLQIRKQEESLKRrsfhIEN 667
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQ----LNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 668 KLKDLlaEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE-LQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLEL 746
Cdd:TIGR04523 343 QISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 747 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQlRF 825
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------ELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQ-KE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 826 FEFKRRQLVKLVNLEKDLVQQKDILKKEV---QEEQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrL 902
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKIsslKEKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---I 563
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 903 QYKERQLQYLLQNHlpTLLEEKQRAFEILdrgplsldntlyqvekemeekeeqLAQYQANANQLQKLQATFEFTA 977
Cdd:TIGR04523 564 DEKNKEIEELKQTQ--KSLKKKQEEKQEL------------------------IDQKEKEKKDLIKEIEEKEKKI 612
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
599-859 |
4.75e-07 |
|
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: 54.27 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEKQKsdkaeleRMQQEVETQRKEteivQLQIRKQEESLKRRsfHIENKLKDLLAEKEK 678
Cdd:pfam15558 72 ARLGREERRRADRREKQVIEKESRWR-------EQAEDQENQRQE----KLERARQEAEQRKQ--CQEQRLKEKEEELQA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 FEEERLREQQEIELQ--KKRQEEETflrvqEELQRLKELNNNEKAEKFQIFQELDqLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:pfam15558 139 LREQNSLQLQERLEEacHKRQLKER-----EEQKKVQENNLSELLNHQARKVLVD-CQAKAEELLRRLSLEQSLQRSQEN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 757 -EQVMLVAHLEEQLREKQEMIQLLRrgeVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQlrffefkRRQLV 834
Cdd:pfam15558 213 yEQLVEERHRELREKAQKEEEQFQR---AKWRAEEKeEERQEHKEALAELADRKIQQARQVAHKTVQD-------KAQRA 282
|
250 260
....*....|....*....|....*
gi 530425794 835 KLVNLEKDLVQQkdILKKEVQEEQE 859
Cdd:pfam15558 283 RELNLEREKNHH--ILKLKVEKEEK 305
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
599-877 |
4.83e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEk 678
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLQ- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 feeerlreqqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE-----QYAKLELEKKRLEE 753
Cdd:COG4372 108 --------------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleeqlESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 754 QEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRR 831
Cdd:COG4372 174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDslEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 530425794 832 QLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEK 877
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
471-551 |
4.97e-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: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716 16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90
|
...
gi 530425794 549 FRF 551
Cdd:COG1716 91 LRF 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
788-1095 |
5.87e-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: 54.68 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 788 EEEKRDLEGIRESLLRVKEARaggdedgEELEKaQLRFFEFKRRQLVKLVNLEKDLVQ-QKDILKKEVQEEQEILECLKc 866
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDIL-------NELER-QLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQ- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 867 ehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQ---YLLQNHLPTLLEEKQRA---FEILDRGPLSLDN 940
Cdd:TIGR02168 246 --EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQQKQILrerLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 941 TLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarqeekvrkkekeILESREKQQREALERALARLERrhsalq 1020
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLE------------------AELEELEAELEELESRLEELEE------ 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 1021 rhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDgvQKDHHGTLEGK 1095
Cdd:TIGR02168 380 -------QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEEL 445
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
600-792 |
6.47e-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: 53.61 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETE----IVQLQIRKQEESLKRRSFHIENKLK----- 670
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelaELEKEIAELRAELEAQKEELAELLRalyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 671 ------DLLAEKEKFEEERLREQQEIELQKKRQEE-ETFLRVQEELQRLKELNNNEKAEKFQIFQE-------LDQLQKE 736
Cdd:COG4942 117 grqpplALLLSPEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAEleeeraaLEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530425794 737 KDEQYAKLELEKKRLEEQekeqvmlvahLEEQLREKQEMIQLLRRGEVQWVEEEKR 792
Cdd:COG4942 197 RQKLLARLEKELAELAAE----------LAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
451-554 |
9.82e-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: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGRDDASTEQ-DIVLHGLDLESEHCI-----------FENIGGT-- 511
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530425794 512 --VTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712 76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
595-1080 |
1.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 595 GLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIR----KQEESLKRRSFHIENKLK 670
Cdd:COG4913 280 ALRLWFAQR----RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 671 DLLAEKEKFEEERLREQQEIELqkkrqEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKR 750
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 751 LEEQ----EKEQVMLVAHLEEQLREKQ-------EMIQLlRRGEVQW----------------VEEE----------KRD 793
Cdd:COG4913 431 LERRksniPARLLALRDALAEALGLDEaelpfvgELIEV-RPEEERWrgaiervlggfaltllVPPEhyaaalrwvnRLH 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 794 L------EGIRESLLRVKEARAGGD------------------------------EDGEELE------------KAQLRF 825
Cdd:COG4913 510 LrgrlvyERVRTGLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRrhpraitragqvKGNGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 826 FE-----FKRRQLV-------KLVNLEKDLVQqkdiLKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDFE 893
Cdd:COG4913 590 HEkddrrRIRSRYVlgfdnraKLAALEAELAE----LEEELAEAEERLE----ALEAELDALQERREALQRLAEYSWDEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 894 KIKPVEYRLQYKERQLQYLLQNH--LPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA 971
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSddLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 972 TFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGME-------------------IEEQ 1032
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldadlesLPEY 817
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 530425794 1033 RQKLASLnsgsrEQSGLqasLEAEQEALEKDQERLEYEIQQLKQKIYE 1080
Cdd:COG4913 818 LALLDRL-----EEDGL---PEYEERFKELLNENSIEFVADLLSKLRR 857
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
604-1078 |
1.16e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 604 EELEKLESKRKLI--EEMEEKQKSDK--AELERMQQEVETQR-----KETEIVQL--QIRKQEESLKRRSFHIENKLKDL 672
Cdd:TIGR04523 75 NKIKILEQQIKDLndKLKKNKDKINKlnSDLSKINSEIKNDKeqknkLEVELNKLekQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 673 LAEKEKFEeerlreqqeiELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQKeKDEQYAKLELEKKRL 751
Cdd:TIGR04523 155 EKLNNKYN----------DLKKQKEELENELnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 752 EEQEKEqvmlvahLEEQLREKQEMIQllrrgevqwveEEKRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRr 831
Cdd:TIGR04523 224 KKQNNQ-------LKDNIEKKQQEIN-----------EKTTEISNTQTQLNQLKDEQ---NKIKKQLSEKQKELEQNNK- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 832 qlvKLVNLEKDLVQQK-DILKKEVQEEQEILECLKCEHDKESRLLE-------KHDESVTDVTEVPQDFEK-IKPVEYRL 902
Cdd:TIGR04523 282 ---KIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEeiqnqisQNNKIISQLNEQISQLKKeLTNSESEN 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 903 QYKERQLQYLlQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQK----LQATFEF 975
Cdd:TIGR04523 359 SEKQRELEEK-QNEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKeierLKETIIK 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 976 TANIARQEEKVRKKEKEILESRE------KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGL 1049
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDntreslETQLKVLSRSINKIKQNLEQKQK------ELKSKEKELKKLNEEKKELEEK 511
|
490 500
....*....|....*....|....*....
gi 530425794 1050 QASLEAEQEALEKDQERLEYEIQQLKQKI 1078
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
590-1067 |
1.34e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.67 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 590 MLYNPGLEFERQQREELEKLESKRKLIEEMEEKqksdkaeLERMQQEVetQRKETEIVQLQIR-----KQEESLKRrsfH 664
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNK-------IDQLKQEL--SKKESELLALQTKletltNQNSDCKQ---H 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 665 IEnKLKDLLAEKEKfeEERLREQQEIELQKKRQEEETFL-RVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAK 743
Cdd:pfam10174 326 IE-VLKESLTAKEQ--RAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 744 LELEKKRLEeqekeqvmlvaHLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 823
Cdd:pfam10174 396 INVLQKKIE-----------NLQEQLRDKDKQLAGLKER----VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 824 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQE-EQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 902
Cdd:pfam10174 461 REDRERLEELESLKKENKDLKEKVSALQPELTEkESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 903 QyKERQLQY-------------LLQNHLPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 969
Cdd:pfam10174 541 K-KAHNAEEavrtnpeindrirLLEQEVARYKEESGKAQAEVER----LLGILREVENEKNDKDKKIAELESLTLRQMKE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 970 QATfeFTANI-ARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHStlgMEIEEQRQKLASLNSGSREQSG 1048
Cdd:pfam10174 616 QNK--KVANIkHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTR---QELDATKARLSSTQQSLAEKDG 690
|
490 500
....*....|....*....|....
gi 530425794 1049 LQASLEAE-----QEALEKDQERL 1067
Cdd:pfam10174 691 HLTNLRAErrkqlEEILEMKQEAL 714
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
616-789 |
1.60e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.94 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 616 IEEMEEKQKSDkaELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKfeeerLREQQEIELQKK 695
Cdd:COG2433 382 LEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDE-----RIERLERELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 696 RQEEETFLRVQEELQRLKELNNNEKAEkfqifqeLDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLE----EQLRE 771
Cdd:COG2433 454 RSEERREIRKDREISRLDREIERLERE-------LEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEkftkEAIRR 526
|
170
....*....|....*...
gi 530425794 772 KQEMIqLLRRGEVQWVEE 789
Cdd:COG2433 527 LEEEY-GLKEGDVVYLRD 543
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
600-929 |
4.58e-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: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE-ESLKRRSFHIENK 668
Cdd:pfam13868 2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 669 LKDLLAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnnNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 748
Cdd:pfam13868 82 IEEREQKRQE------------EYEEKLQEREQMDEIVERIQE------EDQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 749 KRLEEQEKEQVMLVahlEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLrffEF 828
Cdd:pfam13868 144 ELEKEEEREEDERI---LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ---ER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 829 KRRQlvklvnLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESvtdvtEVPQDFEKIKPVEYRLQYKERQ 908
Cdd:pfam13868 218 KERQ------KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFE-----RMLRKQAEDEEIEQEEAEKRRM 286
|
330 340
....*....|....*....|.
gi 530425794 909 LQYLLQNHLPTLLEEKQRAFE 929
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRA 307
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
709-1080 |
4.60e-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: 51.66 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 709 LQRLKELNNNEKAEKFQIFQElDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvAHLEEQ--LREKQEMIQLLRRGEVQW 786
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVE-RRRKLEEAEKARQ---AEMDRQaaIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 787 V--EEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEEqeilecl 864
Cdd:pfam17380 353 IrqEERKRELERIRQEEIAMEISRM------RELERLQM-----ERQQKNERVRQELEAARKVKILEEERQRK------- 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 865 kcehdkesrllekhdesvtdVTEVPQDFEKIKpveyRLQYKERQLQyllqnhLPTLLEEKQRAFEILDRgplsldntlyq 944
Cdd:pfam17380 415 --------------------IQQQKVEMEQIR----AEQEEARQRE------VRRLEEERAREMERVRL----------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 945 vekemeekeeqlaQYQANANQLQKLqatfeftaniaRQEEKVRKKEKEILESREKQQREALEralarlerrhsalQRHST 1024
Cdd:pfam17380 454 -------------EEQERQQQVERL-----------RQQEEERKRKKLELEKEKRDRKRAEE-------------QRRKI 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530425794 1025 LGMEIEEQRQKLAslnSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1080
Cdd:pfam17380 497 LEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
576-1077 |
4.61e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 576 MTDLSKSRENL--------------------SAVMLYNPGL-EFERQQREELEKLESK-RKLIEEMEEKQKSDKAELERM 633
Cdd:pfam05483 25 KSNLSKNGENIdsdpafqklnflpmleqvanSGDCHYQEGLkDSDFENSEGLSRLYSKlYKEAEKIKKWKVSIEAELKQK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 634 QQEVETQRKETE-----IVQLQIRKQEESLKRRSFHIENklKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRvQEE 708
Cdd:pfam05483 105 ENKLQENRKIIEaqrkaIQELQFENEKVSLKLEEEIQEN--KDLIKENNATRHLCNLLKETCARSAEKTKKYEYER-EET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 709 LQRLKELNNNekAEKFQI-FQELdQLQKEKdeqyAKLELEKKRLEEQEKEQvmlvaHLEE----QLREKQEMIQLLRrge 783
Cdd:pfam05483 182 RQVYMDLNNN--IEKMILaFEEL-RVQAEN----ARLEMHFKLKEDHEKIQ-----HLEEeykkEINDKEKQVSLLL--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 784 VQWVEEEKRdlegIRESLLRVKEAR--AGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 861
Cdd:pfam05483 247 IQITEKENK----MKDLTFLLEESRdkANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 862 ECLKCE--HDKESRLLE------KHDESVTDVTEVPQDFEKIKPVE-YRLQYKERQLQYLlqnhlptLLEEKQRAFEild 932
Cdd:pfam05483 323 TKTICQltEEKEAQMEElnkakaAHSFVVTEFEATTCSLEELLRTEqQRLEKNEDQLKII-------TMELQKKSSE--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 933 rgplsldntLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARL 1012
Cdd:pfam05483 393 ---------LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 1013 ERRHSALQRHSTLGMEIEEQRQKLASLNSGS-----------REQSGLQASLEAEQEAL---EKDQERLEYEIQQLKQK 1077
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIELTAHCdklllenkeltQEASDMTLELKKHQEDIincKKQEERMLKQIENLEEK 542
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
576-913 |
7.13e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 576 MTDLSKSRENLSAVMLYNPGLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQrkETEIVQLQIR-- 652
Cdd:pfam15921 450 MAAIQGKNESLEKVSSLTAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT--NAEITKLRSRvd 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 653 ---KQEESLKRRSFHIEN------KLKDLLAEKEKFeeerlreqqeIELQKKRQEEETFLRVQ----------EELQRLK 713
Cdd:pfam15921 528 lklQELQHLKNEGDHLRNvqteceALKLQMAEKDKV----------IEILRQQIENMTQLVGQhgrtagamqvEKAQLEK 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 714 ELNNNEkaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE----KQEMIQLLR-----RGEV 784
Cdd:pfam15921 598 EINDRR--------LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNEL 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 785 QWVEEE----KRDLEGIRESL--------LRVKEARAggdedgeELEKAQ--LRFFEFKRRQLVKL-VNLEKDLVQQK-- 847
Cdd:pfam15921 670 NSLSEDyevlKRNFRNKSEEMetttnklkMQLKSAQS-------ELEQTRntLKSMEGSDGHAMKVaMGMQKQITAKRgq 742
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530425794 848 -DILKKEVQ-EEQEILECLKCEH---DKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 913
Cdd:pfam15921 743 iDALQSKIQfLEEAMTNANKEKHflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
604-820 |
8.09e-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: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 604 EELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 683
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 684 LREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyaklelekkrlEEQEKEQVMLVA 763
Cdd:TIGR02169 892 DELEAQLRELERKIEE-----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE------------DEEIPEEELSLE 954
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425794 764 HLEEQLREKQEMIQLLrrGEV-----QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK 820
Cdd:TIGR02169 955 DVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
599-753 |
1.12e-05 |
|
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: 47.34 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETQRKETEivqlqiRKQEESLKRRSfHIENKLKDLLAEKEK 678
Cdd:pfam05672 28 EREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE------RRREEEERQRK-AEEEAEEREQREQEE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 679 feeerlreqqEIELQKKRQEEETFLRVQEELQRLkelnnnekaEKFQIFQELDQLQKEKdeqyakleleKKRLEE 753
Cdd:pfam05672 96 ----------QERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER----------KKRIEE 141
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
577-929 |
1.17e-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: 50.40 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 577 TDLSKSRENLSavmlyNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEE 656
Cdd:TIGR04523 345 SQLKKELTNSE-----SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 657 SLKRrsfhIENKLKDLLAEKEKFEEERLREQQEI--------ELQKKRQEEETFLRV---------------QEEL-QRL 712
Cdd:TIGR04523 420 EKEL----LEKEIERLKETIIKNNSEIKDLTNQDsvkeliikNLDNTRESLETQLKVlsrsinkikqnleqkQKELkSKE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 713 KELN--NNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ---------EKEQVMLVAHLEEQLREKQEMIqllrr 781
Cdd:TIGR04523 496 KELKklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKisdledelnKDDFELKKENLEKEIDEKNKEI----- 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 782 geVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK-----AQL-RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQ 855
Cdd:TIGR04523 571 --EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEkekkiSSLeKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425794 856 EEQEILECLKcehDKESRLLEKHDESVTDVTEVPQDFEKIKPvEYRLQYKERQLQYLLQNHLPtLLEEKQRAFE 929
Cdd:TIGR04523 649 QIKETIKEIR---NKWPEIIKKIKESKTKIDDIIELMKDWLK-ELSLHYKKYITRMIRIKDLP-KLEEKYKEIE 717
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
599-833 |
1.22e-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: 49.53 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESK-RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhiENKLKDLLAEKE 677
Cdd:pfam13868 108 ERIQEEDQAEAEEKlEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEER----EAEREEIEEEKE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 678 KfEEERLREQQEIELQKKRQEEE-TFLRVQEELQ---RLKELNNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:pfam13868 184 R-EIARLRAQQEKAQDEKAERDElRAKLYQEEQErkeRQKEREEAEKKARQR--QELQQAREEQIELKERRLAEEAEREE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 754 QEKEQVMLV----AHLEEQLREKQEMIQLLRRGEVQWVEEEKRdlegiRESLLRVKEARAGGDEDGEELEKAQLRFFEFK 829
Cdd:pfam13868 261 EEFERMLRKqaedEEIEQEEAEKRRMKRLEHRRELEKQIEERE-----EQRAAEREEELEEGERLREEEAERRERIEEER 335
|
....
gi 530425794 830 RRQL 833
Cdd:pfam13868 336 QKKL 339
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
602-757 |
1.38e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 602 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 681
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425794 682 ERLreqqeiELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 757
Cdd:PRK12704 122 KQQ------ELEKKEEELEE--LIEEQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLikEIEEEAKEEADKK 189
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
599-862 |
1.39e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETQRKETEIVQLQIRKQEeslkrrsfhienKLKDLLAEKEK 678
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 feeerlreqqeielqKKRQEEETFLRVQEELQRlKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQ 758
Cdd:COG3064 78 ---------------KLAEAEKAAAEAEKKAAA-EKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 759 VMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVN 838
Cdd:COG3064 142 KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
250 260
....*....|....*....|....
gi 530425794 839 LEKDLVQQKDILKKEVQEEQEILE 862
Cdd:COG3064 222 AARAAAASREAALAAVEATEEAAL 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
601-1138 |
1.46e-05 |
|
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: 50.22 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 601 QQREELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQ-RKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEkf 679
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREARDRQL---AVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE-- 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 680 eeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLEEQEKEqv 759
Cdd:pfam12128 462 -----------LLLQLENFDERIERAREEQEA-----ANAEVERLQ--SELRQARKRRDQASEALRQASRRLEERQSA-- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 760 mlVAHLEEQLREKQ-EMIQLLRRGEVQWVEEEKRDLEgiRESLLR---VKEARAGGDEDGEELEKAQLRffeFKRRQLVK 835
Cdd:pfam12128 522 --LDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVIS--PELLHRtdlDPEVWDGSVGGELNLYGVKLD---LKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 836 LVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpQDFEKIKPVEYRLQYKERQLQYLLQN 915
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQSEKDKKNK 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 916 HLPTLLEEKQRAFEILDRGPLSLDNT----LYQVEKEMEEKEEQLAQY-----QANANQLQKLQATFE-FTANIARQEEK 985
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQLKQLDKKhqawLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAaRRSGAKAELKA 751
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 986 VRKKEKEILESRE---------KQQREALERALARLE-RRHSALQRH------------------STLGMEIEEQRQKLA 1037
Cdd:pfam12128 752 LETWYKRDLASLGvdpdviaklKREIRTLERKIERIAvRRQEVLRYFdwyqetwlqrrprlatqlSNIERAISELQQQLA 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1038 SLNSGSREQsglQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDhhgtleGKVASSSLPVSAEKSHLVPLMDar 1117
Cdd:pfam12128 832 RLIADTKLR---RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED------ANSEQAQGSIGERLAQLEDLKL-- 900
|
570 580
....*....|....*....|.
gi 530425794 1118 INAYIEEEVQRRLQDLHRVIS 1138
Cdd:pfam12128 901 KRDYLSESVKKYVEHFKNVIA 921
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
595-753 |
1.58e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 595 GLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 674
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 675 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLK-ELNN----NEKAEkfqifQELDQLQKEKD---EQYAKLEL 746
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEE-----LERELERLErEIEAlgpvNLLAI-----EEYEELEERYDflsEQREDLEE 809
|
....*..
gi 530425794 747 EKKRLEE 753
Cdd:COG1196 810 ARETLEE 816
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
471-555 |
1.84e-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: 44.94 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87
|
....*..
gi 530425794 549 FRFNHPK 555
Cdd:pfam16697 88 FCLVPAD 94
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
597-1098 |
1.92e-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: 49.79 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKL-------IEEMEEKQKsdKAELERMQQEVETQRKETEIVQLQ-----IRKQEESLKRRSFH 664
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLknkheamISDLEERLK--KEEKGRQELEKAKRKLEGESTDLQeqiaeLQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 665 IENKLKDLLAEKEKfeeerlREQQEIELQKK-RQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE----KDE 739
Cdd:pfam01576 241 KEEELQAALARLEE------ETAQKNNALKKiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtLDT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 740 QYAKLELEKKRleeqEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELe 819
Cdd:pfam01576 315 TAAQQELRSKR----EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 820 KAQLRFF-------EFKRRQLVKLVNlekDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLE----KHDESVTDVTEV 888
Cdd:pfam01576 390 QAELRTLqqakqdsEHKRKKLEGQLQ---ELQARLSESERQRAELAEKLSKLQSELESVSSLLNeaegKNIKLSKDVSSL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 889 P---QDFEKIKPVEYR----LQYKERQLQYlLQNHLPTLLEEKQRAFEILDRgplsldntlyqvekemeekeeQLAQYQA 961
Cdd:pfam01576 467 EsqlQDTQELLQEETRqklnLSTRLRQLED-ERNSLQEQLEEEEEAKRNVER---------------------QLSTLQA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 962 nanQLQKLQATFEFTANIARQEEKVRKKEKEILESReKQQREALERALARLERRHSALQRH-STLGMEIEEQRQKLASLN 1040
Cdd:pfam01576 525 ---QLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL-TQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQRQLVSNLE 600
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425794 1041 SGSR-------EQSGLQASL-----EAEQEALEKDQE--RLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVAS 1098
Cdd:pfam01576 601 KKQKkfdqmlaEEKAISARYaeerdRAEAEAREKETRalSLARALEEALEAKEELERTNKQLRAEMEDLVSS 672
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
555-1139 |
1.98e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEK--QKSDKAELER 632
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDllKETQLVKLQE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 633 MQQEVETQRKETEIVQLQIRKQEES----------LKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETF 702
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLkvllalikdgVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 703 LRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRG 782
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 783 EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILE 862
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 863 CLKceHDKESRLLEKHDESVTDVTEVPQDFEKIKP-VEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNT 941
Cdd:pfam02463 725 DRV--QEAQDKINEELKLLKQKIDEEEEEEEKSRLkKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 942 LYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftaniaRQEEKVRKKEKEILES------REKQQREALERALARLERR 1015
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEK------------IKEEELEELALELKEEqkleklAEEELERLEEEITKEELLQ 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1016 HSALQRHSTL---------GMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQK 1086
Cdd:pfam02463 871 ELLLKEEELEeqklkdeleSKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 530425794 1087 DHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISE 1139
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
898-1085 |
2.89e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 898 VEYRLQYKERQLQY---LLQNHLPTL---LEEKQRAFEILDR--GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 969
Cdd:COG3206 162 LEQNLELRREEARKaleFLEEQLPELrkeLEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 970 QATFEftANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSAlqRHStlgmEIEEQRQKLASLNSG-SREQSG 1048
Cdd:COG3206 242 LAALR--AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHP----DVIALRAQIAALRAQlQQEAQR 313
|
170 180 190
....*....|....*....|....*....|....*..
gi 530425794 1049 LQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQ 1085
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
596-1078 |
2.91e-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: 48.97 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 596 LEFERQQREELEKleSKRKLIEEMEEKQKSDKAELERMQQevetqRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:pfam05557 43 LDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRL-----KKKYLEALNKKLNEKESQLADAREVISCLKNELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 676 kekfeeerlreqqeieLQKKRQEEETFLRVQE-ELQRLKELNNNEKA------EKFQIFQELDQLQKEKDEQYAKLELEk 748
Cdd:pfam05557 116 ----------------LRRQIQRAELELQSTNsELEELQERLDLLKAkaseaeQLRQNLEKQQSSLAEAEQRIKELEFE- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 749 krLEEQE---------KEQVMLVAHLEEQLREKQEMIQLLR--RGEVQWVEEEKrdlEGIRESLLRVKEARAGGDEDGEE 817
Cdd:pfam05557 179 --IQSQEqdseivknsKSELARIPELEKELERLREHNKHLNenIENKLLLKEEV---EDLKRKLEREEKYREEAATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 818 LEKAQLRFFEFK----------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILeclkcehdkeSRLLEKHDES 881
Cdd:pfam05557 254 KEKLEQELQSWVklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLEKAR----------RELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 882 VTDVTEVPQDFEKIKPVEYRLQ------YKERQL--QYL--------LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQV 945
Cdd:pfam05557 324 LKKIEDLNKKLKRHKALVRRLQrrvlllTKERDGyrAILesydkeltMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 946 EKEMEEKEEQLAQYQANANQLQKLQatfeftaniaRQEEKVRKKEKEILESREKQQREALERALARLERRHSALQrhstl 1025
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALR----------QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELE----- 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 530425794 1026 gMEIEEQR-QKLASLNSGSREQSGLQASLEAEQEALEkDQERLEYEIQQLKQKI 1078
Cdd:pfam05557 469 -MELERRClQGDYDPKKTKVLHLSMNPAAEAYQQRKN-QLEKLQAEIERLKRLL 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
579-771 |
3.51e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 579 LSKSRENLSAVMLynpglEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESL 658
Cdd:TIGR02169 831 LEKEIQELQEQRI-----DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 659 KRRSFHIEnKLKDLLAEKEKFEEERLREQQEIELQKKRQEE------------ETFLRVQEELQRLKELNNneKAEkfQI 726
Cdd:TIGR02169 906 EELEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRALEPVNM--LAI--QE 980
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530425794 727 FQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmLVAHLEEQLRE 771
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAILE-------RIEEYEKKKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
550-752 |
3.72e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 550 RFNHPKEAA---KLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLY----NPGLEFERQQREELEKLESKRKLiEEMEEK 622
Cdd:pfam17380 393 RVRQELEAArkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeERAREMERVRLEEQERQQQVERL-RQQEEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 623 QKSDKAELERMQQEvetqRKETEIVQLQIRKQE-ESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKR---QE 698
Cdd:pfam17380 472 RKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERrkqQE 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530425794 699 EETFLRVQEELQRLKElnnnEKAekfqifqELDQLQKEKDEQYAKLELEKKRLE 752
Cdd:pfam17380 548 MEERRRIQEQMRKATE----ERS-------RLEAMEREREMMRQIVESEKARAE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1078 |
4.09e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 841 KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpqdfeKIKPVEYRLQYKERQLQyllqnhlpTL 920
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR------RIRALEQELAALEAELA--------EL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 921 LEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK- 999
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAe 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1000 --QQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGsreqsglQASLEAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:COG4942 169 leAERAELEALLAELEEERAALEA------LKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALIARLEAE 235
|
.
gi 530425794 1078 I 1078
Cdd:COG4942 236 A 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
610-915 |
4.13e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 610 ESKRKLIEEMEEKQKsdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhienkLKDLLAEKEKfeeerlreqqe 689
Cdd:COG4372 31 EQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQ--------LEEELEELNE----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 690 iELQKKRQEEEtflRVQEELQRLKElnnnekaEKFQIFQELDQLQKEK---DEQYAKLELEKKRLEEQEKEQVMLVAHLE 766
Cdd:COG4372 88 -QLQAAQAELA---QAQEELESLQE-------EAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 767 EQLREKQEMIQLLRRG-EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKL-----VNLE 840
Cdd:COG4372 157 EQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLeaklgLALS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 841 KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQN 915
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
586-860 |
5.89e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 586 LSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhI 665
Cdd:COG4942 6 LLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 666 ENKLKDLLAEKEKFEEerlreqqeiELQKKRQEEETFLRVQEELQRLKE----LNNNEKAEKFQIFQELDQLQKEKDEQY 741
Cdd:COG4942 82 EAELAELEKEIAELRA---------ELEAQKEELAELLRALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 742 AKLELEKKRLEEQEKEqvmlvahLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIREsllrvkearaggdedgeeleka 821
Cdd:COG4942 153 EELRADLAELAALRAE-------LEAERAELEALLAEL--------EEERAALEALKA---------------------- 195
|
250 260 270
....*....|....*....|....*....|....*....
gi 530425794 822 qlrffefKRRQLVKlvNLEKDLVQQKDILKKEVQEEQEI 860
Cdd:COG4942 196 -------ERQKLLA--RLEKELAELAAELAELQQEAEEL 225
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
597-879 |
6.20e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRK----ETEIVQLQIRKQEESLKRRsfhienkLKDL 672
Cdd:pfam02029 10 ERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQggldEEEAFLDRTAKREERRQKR-------LQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 673 LAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNN--------NEKAEKFQIFQELDQLQKEKDEQYAKL 744
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRykeeeteiREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 745 ELEKKRLEEQE--KEQVMLVAHLEEqLREKQEMIQLLRRGEV------QWVEEEKRDLEGIRESLLRVKEARAGGDEDGE 816
Cdd:pfam02029 163 SEEAEEVPTENfaKEEVKDEKIKKE-KKVKYESKVFLDQKRGhpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530425794 817 ELEKAQLRfFEFKRRQLVKLVNLEKDLVQQKdilkkevQEEQEI-LECLKCEHDKESRLLEKHD 879
Cdd:pfam02029 242 VFLEAEQK-LEELRRRRQEKESEEFEKLRQK-------QQEAELeLEELKKKREERRKLLEEEE 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
665-809 |
6.80e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 665 IENKLKDLLAEKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQ--LQKEK--DEQ 740
Cdd:PRK12704 36 AEEEAKRILEEAKK------------EAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKEEnlDRK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 741 YAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLrrgevqwVEEEKRDLEGIreSLLRVKEARA 809
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. |
692-897 |
8.11e-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: 47.30 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 692 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlvahLEEQLR 770
Cdd:pfam05262 183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 771 EKQemiQLLRRGEVQWVEEEKRDLEgiresllrvkearaggdEDGEELEKAQLrffEFKRrqlvKLVNLEKDLVQQKDIL 850
Cdd:pfam05262 256 EAK---NLPKPADTSSPKEDKQVAE-----------------NQKREIEKAQI---EIKK----NDEEALKAKDHKAFDL 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 530425794 851 KKEVQEEQEILEclkcehdkesrllEKHDESVTDVTEVPQDFEKIKP 897
Cdd:pfam05262 309 KQESKASEKEAE-------------DKELEAQKKREPVAEDLQKTKP 342
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
600-856 |
9.25e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELekleskRKLIEEMEEKQKSDKAELERMQ-QEVETQRKETEIVQ-----LQIRKQEESLKRRSFHIENKLKDLL 673
Cdd:COG5022 806 LGSRKEY------RSYLACIIKLQKTIKREKKLREtEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVEL 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 674 AEKEKF-------------EEERLREQQEIELQKKRQE---EETFLRVqEELQRLKELNNNEKAEkfqifqELDQLQKEK 737
Cdd:COG5022 880 AERQLQelkidvksisslkLVNLELESEIIELKKSLSSdliENLEFKT-ELIARLKKLLNNIDLE------EGPSIEYVK 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 738 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDedgeE 817
Cdd:COG5022 953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQESTKQLKELPVEVA----E 1027
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530425794 818 LEKAQLRFFE--FKRRQLVKLVNLEKDLVQQKDILKKEVQE 856
Cdd:COG5022 1028 LQSASKIISSesTELSILKPLQKLKGLLLLENNQLQARYKA 1068
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
598-903 |
1.05e-04 |
|
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: 47.26 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 598 FERQQREELEKLEsKRKLIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRSFHIEN------KLK 670
Cdd:COG5185 217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDKLEkLVEQNTDLRLEKLGENAESSKRLNENANNlikqfeNTK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 671 DLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE----LQRLKELNNNE-----------KAEKFQIFQELDQLQK 735
Cdd:COG5185 296 EKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKREtetgIQNLTAEIEQGqesltenleaiKEEIENIVGEVELSKS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 736 EKDEQYAKLELEKKRLE------EQEKEQVMLVAHLEEQLREKQEMIQLLRR---GEVQWVEEEKRDLEGIRESLLRVKE 806
Cdd:COG5185 376 SEELDSFKDTIESTKESldeipqNQRGYAQEILATLEDTLKAADRQIEELQRqieQATSSNEEVSKLLNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 807 araggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQqkdiLKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVT 886
Cdd:COG5185 456 -----EADEESQSRLEEAYDEINRSVRSKKEDLNEELTQ----IESRVSTLKATLEKLR---AKLERQLEGVRSKLDQVA 523
|
330
....*....|....*..
gi 530425794 887 EVPQDFEKIKPVEYRLQ 903
Cdd:COG5185 524 ESLKDFMRARGYAHILA 540
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
612-757 |
1.56e-04 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 44.88 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 612 KRKLIEEMEEKQKSdKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKlKDLLAEKEKfeeerlrEQQEIE 691
Cdd:pfam12072 52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKK-EESLEKKEK-------ELEAQQ 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425794 692 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 757
Cdd:pfam12072 120 QQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL--LDEVEEELRHEAAVMikEIEEEAKEEADKK 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
604-1081 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 604 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKD---LLAEKEKFE 680
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 681 EERLREQQEIEL--QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQ---LQKEKDEQYAKLELEKKRLEeQE 755
Cdd:TIGR04523 225 KQNNQLKDNIEKkqQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLN-NQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 756 KEQVmLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEKRDLEGIRESLlrvKEARAGGDEDGEELEKAQLRFFEFKRRQ 832
Cdd:TIGR04523 304 KEQD-WNKELKSELKNQEKKLEEIQnqiSQNNKIISQLNEQISQLKKEL---TNSESENSEKQRELEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 833 LVKLVNLEK------DLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKiKPVEYRLQYKE 906
Cdd:TIGR04523 380 QSYKQEIKNlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN-QDSVKELIIKN 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 907 rqlqyllqnhLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarQEEKV 986
Cdd:TIGR04523 459 ----------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT-------KKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 987 RKKEKEILESREKQQREALERALARLERRHSALQRhSTLGMEIEEQRQKLaslnsgsrEQsglqasLEAEQEALEKDQER 1066
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-ENLEKEIDEKNKEI--------EE------LKQTQKSLKKKQEE 586
|
490
....*....|....*
gi 530425794 1067 LEYEIQQLKQKIYEV 1081
Cdd:TIGR04523 587 KQELIDQKEKEKKDL 601
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
611-883 |
1.88e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 611 SKRKLIEEMEEKQKSDKAELERMQQEVETQRKEteivqlqIRKQEESLKRRSFHIENKLKDLLAEKEkfeeerlreqqei 690
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQ------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 691 ELQKKRQEeetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE------QYAKLELEKKRLE----------EQ 754
Cdd:COG1340 61 ELREKRDE------LNEKVKELKEERDELNEKLNELREELDELRKELAElnkaggSIDKLRKEIERLEwrqqtevlspEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 755 EKEQVMLVAHLEEQLREKQEMiqllrrgevqwvEEEKRDLEGIRESLLRVK-EARAGGDEDGEELEKAQLrffefKRRQL 833
Cdd:COG1340 135 EKELVEKIKELEKELEKAKKA------------LEKNEKLKELRAELKELRkEAEEIHKKIKELAEEAQE-----LHEEM 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 530425794 834 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT 883
Cdd:COG1340 198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
695-1085 |
2.23e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 695 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQ-------ELDQLQKEKDeqyAKLELEKKRLEEQE--KEQVMLVAH- 764
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsvidlqtKLQEMQMERD---AMADIRRRESQSQEdlRNQLQNTVHe 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 765 -------LEEQLREKQEMIQLLRRGEVQwveeEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLV 837
Cdd:pfam15921 154 leaakclKEDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 838 NLEKDLVQ--------QKDILKKEVQEEQEILecLKCEHDKESRLLEKHDESVTDVTEVPQDFE-KIKPVEYRLQYKERQ 908
Cdd:pfam15921 230 DTEISYLKgrifpvedQLEALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEKASSARsQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 909 LQ-----YLLQ--------NHLPTLLEEKQRAFEI----LDRGPLSLDNTLYQVEKEMEekeeQLAQYQANAN-QLQKLQ 970
Cdd:pfam15921 308 ARnqnsmYMRQlsdlestvSQLRSELREAKRMYEDkieeLEKQLVLANSELTEARTERD----QFSQESGNLDdQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 971 ATFE------------------------FTANIARQEEKVRKKEKEILESREKQQRE----ALERALARLERRHSALQRH 1022
Cdd:pfam15921 384 ADLHkrekelslekeqnkrlwdrdtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1023 STLGMEIEEQRQKL-----------ASLNSGSREQSGLQASLEAEQEALE-------KDQERLEYEIQQLKQKIYEVDGV 1084
Cdd:pfam15921 464 SSLTAQLESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEKERAIEatnaeitKLRSRVDLKLQELQHLKNEGDHL 543
|
.
gi 530425794 1085 Q 1085
Cdd:pfam15921 544 R 544
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
600-1136 |
2.27e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKL-IEEMEEKQKSDKAELERMQQEVEtqrketeIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEk 678
Cdd:pfam15921 263 QQHQDRIEQLISEHEVeITGLTEKASSARSQANSIQSQLE-------IIQEQARNQNSMYMRQLSDLESTVSQLRSELR- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 feeerlreqqeielQKKRQEEETFlrvqEELQRLKELNNNE----KAEKFQIFQEL----DQLQK-----EKDEQYAKLE 745
Cdd:pfam15921 335 --------------EAKRMYEDKI----EELEKQLVLANSElteaRTERDQFSQESgnldDQLQKlladlHKREKELSLE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 746 LEK-KRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwveeekrdlegirESLLRVKEARAGGdedgeELEKaQLR 824
Cdd:pfam15921 397 KEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-------------------EALLKAMKSECQG-----QMER-QMA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 825 FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQeileclkcehdKESRLLEKHDESVTDVTevpqdfekikpveyrlqy 904
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT-----------AKKMTLESSERTVSDLT------------------ 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 905 kerqlqyllqnhlpTLLEEKQRAFEildrgplSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQAtfeftaniarqee 984
Cdd:pfam15921 503 --------------ASLQEKERAIE-------ATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT------------- 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 985 kvrkkekeilesrekqQREALERALARLERrhsalqrhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQ 1064
Cdd:pfam15921 549 ----------------ECEALKLQMAEKDK-------------VIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530425794 1065 ERLEYEIQQLKqkiyevdgVQKDHHGT----LEGKVASSSLpvsaEKSHLVPLMDARINAyIEEEVQRRLQDLHRV 1136
Cdd:pfam15921 600 NDRRLELQEFK--------ILKDKKDAkireLEARVSDLEL----EKVKLVNAGSERLRA-VKDIKQERDQLLNEV 662
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
605-901 |
2.46e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 605 ELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEE-------------SLKRRSFHIENKLKD 671
Cdd:TIGR00606 208 ELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHnlskimkldneikALKSRKKQMEKDNSE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 672 LLAEKEKFEEERLREQQEIELQKK---RQEEETFLRVQEELQRL---KELNNNEKAEkFQIFQELDQLQKEKDEQYAK-- 743
Cdd:TIGR00606 288 LELKMEKVFQGTDEQLNDLYHNHQrtvREKERELVDCQRELEKLnkeRRLLNQEKTE-LLVEQGRLQLQADRHQEHIRar 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 744 -----------------------------LELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR---RGEVQWVEEEK 791
Cdd:TIGR00606 367 dsliqslatrleldgfergpfserqiknfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekKGLGRTIELKK 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 792 RDLEGIRESLLRVKearaggdEDGEELEKAQLRFFEFK---RRQLVKLVNLEKD-LVQQKDILKKEVQEEQEILECLKCE 867
Cdd:TIGR00606 447 EILEKKQEELKFVI-------KELQQLEGSSDRILELDqelRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRKLRK 519
|
330 340 350
....*....|....*....|....*....|....*...
gi 530425794 868 HDKESRLLEKHDESVTDVTEVPQD----FEKIKPVEYR 901
Cdd:TIGR00606 520 LDQEMEQLNHHTTTRTQMEMLTKDkmdkDEQIRKIKSR 557
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
597-775 |
2.71e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhiENKLKDLLAEK 676
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---GEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKFEEERLREQQEIELQKKRQEEeTFLRVQEELQRLKELNNNE----KAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 752
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEfeklRQKQQEAELELEELKKKREERRKLLEEEEQRRK 301
|
170 180
....*....|....*....|...
gi 530425794 753 EQEKEQvmLVAHLEEQLREKQEM 775
Cdd:pfam02029 302 QEEAER--KLREEEEKRRMKEEI 322
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
746-1080 |
2.73e-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: 45.66 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 746 LEKKRLEEQEKEQVMLV--------AHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESL-LRVKEARAGGDEDGE 816
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVvpraellqNRLEECLQERAELLQAQEAANRQ-REKEKERYKRDREQWeRQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 817 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQE-EQEILEclkCEHDKESrLLEKHDESVTDVTEVPQDFEKI 895
Cdd:pfam07888 88 ELRQSREKHEELEEKY-KELSASSEELSEEKDALLAQRAAhEARIRE---LEEDIKT-LTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 896 KPVEYRLQYKERQLQYLLQ------NHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 969
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQqteeelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 970 QATFeftaNIARQEEKVRKKEKEILESREKQQREALERalARLERRHSALQRhSTLGMEIEEQRQKLAslnsgsREQSGL 1049
Cdd:pfam07888 243 QERL----NASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQL-ADASLALREGRARWA------QERETL 309
|
330 340 350
....*....|....*....|....*....|.
gi 530425794 1050 QASLEAEQEALEKdqerLEYEIQQLKQKIYE 1080
Cdd:pfam07888 310 QQSAEADKDRIEK----LSAELQRLEERLQE 336
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
692-810 |
2.85e-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: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 692 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAhlEEQLRE 771
Cdd:pfam11600 18 LEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLK--EEKRKE 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 530425794 772 KQEMIQlLRRGEVQWVEEEKRdlegIRESLLRVKEARAG 810
Cdd:pfam11600 96 KQEALE-AKLEEKRKKEEEKR----LKEEEKRIKAEKAE 129
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
613-777 |
2.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 613 RKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQlqirkQEESLKRRSfHIENKLKDLLAEkekfeeerlreQQEIEl 692
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEA-----KEEIHKLRN-EFEKELRERRNE-----------LQKLE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 693 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEE-----QEKEQVMLVAHLEE 767
Cdd:PRK12704 89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERisgltAEEAKEILLEKVEE 165
|
170
....*....|.
gi 530425794 768 QLR-EKQEMIQ 777
Cdd:PRK12704 166 EARhEAAVLIK 176
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
478-543 |
3.70e-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: 3.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498 1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
592-809 |
3.70e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 592 YNPGLEFERQQREELEKLESKrklIEEMEEKqksdKAELERMQQEVETQRKETEI-----VQLQIRKQEESLKRRSFHI- 665
Cdd:PRK05771 81 VKSLEELIKDVEEELEKIEKE---IKELEEE----ISELENEIKELEQEIERLEPwgnfdLDLSLLLGFKYVSVFVGTVp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 666 ENKLKDLLAEKEKFEEERLREQQE----IELQKKRQEEEtflrVQEELQRLkELNNNEKAEKFQIFQELDQLQKEKDEQY 741
Cdd:PRK05771 154 EDKLEELKLESDVENVEYISTDKGyvyvVVVVLKELSDE----VEEELKKL-GFERLELEEEGTPSELIREIKEELEEIE 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530425794 742 AKLELEKKRLEEQEKEQVMLVAHLEEQL---REKQEM-IQLLRRGEV----QWVEEEkrDLEGIRESLLRVKEARA 809
Cdd:PRK05771 229 KERESLLEELKELAKKYLEELLALYEYLeieLERAEAlSKFLKTDKTfaieGWVPED--RVKKLKELIDKATGGSA 302
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
473-551 |
3.78e-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: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 473 LKEGQTYVGRDDASteqDIVLHGLDLESEHC-IFENIGGTVTLIPLSGS-QCSVNGVQIVEATHLNQGAVILLGrTNMFR 550
Cdd:cd22673 18 LTKKSCTFGRDLSC---DIRIQLPGVSREHCrIEVDENGKAYLENLSTTnPTLVNGKAIEKSAELKDGDVITIG-GRSFR 93
|
.
gi 530425794 551 F 551
Cdd:cd22673 94 F 94
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
612-899 |
4.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 612 KRKLIEEMEEKQKSDKA-ELERMQQEVETQRKETEivqlqIRKQEESLKRRSFHIENKLKDLLAEKEKfeeerlreqqei 690
Cdd:PTZ00121 1062 AKAHVGQDEGLKPSYKDfDFDAKEDNRADEATEEA-----FGKAEEAKKTETGKAEEARKAEEAKKKA------------ 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 691 elQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEEQEKEQVMLVAhleEQLR 770
Cdd:PTZ00121 1125 --EDARKAEEA--RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE---DAKKAEAARKAEEVRKA---EELR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 771 EKQEM--IQLLRRGEVQWVEEEKRDLEGIR--ESLLRVKEARaggdEDGEELEKAQ--LRFFEFKRRQLVKLVNLEKDLV 844
Cdd:PTZ00121 1195 KAEDArkAEAARKAEEERKAEEARKAEDAKkaEAVKKAEEAK----KDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQA 1270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 845 QQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVE 899
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
599-880 |
4.74e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKL----IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLA 674
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ-RLKNDIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 675 EKEKfeeERLREQQEIELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQI-----FQELDQLQKEKDEQY----AKL 744
Cdd:TIGR00606 769 EQET---LLGTIMPEEESAKVCLTDVTIMeRFQMELKDVERKIAQQAAKLQGSdldrtVQQVNQEKQEKQHELdtvvSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 745 ELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR 824
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 825 ffefkRRQLVKLVNLEKDLVQQK-DILKKEVQEEQEILECL--KCEHDKESRLLEKHDE 880
Cdd:TIGR00606 925 -----KEELISSKETSNKKAQDKvNDIKEKVKNIHGYMKDIenKIQDGKDDYLKQKETE 978
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
610-761 |
4.93e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 610 ESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEiVQLQIRKQEESLKRRSFHIENklkdllAEKEKFEEERLREQQE 689
Cdd:pfam02029 206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE-VFLEAEQKLEELRRRRQEKES------EEFEKLRQKQQEAELE 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425794 690 IELQKKRQEEETFLRVQEELQRlkelnNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVML 761
Cdd:pfam02029 279 LEELKKKREERRKLLEEEEQRR-----KQEEAER--------KLREEEEKRRMKEEIERRRAEAAEKRQKLP 337
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
597-884 |
4.97e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE-----------------ESLK 659
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvleretelERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 660 RRSFHIENKLKDLLAEKEKFEEERLREQQEI-----ELQKKR----QEEETFLRVQEELQRLKELNNN---EKAEKFQIF 727
Cdd:pfam07888 157 ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslskEFQELRnslaQRDTQVLQLQDTITTLTQKLTTahrKEAENEALL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 728 QELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE-QLREKQEMIQL------LRRGEVQW----------VEEE 790
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQLTLQLadaslaLREGRARWaqeretlqqsAEAD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 791 KRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKeVQEEQEILECLKCEHDK 870
Cdd:pfam07888 317 KDRIEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV-AQKEKEQLQAEKQELLE 392
|
330
....*....|....
gi 530425794 871 ESRLLEKHDESVTD 884
Cdd:pfam07888 393 YIRQLEQRLETVAD 406
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
607-850 |
5.88e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 607 EKLESKRKLIEEMEEKQKSDKAELERMqqeVETQRKETEivqlQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 686
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNK---YDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 687 QQEIELQKKrqeEETFLRVQEE----LQRLKElnNNEKAEKfqIFQELDQLQKekdeqyaKLELEKKRLEEQEKeqvmlv 762
Cdd:PHA02562 268 KSKIEQFQK---VIKMYEKGGVcptcTQQISE--GPDRITK--IKDKLKELQH-------SLEKLDTAIDELEE------ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 763 ahLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVK----EARAGGDEDGEELEKAQlrffefkrRQLVKLVN 838
Cdd:PHA02562 328 --IMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKaaieELQAEFVDNAEELAKLQ--------DELDKIVK 393
|
250
....*....|..
gi 530425794 839 LEKDLVQQKDIL 850
Cdd:PHA02562 394 TKSELVKEKYHR 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
597-702 |
6.13e-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: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:COG4942 143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
90 100
....*....|....*....|....*.
gi 530425794 677 EKFEEERLREQQEIELQKKRQEEETF 702
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGF 248
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
607-807 |
6.73e-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: 43.72 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 607 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 686
Cdd:cd16269 87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 687 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLv 762
Cdd:cd16269 155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKaeaAEQERKLLEEQQRELEQK- 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 530425794 763 ahLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 807
Cdd:cd16269 228 --LEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
584-758 |
7.10e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 584 ENLSAVMLyNPGLEFERQQREELEKLESKRKliEEMEEKQKSDKAELERMQQEVETQR-----KETEIVQLQIRKQEESL 658
Cdd:PRK09510 48 SVIDAVMV-DPGAVVEQYNRQQQQQKSAKRA--EEQRKKKEQQQAEELQQKQAAEQERlkqleKERLAAQEQKKQAEEAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 659 KrrsfhienklkdLLAEKEKfeeerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKD 738
Cdd:PRK09510 125 K------------QAALKQK----------QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAA 181
|
170 180
....*....|....*....|
gi 530425794 739 EQYAKLELEKKRLEEQEKEQ 758
Cdd:PRK09510 182 EAKKKAEAEAAAKAAAEAKK 201
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
599-856 |
8.72e-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: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQ--LQIRKQEESLKRRSfhieNKLKDLLAEK 676
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRaiLESYDKELTMSNYS----PQLLERIEEA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKFEEERLREQQEIELQKKRQEEETFLRVQE------ELQRLKElnNNEKAEKFQIFQELDQLQKEKDEqyakLELEKKR 750
Cdd:pfam05557 386 EDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtlerELQALRQ--QESLADPSYSKEEVDSLRRKLET----LELERQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 751 LEEQEKEQVMLVAHLEeqLREKQEM-----IQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRF 825
Cdd:pfam05557 460 LREQKNELEMELERRC--LQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETT 537
|
250 260 270
....*....|....*....|....*....|....*
gi 530425794 826 FEFKRRQLVKL----VNLEKDLVQQKDILKKEVQE 856
Cdd:pfam05557 538 STMNFKEVLDLrkelESAELKNQRLKEVFQAKIQE 572
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
600-861 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 679
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 680 EEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQV 759
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 760 MLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEaraggDEDGEELEKAQLRFFEFKRRQLVKLVNL 839
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE-----EAALELKLLALLLNLAALSLIGALEDAL 317
|
250 260
....*....|....*....|..
gi 530425794 840 EKDLVQQKDILKKEVQEEQEIL 861
Cdd:COG4372 318 LAALLELAKKLELALAILLAEL 339
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
596-779 |
1.22e-03 |
|
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: 42.06 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 596 LEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESL---KRRSFHIEN 667
Cdd:pfam14988 6 LEYLAKKTEEKQKKIEKlwnqyVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALrpfAKLKESQER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 668 KLKDLLAEKEKFEEERLREQQEIELQkkRQEEETFLRVQEELQRLKEL---NNNEKAEKFQ----------------IFQ 728
Cdd:pfam14988 86 EIQDLEEEKEKVRAETAEKDREAHLQ--FLKEKALLEKQLQELRILELgerATRELKRKAQalklaakqalsefcrsIKR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530425794 729 ELDQLQKE---KDEQYAKLELEKKRLEEQEKeqvmlvahleeQLREKQEMIQLL 779
Cdd:pfam14988 164 ENRQLQKEllqLIQETQALEAIKSKLENRKQ-----------RLKEEQWYLEAL 206
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
705-1074 |
1.70e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 705 VQEELQRLKELN--------NNEKAEKFQIFQELDQLQKEKDEQYAKLeLEKKRLEEQEKEQVMLVAHLEEQLREKQEMI 776
Cdd:pfam13868 1 LRENSDELRELNskllaakcNKERDAQIAEKKRIKAEEKEEERRLDEM-MEEERERALEEEEEKEEERKEERKRYRQELE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 777 QLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLRFFEFKR-RQLVKLVNLEKDLVQQKDIlKKEVQ 855
Cdd:pfam13868 80 EQIEEREQKRQEEYEEKLQEREQMDEIVERIQE------EDQAEAEEKLEKQRQlREEIDEFNEEQAEWKELEK-EEERE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 856 EEQEILECLKcehDKESRLLEKHDESvtdvtevpqdfekikpveyRLQYKERQLqylLQNHLPTLLEEKQRAFEILDRgp 935
Cdd:pfam13868 153 EDERILEYLK---EKAEREEEREAER-------------------EEIEEEKER---EIARLRAQQEKAQDEKAERDE-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 936 lsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATF-EFTANIARQEEKVRKKEKEILESREKQQREALERALARLER 1014
Cdd:pfam13868 206 --LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAReEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530425794 1015 RHSALQRHST-LGMEIEEQRQKLAslnsgsREQSGLQASLEAEQEALEKDQERLEYEIQQL 1074
Cdd:pfam13868 284 RRMKRLEHRReLEKQIEEREEQRA------AEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
693-914 |
1.86e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 693 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE---QYAKLELEKKRLEEQEKEQVMLVAHLEEQL 769
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAlarRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 770 REKQEMIQ-----LLRRGEVQWVE-----EEKRDLEGIRESLLRVKEARAggdEDGEELekaqlrffefkRRQLVKLVNL 839
Cdd:COG4942 100 EAQKEELAellraLYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARR---EQAEEL-----------RADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530425794 840 EKDLVQQKDIL---KKEVQEEQEILECLKCEHDKEsrllekhdesvtdVTEVPQDFEKIKPVEYRLQYKERQLQYLLQ 914
Cdd:COG4942 166 RAELEAERAELealLAELEEERAALEALKAERQKL-------------LARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
600-716 |
2.04e-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: 42.82 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 600 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQ-EVETQRKETE-IVQLQIRKQEESlkrrsfhIENKLKDLLAEKE 677
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFErEREEIRESYEeKLRTELERQAEA-------HEEHLKDVLVEQE 389
|
90 100 110
....*....|....*....|....*....|....*....
gi 530425794 678 kfeeerlreqqeIELQKKRQEEETFLRVQEELQRLKELN 716
Cdd:pfam09731 390 ------------IELQREFLQDIKEKVEEERAGRLLKLN 416
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
600-678 |
2.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
621-781 |
2.41e-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: 41.20 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 621 EKQKSDKAELERMQQEVETqrKETEIVQLQIRKQEEslkrrsfHIEN-KLKDLLAEKEKfeeeRLREQQEIELQKKRQEE 699
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEE--KELEINELKAKYEEL-------RRENlEMRKIVAEFEK----TIAQMIEEKQKQKELEH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 700 ETFLRVQEELQRLK-ELNNNEKAeKFQIFQELDQlQKEKDEQYAKLELEKK--------RLEEQEKEQVMLVAHLEEQLR 770
Cdd:pfam05010 68 AEIQKVLEEKDQALaDLNSVEKS-FSDLFKRYEK-QKEVISGYKKNEESLKkcaqdylaRIKKEEQRYQALKAHAEEKLD 145
|
170
....*....|.
gi 530425794 771 EKQEMIQLLRR 781
Cdd:pfam05010 146 QANEEIAQVRS 156
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
613-771 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 613 RKLIEEMEEKQKSDKAELERMQ---------QEVETQRKETE--IVQ-----LQIRKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:COG4026 72 RELAEKFFEELKGMVGHVERMKlplghdveyVDVELVRKEIKnaIIRaglksLQNIPEYNELREELLELKEKIDEIAKEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 677 EKFEEERLreqqeiELQKKRQEeetflrVQEELQRLKElnnnekaekfqifqELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:COG4026 152 EKLTKENE------ELESELEE------LREEYKKLRE--------------ENSILEEEFDNIKSEYSDLKSRFEELLK 205
|
170
....*....|....*
gi 530425794 757 EQVMLVAHLEEQLRE 771
Cdd:COG4026 206 KRLLEVFSLEELWKE 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
955-1080 |
2.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 955 QLAQYQANaNQLQKLQATFEFTANIARQEEKVrkkekeiLESREKQQREALERALARLERRHSALQRH----STLGMEIE 1030
Cdd:PRK12704 56 KEALLEAK-EEIHKLRNEFEKELRERRNELQK-------LEKRLLQKEENLDRKLELLEKREEELEKKekelEQKQQELE 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 530425794 1031 EQRQKLASLNSGSREQ----SGLQASlEAEQEALEKDQERLEYEIQQLKQKIYE 1080
Cdd:PRK12704 128 KKEEELEELIEEQLQEleriSGLTAE-EAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
615-783 |
3.40e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 615 LIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRsfhIENKLKDLLAEKEKFEEErlreqqeIELQK 694
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELE----QKAEEAEALLKE---AEKLKEELEEKKEKLQEE-------EDKLL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 695 KRQEEEtflrVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAKLELE--KKRLEEQEKEqvmlvahLEEQLREK 772
Cdd:PRK00409 569 EEAEKE----AQQAIKEAKK-------EADEIIKELRQLQKGGYASVKAHELIeaRKRLNKANEK-------KEKKKKKQ 630
|
170
....*....|.
gi 530425794 773 QEMIQLLRRGE 783
Cdd:PRK00409 631 KEKQEELKVGD 641
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
601-678 |
3.91e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 601 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:PRK12704 68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
696-795 |
4.02e-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: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 696 RQEEETFLRVQEEL-QRLKELNNnekaekfqifqELDQLQKekdeqyaKLELEKKRLEEQEKEQVML---VAHLEEQLRE 771
Cdd:pfam08614 63 REELAELYRSRGELaQRLVDLNE-----------ELQELEK-------KLREDERRLAALEAERAQLeekLKDREEELRE 124
|
90 100 110
....*....|....*....|....*....|
gi 530425794 772 KQEMIQLLR------RGEVQWVEEEKRDLE 795
Cdd:pfam08614 125 KRKLNQDLQdelvalQLQLNMAEEKLRKLE 154
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
607-774 |
4.14e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.13 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 607 EKLESKRKlieEMEEKQKSDKAELERMQQEVETQRKeteivqlQIRKQEESLKRrsfhienklkdllAEKEKfeeerlre 686
Cdd:pfam20492 2 EEAEREKQ---ELEERLKQYEEETKKAQEELEESEE-------TAEELEEERRQ-------------AEEEA-------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 687 qqeIELQKKRQEEEtflrvqEELQRLKELNNNEKAEKFQIFQELDqlqkEKDEQYAKLELEKKRLEEQEKEqvmlvahLE 766
Cdd:pfam20492 51 ---ERLEQKRQEAE------EEKERLEESAEMEAEEKEQLEAELA----EAQEEIARLEEEVERKEEEARR-------LQ 110
|
....*...
gi 530425794 767 EQLREKQE 774
Cdd:pfam20492 111 EELEEARE 118
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
452-554 |
4.24e-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: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-------VTLIPLSGSQCSV 524
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 530425794 525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
767-1075 |
4.69e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 767 EQLREKQEMIQLlRRGEVQWVEEEKRD----LEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKD 842
Cdd:TIGR02169 173 EKALEELEEVEE-NIERLDLIIDEKRQqlerLRREREKAERYQALL---KEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 843 LVQQKDILKKEVQE-EQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFE-KIKPVEYRLQYKERQLQyllqnhlpTL 920
Cdd:TIGR02169 249 LEEELEKLTEEISElEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELE--------DA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 921 LEEKQRAFEILDRgplsldntlyqVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQ 1000
Cdd:TIGR02169 321 EERLAKLEAEIDK-----------LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 1001 QREALE---RALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREqsgLQASLEAEQEALEKDQERLEYEIQQLK 1075
Cdd:TIGR02169 390 YREKLEklkREINELKRELDRLQeELQRLSEELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
601-910 |
4.82e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 601 QQREELEklESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEkfe 680
Cdd:TIGR00618 577 QCDNRSK--EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL--- 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 681 eerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQ------ELDQLQKEKDEQYAKLELEKKRLEEQ 754
Cdd:TIGR00618 652 --------QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkeMLAQCQTLLRELETHIEEYDREFNEI 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 755 EKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQlRFFEFKRRQLV 834
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMH-------QARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLRE 795
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530425794 835 KLVNLEKDLVQQKDILKKEVQEEQEiLECLKCEHDKE---SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQ 910
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILN-LQCETLVQEEEqflSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
604-934 |
5.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 604 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETeivQLQIRKQEESLKRRSFHIENKLKDLLAEKEKfeeer 683
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQQRLAELEEELEE----- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 684 lrEQQEIE-LQKKRQEEETFLRVQEELQRLKEL--------------------------------------------NNN 718
Cdd:COG4717 218 --AQEELEeLEEELEQLENELEAAALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallfllLAR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 719 EKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKR---- 792
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeELQLEELEQEiaal 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 793 -------DLEGIRESLLRVKEARAG-----------GDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEV 854
Cdd:COG4717 376 laeagveDEEELRAALEQAEEYQELkeeleeleeqlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 855 QEEQEILECLkcEHDKE-SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLqykERQLQYLLQNHLPTLLEEKQRAFEILDR 933
Cdd:COG4717 456 AELEAELEQL--EEDGElAELLQELEELKAELRELAEEWAALKLALELL---EEAREEYREERLPPVLERASEYFSRLTD 530
|
.
gi 530425794 934 G 934
Cdd:COG4717 531 G 531
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
728-858 |
5.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 728 QELDQLqkekDEQYAKLELEKKRLE-EQEKEQVMLVAHLEEQLREKQEMIQLLRRgevQWvEEEKRDLEGIREsllrVKE 806
Cdd:COG0542 411 EELDEL----ERRLEQLEIEKEALKkEQDEASFERLAELRDELAELEEELEALKA---RW-EAEKELIEEIQE----LKE 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 530425794 807 ARAGGDEDGEELEKaqlrffefkrrqlvKLVNLEKDLVQQKDILKKEVQEEQ 858
Cdd:COG0542 479 ELEQRYGKIPELEK--------------ELAELEEELAELAPLLREEVTEED 516
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
609-1087 |
5.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 609 LESKRKLIEEMEEKQKSDKA-ELERmqqEVETQRKETEIVQlQIRKQEESLKRRSfHIENKLKDLLAEKEKfeeerlreq 687
Cdd:PRK04863 479 YQLVRKIAGEVSRSEAWDVArELLR---RLREQRHLAEQLQ-QLRMRLSELEQRL-RQQQRAERLLAEFCK--------- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 688 qeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLE-LEKKRLEEQEKeqvmlVAHLE 766
Cdd:PRK04863 545 ---RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAaRAPAWLAAQDA-----LARLR 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 767 EQLREKQE--------MIQLLRR-----GEVQWVEEEKRDLEGIRESLlrvkeARAGGDEDGE----------------- 816
Cdd:PRK04863 617 EQSGEEFEdsqdvteyMQQLLERereltVERDELAARKQALDEEIERL-----SQPGGSEDPRlnalaerfggvllseiy 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 817 ---ELEKA--------QLRF------FEFKRRQLVKLVNLEKDLvqqkdilkkevqeeqeilecLKCEHDKESrllekHD 879
Cdd:PRK04863 692 ddvSLEDApyfsalygPARHaivvpdLSDAAEQLAGLEDCPEDL--------------------YLIEGDPDS-----FD 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 880 ESVTDVTEvpqdFEKIKPVeyrlQYKERQLQYLLQNHLPtLLEEKQRafeildrgplslDNTLYQVEKEMEEKEEQLAQY 959
Cdd:PRK04863 747 DSVFSVEE----LEKAVVV----KIADRQWRYSRFPEVP-LFGRAAR------------EKRIEQLRAEREELAERYATL 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 960 QANANQLQKLQATFE----------FTAN------IARQEEKVRKKEKEILESREKQQREALERALARLerrhSALQRH- 1022
Cdd:PRK04863 806 SFDVQKLQRLHQAFSrfigshlavaFEADpeaelrQLNRRRVELERALADHESQEQQQRSQLEQAKEGL----SALNRLl 881
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530425794 1023 --------STLGMEIEEQRQKLASLNSGSR---EQSGLQASLEAEQEALEKDQERLEyeiqQLKQKIYEVDGVQKD 1087
Cdd:PRK04863 882 prlnlladETLADRVEEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQSDPEQFE----QLKQDYQQAQQTQRD 953
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
999-1108 |
5.82e-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: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 999 KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1078
Cdd:COG3883 139 KADKAELEAKKAELEAKLAELEA------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
90 100 110
....*....|....*....|....*....|
gi 530425794 1079 YEVDGVQKDHHGTLEGKVASSSLPVSAEKS 1108
Cdd:COG3883 213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
603-887 |
6.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 603 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsF--------HIENKLKDLLA 674
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER-FgdapvdlgNAEDFLEELRE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 675 EKEKFEEERLREQQEI-ELQKKRQEEETFL-------------------RVQEELQRLKELnnneKAEKFQIFQELDQLQ 734
Cdd:PRK02224 420 ERDELREREAELEATLrTARERVEEAEALLeagkcpecgqpvegsphveTIEEDRERVEEL----EAELEDLEEEVEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 735 K--EKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR---------------------------RGEVQ 785
Cdd:PRK02224 496 ErlERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaeekreaaaeaeeeaeeaREEVA 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 786 WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKaqLRffeFKRRQLVKLVNLEKDLVQQKDILKKEVQEE--QEILEC 863
Cdd:PRK02224 576 ELNSKLAELKERIESLERIRTLLAAIADAEDEIER--LR---EKREALAELNDERRERLAEKRERKRELEAEfdEARIEE 650
|
330 340
....*....|....*....|....
gi 530425794 864 LKCEHDKESRLLEKHDESVTDVTE 887
Cdd:PRK02224 651 AREDKERAEEYLEQVEEKLDELRE 674
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
609-779 |
6.86e-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: 40.51 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 609 LESKRKLIEEMEEKQKSD--------KAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIENKLKdLLAEKEKFE 680
Cdd:pfam09787 20 LQSKEKLIASLKEGSGVEgldsstalTLELEELRQERDLLREEIQ----KLRGQIQQLRTELQELEAQQQ-EEAESSREQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 681 EERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEkfqiFQELDQlQKEKDEQYAKLELEKKRL---EEQEKE 757
Cdd:pfam09787 95 LQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKAT----LQSRIK-DREAEIEKLRNQLTSKSQsssSQSELE 169
|
170 180
....*....|....*....|..
gi 530425794 758 QvmLVAHLEEQLREKQEMIQLL 779
Cdd:pfam09787 170 N--RLHQLTETLIQKQTMLEAL 189
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
596-661 |
7.10e-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: 40.35 E-value: 7.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530425794 596 LEFERQQREEleklESKRKLIEEmEEKQKSDKAELE------RMQQEVETQRKETEivqLQIRKQEESLKRR 661
Cdd:pfam12037 76 LKIERQRVEY----EERRKTLQE-ETKQKQQRAQYQdelarkRYQDQLEAQRRRNE---ELLRKQEESVAKQ 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
920-1080 |
7.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 920 LLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQatfeftaniarqeekvrkkekeilesrek 999
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELE----------------------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1000 QQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEaLEKDQERLEYEIQQLKQKIY 1079
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELE 180
|
.
gi 530425794 1080 E 1080
Cdd:COG4717 181 E 181
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
580-756 |
7.48e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 580 SKSRENLSAVMlYNPGL---EFERQQREElekleskrkliEEMEEKQKSDKAELERMQQEVETQRK--ETEIVQLQIRKQ 654
Cdd:TIGR02794 32 GGGAEIIQAVL-VDPGAvaqQANRIQQQK-----------KPAAKKEQERQKKLEQQAEEAEKQRAaeQARQKELEQRAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 655 EESLKRRsfhiENKLKDLLAEKEKfeeerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQ 734
Cdd:TIGR02794 100 AEKAAKQ----AEQAAKQAEEKQK----------QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAK 165
|
170 180
....*....|....*....|..
gi 530425794 735 KEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02794 166 KKAEEAKKKAEAEAKAKAEAEA 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
705-908 |
7.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 705 VQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMI-------- 776
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELgeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 777 -------------------QLLRRGE-VQWVEEEKRDLegiresLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKL 836
Cdd:COG3883 97 rsggsvsyldvllgsesfsDFLDRLSaLSKIADADADL------LEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425794 837 VNLEKDLVQQKDI---LKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQ 908
Cdd:COG3883 171 AELEAQQAEQEALlaqLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
604-1162 |
8.05e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 604 EELEKLESKR-KLIEEMEEKQKSDKAELERMQQEVE--TQRK---ETEIVQLQI---RKQEESLKRRSFHIENKLKDLLA 674
Cdd:TIGR00606 301 EQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRllNQEKtelLVEQGRLQLqadRHQEHIRARDSLIQSLATRLELD 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 675 EKEKFEEERLREQQEIELQKKRQEEETflrvqeelqRLKELNNNEKAEKFQIFQE-LDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQEDEA---------KTAAQLCADLQSKERLKQEqADEIRDEKKGLGRTIELKKEILEK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 754 Q----------------------EKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLE---------------- 795
Cdd:TIGR00606 452 KqeelkfvikelqqlegssdrilELDQELRKAERELSKAEKNSLTETLKK-EVKSLQNEKADLDrklrkldqemeqlnhh 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 796 -GIRESLLRVKEARAGGDED-------GEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKeVQEEQEILECLKCE 867
Cdd:TIGR00606 531 tTTRTQMEMLTKDKMDKDEQirkiksrHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNH 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 868 HDKESRLLEKHDESVTD-VTEV--PQDFE-KIKPVEYRLQYKERQLQYL------LQNHLPTLLEEKQRAFEILDR---- 933
Cdd:TIGR00606 610 INNELESKEEQLSSYEDkLFDVcgSQDEEsDLERLKEEIEKSSKQRAMLagatavYSQFITQLTDENQSCCPVCQRvfqt 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 934 -----------------GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILES 996
Cdd:TIGR00606 690 eaelqefisdlqsklrlAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 997 REKQqreaLERALARLERRHSALQRHST---LGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE--RLEYEI 1071
Cdd:TIGR00606 770 QETL----LGTIMPEEESAKVCLTDVTImerFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHEldTVVSKI 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 1072 QQLKQKIYEvdgvQKDHHGTLEGKvassslpVSAEKSHLVPLMD--ARINAYIE--EEVQRRLQDLHRVIS---EGCSTS 1144
Cdd:TIGR00606 846 ELNRKLIQD----QQEQIQHLKSK-------TNELKSEKLQIGTnlQRRQQFEEqlVELSTEVQSLIREIKdakEQDSPL 914
|
650
....*....|....*...
gi 530425794 1145 ADTMKDNEKLHNGTIQRK 1162
Cdd:TIGR00606 915 ETFLEKDQQEKEELISSK 932
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
603-775 |
9.03e-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: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 603 REELEKL-ESKRKLIEE---MEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKqeesLKRRSFHIENKLKDLLAEKEK 678
Cdd:pfam15066 369 KENVEELiEDKYNVILEkndINKTLQNLQEILANTQKHLQESRKEKETLQLELKK----IKVNYVHLQERYITEMQQKNK 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425794 679 feeerlREQQEIELQKKRQEEEtflrvqEELQRLKELNNN-EKAEKfqifQELDQLQKEKDEQyaklelEKKRLEEQEKE 757
Cdd:pfam15066 445 ------SVSQCLEMDKTLSKKE------EEVERLQQLKGElEKATT----SALDLLKREKETR------EQEFLSLQEEF 502
|
170
....*....|....*...
gi 530425794 758 QvmlvAHLEEQLREKQEM 775
Cdd:pfam15066 503 Q----KHEKENLEERQKL 516
|
|
| |
