|
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: 568.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365 80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE- 239
Cdd:cd01365 159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWL 318
Cdd:cd01365 239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2507456505 319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365 315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
3-365 |
8.34e-151 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 467.43 E-value: 8.34e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129 68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC 242
Cdd:smart00129 146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2507456505 323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
9-358 |
1.58e-149 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 463.58 E-value: 1.58e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225 68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 169 TFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSK 247
Cdd:pfam00225 146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225 226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294
|
330 340 350
....*....|....*....|....*....|..
gi 2507456505 327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225 295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
3-356 |
5.98e-141 |
|
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: 440.15 E-value: 5.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEALFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106 66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMP 241
Cdd:cd00106 145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291
|
330 340 350
....*....|....*....|....*....|....*
gi 2507456505 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 |
8.23e-119 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 378.73 E-value: 8.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371 148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 238 AEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTW 317
Cdd:cd01371 226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2507456505 318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371 294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
3-358 |
8.01e-115 |
|
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: 367.81 E-value: 8.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372 62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372 140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 237 DAEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvkkkqvFV 308
Cdd:cd01372 220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2507456505 309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372 291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
3-358 |
6.14e-105 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 339.71 E-value: 6.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370 76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01370 154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 236 FDAEMPCET-VSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaanplvKKKQVFVPYRDSV 314
Cdd:cd01370 231 KTASINQQVrQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2507456505 315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370 302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
4-367 |
1.54e-103 |
|
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: 336.02 E-value: 1.54e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEALFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373 64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373 144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 234 AKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaanplvkkKQVFVPYRDS 313
Cdd:cd01373 221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2507456505 314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373 293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
3-358 |
2.78e-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: 331.22 E-value: 2.78e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374 61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDAEMP 241
Cdd:cd01374 138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374 215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 2507456505 322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374 285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
1-358 |
1.84e-100 |
|
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: 326.21 E-value: 1.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYsADTkspdyvSQEMVF 79
Cdd:cd01369 1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFD-PNT------TQEDVY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369 62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369 140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 237 DAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLT 316
Cdd:cd01369 215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2507456505 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 |
2.24e-99 |
|
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: 323.39 E-value: 2.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366 9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRK 165
Cdd:cd01366 71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 166 SSKTFNLRVREHPKEGP-YVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfda 238
Cdd:cd01366 148 NAPQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 239 empceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFVPYRDSVLTWL 318
Cdd:cd01366 225 -----SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYL 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2507456505 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 |
5.01e-90 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 297.31 E-value: 5.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364 1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEALFSRINETtrwdEASFRTEVS 149
Cdd:cd01364 69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364 145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 228 TIkfTQAKFDAEMPCETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkkK 304
Cdd:cd01364 225 SI--TIHIKETTIDGEELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507456505 305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364 291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-507 |
2.48e-88 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 300.50 E-value: 2.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059 18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059 91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 176 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 255
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059 244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 406 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059 394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 2507456505 477 QT-----YVGREDASTEQDIVLHGLDLES--EHCVFEN 507
Cdd:COG5059 474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRD 511
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
446-562 |
1.56e-76 |
|
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: 248.70 E-value: 1.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2507456505 526 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
4-392 |
3.41e-76 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 279.51 E-value: 3.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188 100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188 154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188 232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 228 T-IKFTQAKFDAE-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQ 305
Cdd:PLN03188 309 TcVVESRCKSVADgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 306 VFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAE 379
Cdd:PLN03188 382 RHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDE 461
|
410
....*....|...
gi 2507456505 380 IARLKtllAQGNQ 392
Cdd:PLN03188 462 LQRVK---ANGNN 471
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
4-356 |
6.34e-74 |
|
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: 250.77 E-value: 6.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368 78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE 239
Cdd:cd01368 150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaANPLVKKKQVFVPYRDS 313
Cdd:cd01368 230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVL-------RENQLQGTNKMVPFRDS 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2507456505 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 |
2.54e-73 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 248.65 E-value: 2.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375 1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEALFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375 68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375 145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 236 FDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVL 315
Cdd:cd01375 225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2507456505 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 |
2.05e-69 |
|
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: 236.63 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376 66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC 242
Cdd:cd01376 142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaanplvKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376 219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285
|
330 340 350
....*....|....*....|....*....|....
gi 2507456505 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 |
7.62e-69 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 235.27 E-value: 7.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG----NSGDSGLIPRICEALFSRINETTRWDEasFRTEVS 149
Cdd:cd01367 63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN--LGVTVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367 141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 230 KFTQAKFDAempceTVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFV 308
Cdd:cd01367 217 ILRDRGTNK-----LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2507456505 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 |
3.49e-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: 215.98 E-value: 3.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 2507456505 526 GVQIVDATQLNQGAVILLGRTNMFRFNHP 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 |
2.22e-49 |
|
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 171.11 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 525
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2507456505 526 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLREKR 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 |
1.50e-33 |
|
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: 125.90 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTeqdIVLHGLDLESEHCVFENAGGTVTLIPL 517
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2507456505 518 rGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLR 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 |
3.24e-31 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438757 [Multi-domain] Cd Length: 101 Bit Score: 118.49 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDA 532
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 2507456505 533 TQLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705 81 TRLKTGSRVILGKNHVFRFNH 101
|
|
| FHA_KIF14 |
cd22707 |
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ... |
450-554 |
1.42e-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: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQI 529
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 2507456505 530 VDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707 84 SEPTVLHHGDRVILGGDHYFRFNHP 108
|
|
| FHA_KIF1A |
cd22726 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
454-562 |
1.75e-26 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438778 [Multi-domain] Cd Length: 115 Bit Score: 105.78 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGT-----VTLIPLRGSQCSVNGVQ 528
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 2507456505 529 IVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 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 |
3.92e-26 |
|
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: 104.35 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 528
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 2507456505 529 IVDATQLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727 83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
454-554 |
1.23e-24 |
|
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: 99.98 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDA 532
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 2507456505 533 TQLNQGAVILLGRTNMFRFNHP 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 |
2.92e-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: 101.27 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363 1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEALFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363 42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 163 rrkssktfnlrvrehpkegpyvedlskhlVQNYSDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdaempc 242
Cdd:cd01363 100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2507456505 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 |
1.98e-19 |
|
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: 85.04 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 471 YHLKEgQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFR 550
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 2507456505 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 |
5.92e-19 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 83.77 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 454 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAsteqDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 528
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFrsipnPSGEVVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 2507456505 529 IVDATQLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-1084 |
1.76e-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: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 689
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 769
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 849
Cdd:COG1196 446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 850 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 909
Cdd:COG1196 521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 910 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 988
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 989 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1068
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
490
....*....|....*.
gi 2507456505 1069 DPARLEHEIHQLKQKI 1084
Cdd:COG1196 761 DLEELERELERLEREI 776
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
3-162 |
2.02e-16 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 78.03 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796 21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEALFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 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 |
2.85e-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: 73.51 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRG-SQCSV 524
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 2507456505 525 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
456-564 |
9.20e-13 |
|
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: 66.45 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 456 LIGIDDDLLSTGIILYHLKeGQTYVGredASTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 534
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 2507456505 535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
456-554 |
2.51e-12 |
|
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: 64.93 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 456 LIGIDDDLLSTGIILYHLKEgQTYVGREDAsteQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 534
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 2507456505 535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-1067 |
1.23e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 621 ESKRKLIEE----MEEKQKSDKAE--LERMQQEVEtrrkETEIVQRQIRKQEESLKR-----RSFH-IENKLKDLLAEKE 688
Cdd:COG1196 155 EERRAIIEEaagiSKYKERKEEAErkLEATEENLE----RLEDILGELERQLEPLERqaekaERYReLKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 689 RFEEERLREQQGLEQQRRQEEESlfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeeekeQ 768
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---------------L 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 769 VQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLA 848
Cdd:COG1196 294 LAELARLEQDIARLEE--------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 849 SLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQnhlpaL 928
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEA-------------------------LRAAAELAAQLEELEEAEEALLE-----R 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 929 LEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQ 1008
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2507456505 1009 QREALEQAVAKLEQRRSALQRcstldleiqeQRQKLGSLHTSEWSGWQASLETDGEALE 1067
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLL----------AGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
611-1084 |
1.96e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSfhIENKLKDLLAEKERF 690
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 691 EEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIF-QELDRLHQEQNAQSAKLRLEKrrleeeekeqv 769
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQ----------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL------LQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 843
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALlglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 844 LVKLASLEKDLVQQKDLLSKEVQEEkvalehvkCDAGGDPSFLATDDgnILGGPPDLDKIKTAETRLQSREHQLQdllqn 923
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEEL--------LAALGLPPDLSPEE--LLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 924 hLPALLEEKQRVLDALDSGvlgldttlcqvekevgekeeQIAQYQANASQLQQLRatfEFTANVARQEEKVRRKEKEILE 1003
Cdd:COG4717 365 -LEELEQEIAALLAEAGVE--------------------DEEELRAALEQAEEYQ---ELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1004 SQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSewsgwQASLETDGEAlemdpARLEHEIHQLKQK 1083
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEE------ELEELREELAELEAE-----LEQLEEDGEL-----AELLQELEELKAE 484
|
.
gi 2507456505 1084 I 1084
Cdd:COG4717 485 L 485
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
364-476 |
2.13e-11 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 64.48 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 395 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 2507456505 463 LLSTGIILYHLKEG 476
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
608-1086 |
8.48e-11 |
|
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: 67.30 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 674
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 675 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLH---------- 744
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqqkttlt 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 745 -QEQNAQSAKLRLEKRRLEEEEKEQVQRV-----AHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 818
Cdd:TIGR00618 393 qKLQSLCKELDILQREQATIDTRTSAFRDlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 819 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 897
Cdd:TIGR00618 472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 898 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVG---- 958
Cdd:TIGR00618 544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqp 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 959 -EKEEQIAQYQANASQ-LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1034
Cdd:TIGR00618 624 eQDLQDVRLHLQQCSQeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2507456505 1035 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARLEHEI-HQLKQKICE 1086
Cdd:TIGR00618 704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELmHQARTVLKA 758
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
612-1022 |
1.52e-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: 66.62 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 612 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENkLKDLLAEK 687
Cdd:TIGR02168 674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 688 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeEEKE 767
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-----------EAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 768 QVQRVAHLEEQLRkrqdtaplLCPGEAQRAQEEKRELESIREALlqAKEMRAGGdhTCRDELERAQQYFLEFKRRQLVKL 847
Cdd:TIGR02168 822 LRERLESLERRIA--------ATERRLEDLEEQIEELSEDIESL--AAEIEELE--ELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 848 ASLEKDLvQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPA 927
Cdd:TIGR02168 890 ALLRSEL-EELSEELRELESKRSELRR------------------------ELEELREKLAQLELRLEGLEVRIDNLQER 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 928 LLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeQIAQYQANASQLQQ---------LRATFEFtanvarQEEKVRRKE 998
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIED--------------DEEEARRRLKRLENkikelgpvnLAAIEEY------EELKERYDF 1004
|
410 420
....*....|....*....|....
gi 2507456505 999 KEilesqekQQREALEQAVAKLEQ 1022
Cdd:TIGR02168 1005 LT-------AQKEDLTEAKETLEE 1021
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
624-873 |
1.62e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 66.30 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 624 RKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkdllaekerfeEERLREQQGLEQ 703
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ------------AAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 704 QRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleeeekeqvQRVAHLEEQLRK 781
Cdd:pfam17380 345 ERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN------------------ERVRQELEAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 782 RQdtaplLCPGEAQRA-QEEKRELESIREALLQAK--EMRAGGDHTCRdELERAQQYFLEfKRRQLVKLASLEKDLVQQK 858
Cdd:pfam17380 404 VK-----ILEEERQRKiQQQKVEMEQIRAEQEEARqrEVRRLEEERAR-EMERVRLEEQE-RQQQVERLRQQEEERKRKK 476
|
250
....*....|....*
gi 2507456505 859 DLLSKEVQEEKVALE 873
Cdd:pfam17380 477 LELEKEKRDRKRAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
623-1029 |
4.29e-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: 65.09 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 623 KRKLIEEM-------EEKQKSdKAELErmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEEERL 695
Cdd:TIGR02169 155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 696 REQ-QGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKEQVQ-RVA 773
Cdd:TIGR02169 229 LKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQLRVKeKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 774 HLEEQLRKRQDTAPLlCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVKLASLEKD 853
Cdd:TIGR02169 298 ELEAEIASLERSIAE-KERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 854 LVQQKDLLSKEVQEEkvalehvkcdaggDPSFLATddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhLPALLEEKQ 933
Cdd:TIGR02169 362 LKEELEDLRAELEEV-------------DKEFAET-----------RDELKDYREKLEKLKREINELKRE-LDRLQEELQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 934 RvldaldsgvlgldttlcqvekevgeKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE--SQEKQQR 1010
Cdd:TIGR02169 417 R-------------------------LSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAAdlSKYEQEL 471
|
410
....*....|....*....
gi 2507456505 1011 EALEQAVAKLEQRRSALQR 1029
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQR 490
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
455-551 |
6.78e-10 |
|
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: 57.67 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 455 HLIGIDDDllsTGIILYHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQC--SVNGVQIVDA 532
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDL-GSTNgtFVNGKRITPP 73
|
90
....*....|....*....
gi 2507456505 533 TQLNQGAVILLGRTNmFRF 551
Cdd:cd00060 74 VPLQDGDVIRLGDTT-FRF 91
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
606-876 |
8.39e-10 |
|
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: 63.99 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFER--QQREELEKLESKRKLIEEME-------EKQKSDKAELERMQQEvetRRKETEIVQRQIRKQE-ESLKRRSFH 675
Cdd:pfam17380 295 KMEQERlrQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAME---RERELERIRQEERKRElERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 676 IE-NKLKDLlaekerfeeerlreqQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 754
Cdd:pfam17380 372 MEiSRMREL---------------ERLQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 755 RLEKRRLEEEEKEQVQRVaHLEEQlrKRQDTAPLLCPGEAQRaQEEKRELESIREALLQAKEMRAggdHTCRDELERAQQ 834
Cdd:pfam17380 434 QREVRRLEEERAREMERV-RLEEQ--ERQQQVERLRQQEEER-KRKKLELEKEKRDRKRAEEQRR---KILEKELEERKQ 506
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2507456505 835 YFLEFKRRQLVklasLEKDLVQQKDLLSKEVQEEKVALEHVK 876
Cdd:pfam17380 507 AMIEEERKRKL----LEKEMEERQKAIYEEERRREAEEERRK 544
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-1088 |
2.39e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 686 EKERFEEERLREQQGLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQ---ELDRLHQEQNAQSAKLRLEKRRLE 762
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 763 EEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhTCRDELERAQQYFLEFkRR 842
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-------ELREELEEAEQALDAA-ER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 843 QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDP---SFLATDDG------NILGGppDLDKI--KTAETRLQ 911
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGyeaaieAALGG--RLQAVvvENLNAAKK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 912 SREHQLQD--------LLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEK------EEQIAQYQANAsqLQQL 977
Cdd:TIGR02168 561 AIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllgGVLVVDDLDNA--LELA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 978 RATFEFTANVARQEEKVRR-----------------KEKEILESQEKQQR-----EALEQAVAKLEQRRSALQ-RCSTLD 1034
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPggvitggsaktnssileRRREIEELEEKIEEleekiAELEKALAELRKELEELEeELEQLR 718
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2507456505 1035 LEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKICEVD 1088
Cdd:TIGR02168 719 KELEELSRQISALRKD-----LARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
555-827 |
2.45e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 555 KEAAKLREKRKSGLLSSFSLSMTDLSKSCEN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 632
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 633 KQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSFHIENKlkdllaekerfeeerlreqqglEQQRRQEEESL 712
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKAEEAKKA----------------------EEDEKKAAEAL 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 713 FRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQlrkrqdtap 787
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE--------- 1765
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2507456505 788 llcpgEAQRAQEEKRELESIREALLQAKE--MRAGGDHTCRD 827
Cdd:PTZ00121 1766 -----EEKKAEEIRKEKEAVIEEELDEEDekRRMEVDKKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
606-1084 |
3.21e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREEL--------EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQR---QIRKQEESLKRRSF 674
Cdd:TIGR02168 324 QLEELESKLDELaeelaeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 675 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQE-EESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAK 753
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 754 LRLEKrrleeeekeqvQRVAHLEEQLRKRQDtapllcPGEAQRAQEEKR-----------ELESIREALLQAKEMRAGG- 821
Cdd:TIGR02168 484 LAQLQ-----------ARLDSLERLQENLEG------FSEGVKALLKNQsglsgilgvlsELISVDEGYEAAIEAALGGr 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 822 -DHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK-------VALEHVKCDAGGDPSF-------- 885
Cdd:TIGR02168 547 lQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgVAKDLVKFDPKLRKALsyllggvl 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 886 --------------------LATDDGNIL-------GGPPDLD--------KIKTAETRLQSREHQLQDLLQNhlpalLE 930
Cdd:TIGR02168 627 vvddldnalelakklrpgyrIVTLDGDLVrpggvitGGSAKTNssilerrrEIEELEEKIEELEEKIAELEKA-----LA 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 931 EKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQR 1010
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507456505 1011 EALEQAVAKLEQrrsALQRCSTLDLEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKI 1084
Cdd:TIGR02168 782 AEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEE-----AANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-1067 |
9.63e-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: 60.84 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 703 QQRRQEEES-LFRIREELRKLQ----ELNS-----HEQAEKVQIFQELDRlhQEQNAQsaklrlekrrleeeEKEQVQRV 772
Cdd:TIGR02168 171 KERRKETERkLERTRENLDRLEdilnELERqlkslERQAEKAERYKELKA--ELRELE--------------LALLVLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 773 AHLEEQLRKRQDtapllcpgEAQRAQEEKRELES-IREALLQAKEMRAgGDHTCRDELERAQQYFLEFKRRQlvklasle 851
Cdd:TIGR02168 235 EELREELEELQE--------ELKEAEEELEELTAeLQELEEKLEELRL-EVSELEEEIEELQKELYALANEI-------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 852 KDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflatddgnilggppdldKIKTAETRLQSREHQLQDLLQNH--LPALL 929
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELES-----------------KLDELAEELAELEEKLEELKEELesLEAEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 930 EEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQyqaNASQLQQLRATFE-FTANVARQEEKVRRKEKEILESQEKQ 1008
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIAS---LNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAELKE 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507456505 1009 QREAL---EQAVAKLEQRRSAL-QRCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALE 1067
Cdd:TIGR02168 438 LQAELeelEEELEELQEELERLeEALEELREELEEAEQALDAAERelAQLQARLDSLERLQENLE 502
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
606-819 |
1.69e-08 |
|
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: 59.75 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQeveTRRKETEIVQRQIRKQEESLKRRSFHIENKlkdl 683
Cdd:pfam17380 382 RLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQREVRRLEEERAREMERVRLE---- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 684 laekerfeeeRLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQ---IFQELdrlhqEQNAQSAKLRLEKRR 760
Cdd:pfam17380 455 ----------EQERQQQVERLRQQEEE---RKRKKLELEKEKRDRKRAEEQRrkiLEKEL-----EERKQAMIEEERKRK 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2507456505 761 LEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKEMRA 819
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAE---------EERRKQQEMEERRRIQEQMRKATEERS 566
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-1023 |
1.75e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 689
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQ------ELDRLHQEQNAQSAKLRLEKRRLEE 763
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeeeeALLELLAELLEEAALLEAALAELLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 764 EEKEQVQRVAHLEEQLRKRQ------------DTAPLLCPGEAQRAQEEKRELESIREALLqakemrAGGDHTCRDELER 831
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEgflegvkaalllAGLRGLAGAVAVLIGVEAAYEAALEAALA------AALQNIVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 832 AQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKV--ALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 909
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 910 LQSREHQLQDL--------------------LQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQA 969
Cdd:COG1196 639 AVTLAGRLREVtlegeggsaggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 970 NASQLQQLRATFEFT--------------------------ANVARQEEKVRRKEKEI-------------LESQE---- 1006
Cdd:COG1196 719 EELEEEALEEQLEAEreelleelleeeelleeealeelpepPDLEELERELERLEREIealgpvnllaieeYEELEeryd 798
|
490
....*....|....*....
gi 2507456505 1007 --KQQREALEQAVAKLEQR 1023
Cdd:COG1196 799 flSEQREDLEEARETLEEA 817
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-1083 |
1.86e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQR---QIRKQEESLKRRSFhiENKLKDLL 684
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKKAE--EKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 685 AEKERFEEERLREQQGLEQQRRQEEEsLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE-QNAQSAKLRLEKRRLEE 763
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKAD 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 764 EEKEQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELERAQqyflEFKR 841
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAKKAeeAKKADEAKKAEEAKKADEAKKAE----EKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 842 RQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLL 921
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 922 QNHlpalLEEKQRVldaldsgvlgldttlcQVEKEVGEKEEQIAQYQANASQLQQLRAtfeftANVARQEEKVRRKEKEi 1001
Cdd:PTZ00121 1626 KKA----EEEKKKV----------------EQLKKKEAEEKKKAEELKKAEEENKIKA-----AEEAKKAEEDKKKAEE- 1679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1002 LESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPARLEHE----I 1077
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkI 1759
|
....*.
gi 2507456505 1078 HQLKQK 1083
Cdd:PTZ00121 1760 AHLKKE 1765
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1043 |
2.01e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEKLESKRKLIEEM----EEKQKSD----KAELERMQQEVETRRKETEIVQRQIRKQEEslKRRSFHIE 677
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAkkkaEEKKKADeakkKAEEAKKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAK 1476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 678 NKLKDLLAEKERFEEERLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLE 757
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 758 KRRLEeeekeQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKReLESIREALLQAKEMRAggdhtcrDELERAQQyfl 837
Cdd:PTZ00121 1554 AEELK-----KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKA-------EEAKKAEE--- 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 838 EFKRRQLVKLASLEKDLVQQkdlLSKEVQEEKVALEHVKCDAggdpsflatddgnilggppDLDKIKTAETRLQSREHQL 917
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAE-------------------EENKIKAAEEAKKAEEDKK 1675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 918 QdllQNHLPALLEEKQRVLDALdsgvlgldttlcQVEKEVGEKEEQIAQYQAN-ASQLQQLRATFEFTANVARQEEKVRR 996
Cdd:PTZ00121 1676 K---AEEAKKAEEDEKKAAEAL------------KKEAEEAKKAEELKKKEAEeKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2507456505 997 KEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQK 1043
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
613-1024 |
2.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 613 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEE 692
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL-------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 693 ERLREQQGLEQQRRQEEESLFRIREELRKLQE--------LNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleee 764
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleeaLNDLEARLSHSRIPEIQAELSKLEEEVS------------ 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 765 ekEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELErAQQYFLEFKRRQL 844
Cdd:TIGR02169 809 --RIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIE-NLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 845 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDlLQNH 924
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELE------------------------RKIEELEAQIEKKRKRLSE-LKAK 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 925 LPALLEEKQRVLDALDSGVlgldttlcqvekEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE 1003
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDE------------EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEyEEVLKRLDELKE 993
|
410 420
....*....|....*....|...
gi 2507456505 1004 SQEK--QQREALEQAVAKLEQRR 1024
Cdd:TIGR02169 994 KRAKleEERKAILERIEEYEKKK 1016
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
606-834 |
3.07e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.42 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetRRKEtEIVQRQIRKQEESLKRRsfhiENKLKDLLa 685
Cdd:pfam15709 347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ----RRFE-EIRLRKQRLEEERQRQE----EEERKQRL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 686 ekerfeeerlREQQGLEQQRRQEEEslFRireelRKLQELNSHEQAEkvqifqELDRLHQEQnaqsaklrlekrrleeee 765
Cdd:pfam15709 413 ----------QLQAAQERARQQQEE--FR-----RKLQELQRKKQQE------EAERAEAEK------------------ 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507456505 766 keqvQRVAHLEEQLRKRQDTapLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQ 834
Cdd:pfam15709 452 ----QRQKELEMQLAEEQKR--LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
615-1083 |
4.54e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.44 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 615 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL------LAEKE 688
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 689 RFEEERLREQQGLEQQRRQEEE--SLFRIREELRKLQELNSH------EQAEKVQIFQELDRLHQEQNAQSAK------- 753
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQAQRIHTELQSKMRSrakllmk 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 754 -LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEK---RELESIREALLQAKEMRAGGDHTCRDel 829
Cdd:TIGR00618 330 rAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhiHTLQQQKTTLTQKLQSLCKELDILQR-- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 830 ERAQQYFLEFKRRQL-VKLASLEKDLV-QQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGppDLDKIKTAE 907
Cdd:TIGR00618 408 EQATIDTRTSAFRDLqGQLAHAKKQQElQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--TKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 908 TRLQSREHQLQDLLQNhLPALLEEKQRVLDA--LDSGVLGLDTTLCQVEKEVGEKEEQ-IAQYQANASQLQQLRATFEFT 984
Cdd:TIGR00618 486 TRKKAVVLARLLELQE-EPCPLCGSCIHPNParQDIDNPGPLTRRMQRGEQTYAQLETsEEDVYHQLTSERKQRASLKEQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 985 ANVARQEEKV----RRKEKEILE--SQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLgSLHTSEWSGWQAS 1058
Cdd:TIGR00618 565 MQEIQQSFSIltqcDNRSKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELAL 643
|
490 500
....*....|....*....|....*
gi 2507456505 1059 LETDGEALEMDPARLEHEIHQLKQK 1083
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIR 668
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
451-554 |
6.65e-08 |
|
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: 52.69 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDASTEQ-DIVLHGLDLESEHCV-----------FENAGGT-- 511
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2507456505 512 --VTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712 76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
770-1084 |
7.06e-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: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA---QQYFLEFKRRQLVK 846
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 847 LASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsfLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLP 926
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAE-----------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 927 ALLEEKQRVLDALDSgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQE 1006
Cdd:TIGR02168 825 RLESLERRIAATERR---------------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1007 KQQREALEQAVAKL---EQRRSALQR--------CSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGE---ALEMDPAR 1072
Cdd:TIGR02168 890 ALLRSELEELSEELrelESKRSELRReleelrekLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenKIEDDEEE 969
|
330
....*....|..
gi 2507456505 1073 LEHEIHQLKQKI 1084
Cdd:TIGR02168 970 ARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
606-867 |
1.78e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETRRKETEIVQRQI---RKQEESLKRRSFHIENKL 680
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEIselEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 681 KDL------------------LAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDR 742
Cdd:TIGR02169 282 KDLgeeeqlrvkekigeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 743 LHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELESireallqakemrAGGD 822
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK-----RELDRLQEELQRLSE------------ELAD 424
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2507456505 823 HtcRDELERAQQYFLEFKRRQLVKLASLEKD---LVQQKDLLSKEVQE 867
Cdd:TIGR02169 425 L--NAAIAGIEAKINELEEEKEDKALEIKKQewkLEQLAADLSKYEQE 470
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-879 |
3.17e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQRE---ELEKLESKRKLIEEmEEKQKSDKAELERMQQEV-----ETRRKETEIVQRQIRKQEESLKR---RSFHI 676
Cdd:PTZ00121 1078 DFDFDAKEdnrADEATEEAFGKAEE-AKKTETGKAEEARKAEEAkkkaeDARKAEEARKAEDARKAEEARKAedaKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 677 ENKLKDllaEKERFEEERLREQQGLEQQRRQEEeslFRIREELRKLQELNSHEQA---EKVQIFQELDRLHQEQNAQsAK 753
Cdd:PTZ00121 1157 ARKAED---ARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAArkaEEERKAEEARKAEDAKKAE-AV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 754 LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELER 831
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeeKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2507456505 832 AQQyflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDA 879
Cdd:PTZ00121 1310 KAE-----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
471-551 |
4.56e-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: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 471 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 548
Cdd:COG1716 16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90
|
...
gi 2507456505 549 FRF 551
Cdd:COG1716 91 LRF 93
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
610-1084 |
4.94e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETeiVQRQIRKQEESLKRRsfhiENKLKDLLAEKER 689
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEER----ERRRARLEALLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRleeeekeQV 769
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR-------LL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLC------PGEAQ--------------------------------------------RAQE 799
Cdd:COG4913 444 ALRDALAEALGLDEAELPFVGelievrPEEERwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 800 EKRELESIREALLQAK--------------EMRAGGDHTC---RDELER--------------------------AQQYF 836
Cdd:COG4913 524 PDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdsPEELRRhpraitragqvkgngtrhekddrrriRSRYV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 837 LEFKRRQlvKLASLEKDLVQQKDLLSkEVQEEKVALEhvkcDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQ 916
Cdd:COG4913 604 LGFDNRA--KLAALEAELAELEEELA-EAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 917 LQDLLQNhlPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRR 996
Cdd:COG4913 677 LERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 997 KEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMdPARLEHE 1076
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREWPAETADLDADLESLPEYLAL-LDRLEED 827
|
....*....
gi 2507456505 1077 -IHQLKQKI 1084
Cdd:COG4913 828 gLPEYEERF 836
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
605-1083 |
6.18e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 605 LRLEFERQQREElEKLESKRKLIEEMEEKQK--------------SDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 670
Cdd:pfam02463 253 IESSKQEIEKEE-EKLAQVLKENKEEEKEKKlqeeelkllakeeeELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 671 RRSFHIENKLKDLLAEKERFEEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQifQELDRLHQEQNAQ 750
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE--ELELKSEEEKEAQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 751 SAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEA---QRAQEEKRELESIREALLQAKEMRAGGDHTCRD 827
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEElekQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 828 ELERAQQYFLEFKRRQLVK-LASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTA 906
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSgLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 907 ETR-----LQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQ-------ANASQL 974
Cdd:pfam02463 569 ALTelplgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTklkesakAKESGL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 975 QQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREalEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEwsg 1054
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA--ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL--- 723
|
490 500
....*....|....*....|....*....
gi 2507456505 1055 wQASLETDGEALEMDPARLEHEIHQLKQK 1083
Cdd:pfam02463 724 -ADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-1007 |
9.19e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELE-KLESKRK-------LIEEMEEKQKSdkaeLERmQQEVETRRKEteivqrqIRKQEESLKRRSFHIE-NKLK 681
Cdd:TIGR02168 171 KERRKETErKLERTREnldrledILNELERQLKS----LER-QAEKAERYKE-------LKAELRELELALLVLRlEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 682 DLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLhqEQNAQsaklrlekrrl 761
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQ----------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 762 eeeekEQVQRVAHLEEQLRKRQDTAPLLcpgeAQRAQEEKRELESIREALLQAKEMRAGgdhtCRDELERAQQYFLEFKR 841
Cdd:TIGR02168 306 -----ILRERLANLERQLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELES----LEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 842 R------QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdldkiktAETRLQSREH 915
Cdd:TIGR02168 373 RleeleeQLETLRSKVAQLELQIASLNNEIERLEARLER-------------------------------LEDRRERLQQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 916 QLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQ----YQANASQLQQLRATFEFTANVARQE 991
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQENL 501
|
410
....*....|....*.
gi 2507456505 992 EKVRRKEKEILESQEK 1007
Cdd:TIGR02168 502 EGFSEGVKALLKNQSG 517
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
611-1028 |
9.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQ---QEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEK 687
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALE----AELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 688 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKL-QELNSHE-QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEE 765
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELeEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 766 KEQ--------VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFL 837
Cdd:COG4717 271 LILtiagvlflVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 838 EFKRRQLVKLASLEKDLVQQkdllskEVQEEKVALEHvKCDAGGDPSFLAtddgnilggppdLDKIKTAETRLQSREHQL 917
Cdd:COG4717 347 EELQELLREAEELEEELQLE------ELEQEIAALLA-EAGVEDEEELRA------------ALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 918 QDLLQNHLPALLEEkqrvLDALDSGVLgldttlcqvekevgekEEQIAQYQANASQLQQLRAtfEFTANVARQEEKVRRK 997
Cdd:COG4717 408 EEQLEELLGELEEL----LEALDEEEL----------------EEELEELEEELEELEEELE--ELREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|.
gi 2507456505 998 EKEILESQEKQQREALEQAVAKLEQRRSALQ 1028
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
610-923 |
9.57e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKER 689
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEeekeqv 769
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEkRELESIREALLQAKEMRAGGDHTcRDELERAQQYFLEFKRRQLVKLAS 849
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLP-RELAEELLEAKDSLEAKLGLALS-ALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507456505 850 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQN 923
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
614-1147 |
2.20e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 614 REELEKLESKRKLIEEMEE------KQKSDKAELERMQQ--EVETRRKETEIVQRQIRKQEESLKRrsfhienkLKDLLA 685
Cdd:COG4913 241 HEALEDAREQIELLEPIRElaeryaAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR--------LEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 686 EKERFEEERLREQQGLEQQRRQEE-ESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEE 764
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 765 EKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAqqyfLEFKRRQ- 843
Cdd:COG4913 389 AAALLEALEEELEALEEALAEA----EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA----LGLDEAEl 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 844 -----LVKLASLEKD----------------LVQQKDLlsKEVQE--------EKVALEHVKcDAGGDPSFLATDDGNIL 894
Cdd:COG4913 461 pfvgeLIEVRPEEERwrgaiervlggfaltlLVPPEHY--AAALRwvnrlhlrGRLVYERVR-TGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 895 GgppdldKIKTAETRLQSRehqLQDLLQNHLPALLEEKQRVLDALDSGVlgldTTLCQVEKEVGEKEEQIAQYQANASQL 974
Cdd:COG4913 538 G------KLDFKPHPFRAW---LEAELGRRFDYVCVDSPEELRRHPRAI----TRAGQVKGNGTRHEKDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 975 QqlratFEFTANVARQEEKVRRKEKEILESQEkqQREALEQAVAKLEQRRSALQRCS----------TLDLEIQEQRQKL 1044
Cdd:COG4913 605 G-----FDNRAKLAALEAELAELEEELAEAEE--RLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1045 GSLHTSewSGWQASLETDGEALEMDPARLEHEIHQLKQKIcevDGVQRPHHGILEGQAVLSSL---PPSGGNSHLAPLMD 1121
Cdd:COG4913 678 ERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRleaAEDLARLELRALLE 752
|
570 580
....*....|....*....|....*..
gi 2507456505 1122 ARISAYIEEEVQRRLHD-LHRAIGDAN 1147
Cdd:COG4913 753 ERFAAALGDAVERELREnLEERIDALR 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
614-1147 |
2.24e-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: 52.76 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 614 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF---HIENKLKDLLAEKERF 690
Cdd:TIGR02169 363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 691 EEERLREQQGLEQQRRQ----------EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRR 760
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKleqlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 761 L-----EEEEKEQV--QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDH---------- 823
Cdd:TIGR02169 520 IqgvhgTVAQLGSVgeRYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDlsilsedgvi 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 824 -------TCRDELERAQQYF---------LEFKRRQL--VKLASLEKDLVQQ-------------KDLLSKEVQEEKVAL 872
Cdd:TIGR02169 600 gfavdlvEFDPKYEPAFKYVfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 873 EHVKCDAGGDPSFLATDDGNILGGPPDL-DKIKTAETRLQSREHQLQDLLQNH--LPALLEEKQRVLDALDSGVLGLDTT 949
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEekLKERLEELEEDLSSLEQEIENVKSE 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 950 LCQVEKEVGEKEEQIAQYQA---------NASQLQQLRATFEFT-ANVARQEEKVRRKEKEIleSQEKQQREALEQAVAK 1019
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEalndlearlSHSRIPEIQAELSKLeEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQE 837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1020 LEQRRSALQ-RCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKICEVDG-VQRPHH 1095
Cdd:TIGR02169 838 LQEQRIDLKeQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAqIEKKRK 917
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507456505 1096 GILEGQAVLSSL---------PPSGGNSHLAPLMDARISAYIEEEVQRRLhdlhRAIGDAN 1147
Cdd:TIGR02169 918 RLSELKAKLEALeeelseiedPKGEDEEIPEEELSLEDVQAELQRVEEEI----RALEPVN 974
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
610-1047 |
2.35e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETR---------------RKETEIVQRQIRKQEES--LKRR 672
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqqlqtkeqihlqetRKKAVVLARLLELQEEPcpLCGS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 673 SFHIENKLKDLLaekerFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 752
Cdd:TIGR00618 510 CIHPNPARQDID-----NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 753 KLRLEKRRleeeekeqVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA 832
Cdd:TIGR00618 585 DIPNLQNI--------TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 833 QQYflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQS 912
Cdd:TIGR00618 657 QER----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 913 REHQLQDLLQNHLPALLEEKQRVLDAL-------DSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRAtfefta 985
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARteahfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA------ 806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2507456505 986 nvaRQEEKVRRKEKEILESQEKQQREaLEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1047
Cdd:TIGR00618 807 ---EIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
610-1081 |
3.02e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIE--EMEEKQKSD----KAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL 683
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEakKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 684 LAEKERFEEERLREQQGLEQQRRQEEEsLFRIREELRKLQELNSHEQAEKVQIfQELDRLHQEQNAQSAKLRLEKRRLEE 763
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 764 EEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIR---EALLQAKEMRAGGDhtCRDELERAQQYFLEFK 840
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAE--------EAKKAEEAKKKAEEAKkadEAKKKAEEAKKADE--AKKKAEEAKKKADEAK 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 841 RRQLVKLASLEKDLVQQKdllsKEVQEEKVALEHVKCDAGGDPSFLATDDgnilggppDLDK---IKTAETRLQSREHQL 917
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEA----KKADEAKKAEEAKKADEAKKAEEKKKAD--------ELKKaeeLKKAEEKKKAEEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 918 QDLLQNHLPALLEEKQRVLDALDSGVLGLDTtlcQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRK 997
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYE---EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 998 EKEILESQEKQQREALEQAVAKLEQRRSAlqrcSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPA---RLE 1074
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKA----EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKA 1724
|
....*..
gi 2507456505 1075 HEIHQLK 1081
Cdd:PTZ00121 1725 EEENKIK 1731
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
606-803 |
3.81e-06 |
|
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: 51.88 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 686 EKERFEEERLREQQGLEQQRRQEEEslFRIREELRKLQELNSHEQaekvqifqeLDRLHQEQNAQSaklrlekrrleeee 765
Cdd:pfam15709 434 ELQRKKQQEEAERAEAEKQRQKELE--MQLAEEQKRLMEMAEEER---------LEYQRQKQEAEE-------------- 488
|
170 180 190
....*....|....*....|....*....|....*...
gi 2507456505 766 keqvQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRE 803
Cdd:pfam15709 489 ----KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
612-934 |
5.23e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 612 QQREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFE 691
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEE---EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 692 EERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQA-----EKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEK 766
Cdd:pfam02463 269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 767 EQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK 846
Cdd:pfam02463 349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 847 lasLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsFLATDDGNILggppDLDKIKTAETRLQSREHQLQDLLQNHLP 926
Cdd:pfam02463 429 ---LEILEEEEESIELKQGKLTEEKEELEK--------QELKLLKDEL----ELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
....*...
gi 2507456505 927 ALLEEKQR 934
Cdd:pfam02463 494 KLEERSQK 501
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
623-736 |
5.53e-06 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 49.11 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 623 KRKLIEEMEEKQKSdKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEEERLREQQGLE 702
Cdd:pfam12072 52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEK----KEKELEAQQQQLE 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 2507456505 703 QQRRQEEEslfRIREELRKLQELN--SHEQAEKVQI 736
Cdd:pfam12072 124 EKEEELEE---LIEEQRQELERISglTSEEAKEILL 156
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
608-813 |
6.30e-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: 50.30 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERM-------QQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKl 680
Cdd:pfam13868 170 EREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELraklyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELK- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 681 kdllaekerfeeerlreQQGLEQQRRQEEESLFRIREELRKLQELnshEQAEKVQIFQELDRLHQEQNAQsaklrlekrr 760
Cdd:pfam13868 249 -----------------ERRLAEEAEREEEEFERMLRKQAEDEEI---EQEEAEKRRMKRLEHRRELEKQ---------- 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2507456505 761 leeEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQ 813
Cdd:pfam13868 299 ---IEEREEQRAAEREEELEEGER--------LREEEAERRERIEEERQKKLK 340
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
676-1084 |
6.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 676 IENKLKDLLAEKERFEEERLREQQGLEQQRRQ---EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 752
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 753 KLRLEKRRLEEEEKEqvQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELE-SIREALLQAKEMRAGGDHTCRDELER 831
Cdd:COG4717 131 YQELEALEAELAELP--ERLEELEERLEELRELE-----EELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 832 AQQYFLEFKRRQLV---KLASLEKDLVQ-QKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGN------------ILG 895
Cdd:COG4717 204 LQQRLAELEEELEEaqeELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlsliltiagvlfLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 896 GPPDLDKIKTAETRLQSREHQLQDLLQNHLPALleEKQRVLDALDSgvLGLDTTLcqVEKEVGEKEEQIAQYQANASQLQ 975
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAA--LGLPPDL--SPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 976 QLRAtfeftanvARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQrqkLGSLHTSEWSGW 1055
Cdd:COG4717 358 ELEE--------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL---LGELEELLEALD 426
|
410 420
....*....|....*....|....*....
gi 2507456505 1056 QASLETDGEALEMDPARLEHEIHQLKQKI 1084
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREEL 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
632-869 |
7.13e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 632 EKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhIENKLKDLlaekerfeeerLREQQGLEQQRRQEEES 711
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAAL-----------ARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 712 LFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRqdtapllcp 791
Cdd:COG4942 85 LAELEKEIAELRA----ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ--------- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2507456505 792 geAQRAQEEKRELESIREALLQAKEMRAGGdhtcRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK 869
Cdd:COG4942 152 --AEELRADLAELAALRAELEAERAELEAL----LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
793-1047 |
7.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 793 EAQRAQEEKRELESIREALLQAKEmraggdhtCRDELERAQQYFLEFkRRQLVKLASLEkdlvQQKDLLSKEVQEEKVAL 872
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERY-AAARERLAELE----YLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 873 EHVKCDAGGDpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLcq 952
Cdd:COG4913 293 LEAELEELRA----------------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL-- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 953 vekevgekeeqiAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILEsQEKQQREALEQAVAKLEQRRSALQRcs 1031
Cdd:COG4913 355 ------------EERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLE-ALEEELEALEEALAEAEAALRDLRR-- 419
|
250
....*....|....*.
gi 2507456505 1032 tldlEIQEQRQKLGSL 1047
Cdd:COG4913 420 ----ELRELEAEIASL 431
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
611-857 |
1.19e-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: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENK 679
Cdd:pfam13868 2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 680 LKDLLAEKERFEEERLR-EQQGLEQQRRQEEESLFRIREELRK-----------LQELNSHEQAEKVQIFQELDRLHQ-- 745
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKqrqlreeidefNEEQAEWKELEKEEEREEDERILEyl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 746 -EQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLcpgEAQRAQEEKRELESIREALLQAKEMRAggdht 824
Cdd:pfam13868 162 kEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL---RAKLYQEEQERKERQKEREEAEKKARQ----- 233
|
250 260 270
....*....|....*....|....*....|...
gi 2507456505 825 cRDELERAQQYFLEFKRRQLVKLASLEKDLVQQ 857
Cdd:pfam13868 234 -RQELQQAREEQIELKERRLAEEAEREEEEFER 265
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
605-732 |
1.22e-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: 46.96 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 605 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETRRKETEivqRQIRKQEESLKRRSFHIENKLKDll 684
Cdd:pfam05672 23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE---RRREEEERQRKAEEEAEEREQRE-- 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2507456505 685 aekerfeeerlreQQGLEQQRRQEEESLFRIREEL-RKLQELNSHEQAE 732
Cdd:pfam05672 93 -------------QEEQERLQKQKEEAEAKAREEAeRQRQEREKIMQQE 128
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
610-876 |
1.31e-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: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 689
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 feeerlrEQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIfqELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 769
Cdd:pfam13868 167 -------REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL--RAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKE---MRAGGDHTCRDELERAQQYFLEFKRRQlvK 846
Cdd:pfam13868 238 QQAREEQIELKERR---------LAEEAEREEEEFERMLRKQAEDEEieqEEAEKRRMKRLEHRRELEKQIEEREEQ--R 306
|
250 260 270
....*....|....*....|....*....|
gi 2507456505 847 LASLEKDLvQQKDLLSKEVQEEKVALEHVK 876
Cdd:pfam13868 307 AAEREEEL-EEGERLREEEAERRERIEEER 335
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
613-740 |
1.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 613 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEE 692
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK----KEK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2507456505 693 ERLREQQGLEQQRRQEEEslfRIREELRKLQELN--SHEQAeKVQIFQEL 740
Cdd:PRK12704 118 ELEQKQQELEKKEEELEE---LIEEQLQELERISglTAEEA-KEILLEKV 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
611-869 |
1.37e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhienklkdllaeker 689
Cdd:COG4942 26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 feeerlreqqgLEQQRRQEEESLFRIREELRK-LQELNSHEQAEKVQIFqeldrLHQEQNAQSAKLRLEKRRLEEEEKEQ 768
Cdd:COG4942 88 -----------LEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 769 VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELERAQQYFLEfKRRQLVKLA 848
Cdd:COG4942 152 AEELRADLAELAALRAEL----EAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAE-LAAELAELQ 219
|
250 260
....*....|....*....|.
gi 2507456505 849 SLEKDLVQQKDLLSKEVQEEK 869
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
786-1047 |
1.79e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 786 APLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAQQyflefKRRQLVK-LASLEKDLVQQKDLLsKE 864
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEK-----------ELAALKK-----EEKALLKqLAALERRIAALARRI-RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 865 VQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSG- 942
Cdd:COG4942 74 LEQELAALEA------------------------ELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPe 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 943 -VLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLE 1021
Cdd:COG4942 130 dFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
250 260
....*....|....*....|....*.
gi 2507456505 1022 QRRSALQrcstldlEIQEQRQKLGSL 1047
Cdd:COG4942 210 ELAAELA-------ELQQEAEELEAL 228
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
606-937 |
1.87e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEE---SLKRRSFH 675
Cdd:pfam07888 68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdikTLTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 676 IENKLKDLlaekerfeeerLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEkvqiFQELDRLHQEQNAQSAKLR 755
Cdd:pfam07888 148 RETELERM-----------KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 756 LEKRRLEEEEKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELES-----------IREALLQAKEMR--- 818
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSSmaaqrdrtqaeLHQARLQAAQLTlql 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 819 AGGDHTCRDELERAQQyflefKRRQLVKLASLEKDLVQQ--KDLLSKE--VQEEKVALEHVKCDaggdpsflatddgniL 894
Cdd:pfam07888 289 ADASLALREGRARWAQ-----ERETLQQSAEADKDRIEKlsAELQRLEerLQEERMEREKLEVE---------------L 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2507456505 895 GGPPDLDKIKTAETRLQSREHQL-QDLLQNHLPALLEEKQRVLD 937
Cdd:pfam07888 349 GREKDCNRVQLSESRRELQELKAsLRVAQKEKEQLQAEKQELLE 392
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
608-731 |
2.41e-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: 49.35 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetrRKETEIVQRQIRKQE-ESLKRRSFHIENKLKDLLAE 686
Cdd:pfam17380 447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKE 521
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2507456505 687 KERFEEERLREQQG--LEQQRR--QEEESLFRIREELRKLQELNSHEQA 731
Cdd:pfam17380 522 MEERQKAIYEEERRreAEEERRkqQEMEERRRIQEQMRKATEERSRLEA 570
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
606-1047 |
3.03e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEKLesKRKLIEEMEEKQKsdkaELERMQQEVETRR-----KETEIVQRQIRKQEESLKRRSFHIENK- 679
Cdd:pfam01576 195 RLKKEEKGRQELEKA--KRKLEGESTDLQE----QIAELQAQIAELRaqlakKEEELQAALARLEEETAQKNNALKKIRe 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 680 LKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQ--EQNAQSaklrle 757
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKalEEETRS------ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 758 krrleeeEKEQVQrvahleeQLRKRQDTApllcpgeaqraqeekreLESIREALLQAKEMRAGgdhtcrdeLERAQQYfL 837
Cdd:pfam01576 343 -------HEAQLQ-------EMRQKHTQA-----------------LEELTEQLEQAKRNKAN--------LEKAKQA-L 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 838 EFKRRQLVK----LASLEKDLVQQKDLLSKEVQEEKVAL---EHVKCDAGGDPSFLATDDGNILGGPPDLDK--IKTAEt 908
Cdd:pfam01576 383 ESENAELQAelrtLQQAKQDSEHKRKKLEGQLQELQARLsesERQRAELAEKLSKLQSELESVSSLLNEAEGknIKLSK- 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 909 RLQSREHQLQD---LLQNHLPALLEEKQRvLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATFEFTA 985
Cdd:pfam01576 462 DVSSLESQLQDtqeLLQEETRQKLNLSTR-LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA---QLSDMKKKLEEDA 537
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507456505 986 NVARQEEKVRRKEKEILESQeKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSL 1047
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEAL-TQQLEEKAAAYDKLEKTKNRLQQeLDDLLVDLDHQRQLVSNL 599
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
614-874 |
5.33e-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: 48.43 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 614 REELEKLESKRKLIEEMEEK-QKSDKAELERMQQEVETRRKETEIVQRQIRKQEES------LKRRSFHIENKLKDLlae 686
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELeeeyllYLDYLKLNEERIDLL--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 687 kerfeeerlreqQGLEQQRRQEEESLFRIRE-ELRKL-QELNSHEQAEKVQIFQELDRLHQEqnAQSAKLRLEKRRLEEE 764
Cdd:pfam02463 243 ------------QELLRDEQEEIESSKQEIEkEEEKLaQVLKENKEEEKEKKLQEEELKLLA--KEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 765 EKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGgdhtcRDELERAQQYFLEFKRRQL 844
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-----QEKLEQLEEELLAKKKLES 383
|
250 260 270
....*....|....*....|....*....|
gi 2507456505 845 VKLASLEKDLVQQKDLLSKEVQEEKVALEH 874
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
614-873 |
6.72e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 614 REELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEN--KLKDLLAEKE 688
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 689 RFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELnsheQAEKVQIFQELDRL---HQEQNAQSAKLRLEKRRLEEEE 765
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL----KKKLKELEKRLEELeerHELYEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 766 KEQVQRVAHLEEQLRKRQDTAPLlcpgEAQRAQEEKRELESIREALLQAKEMRAGGDH---TCRDELEraQQYFLEFKRR 842
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEE----EISKITARIGELKKEIKELKKAIEELKKAKGkcpVCGRELT--EEHRKELLEE 456
|
250 260 270
....*....|....*....|....*....|.
gi 2507456505 843 QLVKLASLEKDLVQQKDLLSKeVQEEKVALE 873
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERK-LRKELRELE 486
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
473-551 |
1.04e-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: 42.97 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 473 LKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLrgSQCS---VNGVQIVDATQLNQGAVILLGrTNM 548
Cdd:cd22673 18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENL--STTNptlVNGKAIEKSAELKDGDVITIG-GRS 91
|
...
gi 2507456505 549 FRF 551
Cdd:cd22673 92 FRF 94
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
605-671 |
1.07e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507456505 605 LRLEFERQQREELEKlESKRKLIE-EMEEKQKSDKAELERMQQEvETRRKETEI-----VQRQIRKQEESLKR 671
Cdd:pfam17380 497 LEKELEERKQAMIEE-ERKRKLLEkEMEERQKAIYEEERRREAE-EERRKQQEMeerrrIQEQMRKATEERSR 567
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
612-869 |
1.50e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 612 QQREELEKLESKRK-LIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLlaekerf 690
Cdd:COG4372 10 KARLSLFGLRPKTGiLIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 691 eeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlEKRRLEEEEKEQVQ 770
Cdd:COG4372 83 --------EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA----QIAELQSEIAEREE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 771 RVAHLEEQLRKRQDTAPLLcpGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASL 850
Cdd:COG4372 151 ELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
250
....*....|....*....
gi 2507456505 851 EKDLVQQKDLLSKEVQEEK 869
Cdd:COG4372 229 AKLGLALSALLDALELEED 247
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
610-844 |
1.77e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREEleklESKRKLIEEMEEKQK---------SDKAELERMQQEVETR---RKETEIVQRQIRKQEESLKRRSFHI- 676
Cdd:pfam02029 66 DRTAKRE----ERRQKRLQEALERQKefdptiadeKESVAERKENNEEEENsswEKEEKRDSRLGRYKEEETEIREKEYq 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 677 ENKLKDllaekerfeEERLREQQGLEQQRRQEEESLFR----IREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 752
Cdd:pfam02029 142 ENKWST---------EVRQAEEEGEEEEDKSEEAEEVPtenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 753 KLRLEKRRLEEEEKEQVQRVAH---------------LEEQLRKRQDTAPLLCPGEAQRAQEEKRELESI------REAL 811
Cdd:pfam02029 213 EEEVTKLKVTTKRRQGGLSQSQereeeaevfleaeqkLEELRRRRQEKESEEFEKLRQKQQEAELELEELkkkreeRRKL 292
|
250 260 270
....*....|....*....|....*....|...
gi 2507456505 812 LQAKEMRaggdhtcRDELERAQQYFLEFKRRQL 844
Cdd:pfam02029 293 LEEEEQR-------RKQEEAERKLREEEEKRRM 318
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
701-1044 |
2.03e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 701 LEQQR-RQEEESLFRIREELRKLQELNSHEQAE---KVQIFQELDRLHQEQNaqsaklrlekrrleeeekEQVQRVaHLE 776
Cdd:pfam17380 296 MEQERlRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERE------------------RELERI-RQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 777 EqlRKRQDtapllcpgEAQRAQEEKRELESIREalLQAKEM-RAGGDHTCRDELERAQQYFLEFKRRQlvklaslekdlv 855
Cdd:pfam17380 357 E--RKREL--------ERIRQEEIAMEISRMRE--LERLQMeRQQKNERVRQELEAARKVKILEEERQ------------ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 856 qqkdllsKEVQEEKVALEHVKCDaggdpsflatddgnilggppdldkiktaetRLQSREHQLQdllqnhlpALLEEKQRV 935
Cdd:pfam17380 413 -------RKIQQQKVEMEQIRAE------------------------------QEEARQREVR--------RLEEERARE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 936 LDALDSgvlgldttlcqvekevgekeeqiaQYQANASQLQQLRatfeftanvarQEEKVRRKEKEILESQEKQQREAleq 1015
Cdd:pfam17380 448 MERVRL------------------------EEQERQQQVERLR-----------QQEEERKRKKLELEKEKRDRKRA--- 489
|
330 340
....*....|....*....|....*....
gi 2507456505 1016 avakLEQRRSALQRcstldlEIQEQRQKL 1044
Cdd:pfam17380 490 ----EEQRRKILEK------ELEERKQAM 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
611-1087 |
2.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRkliEEMEEKQKSDKAELERMQQEVetrrKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERF 690
Cdd:PRK03918 175 KRRIERLEKFIKRT---ENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 691 EEERLREQQGLEQQRRQEEESLFRIREELRKLQEL--NSHEQAEKVQIFQELDRLHQEQNAQSAKLRlekrrleeeekeq 768
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEEYLDELREIE------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 769 vQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREAL--LQAKEMRAGGDHtcrDELERAQQyflefKRRQLVK 846
Cdd:PRK03918 314 -KRLSRLEEEINGIEE--------RIKELEEKEERLEELKKKLkeLEKRLEELEERH---ELYEEAKA-----KKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 847 LASLEKDLVQQKdlLSKEVQEEKVALEHVKcdaggdpsflatddgnilggpPDLDKIKTAETRLQSREHQLQDLLQNhlp 926
Cdd:PRK03918 377 LKKRLTGLTPEK--LEKELEELEKAKEEIE---------------------EEISKITARIGELKKEIKELKKAIEE--- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 927 alLEEKQRVldaldsgvlgldTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEftanvaRQEEKVRRKEKEiLESQE 1006
Cdd:PRK03918 431 --LKKAKGK------------CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE------EKERKLRKELRE-LEKVL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1007 KQQREALEQAvAKLEQRRSALQRCSTLDLEIQEQ--------RQKLGSLhtsewSGWQASLETD---GEALEMDPARLEH 1075
Cdd:PRK03918 490 KKESELIKLK-ELAEQLKELEEKLKKYNLEELEKkaeeyeklKEKLIKL-----KGEIKSLKKElekLEELKKKLAELEK 563
|
490
....*....|..
gi 2507456505 1076 EIHQLKQKICEV 1087
Cdd:PRK03918 564 KLDELEEELAEL 575
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
471-555 |
2.44e-04 |
|
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.
Pssm-ID: 465238 [Multi-domain] Cd Length: 94 Bit Score: 41.86 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 471 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDAT-QLNQGAVILLGRTnM 548
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGiALRPGDRIELGQT-E 87
|
....*..
gi 2507456505 549 FRFNHPK 555
Cdd:pfam16697 88 FCLVPAD 94
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
607-874 |
3.38e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 607 LEFERQQREEL-EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrrsfhiENKLKDLLA 685
Cdd:COG4372 68 LEQARSELEQLeEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ--------RKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 686 EKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKV--QIFQELDRLHQEQNAQSAKLRLEKRRLEE 763
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELlkEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 764 EEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 843
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
250 260 270
....*....|....*....|....*....|.
gi 2507456505 844 LVKLASLEKDLVQQKDLLSKEVQEEKVALEH 874
Cdd:COG4372 300 LLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
648-1047 |
3.62e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 648 VETRRKETEIVQRQIRKQEESLKRRSFH-----IENKLKDLLAEKERFEEERLREQQGLEQ---------QRRQEEESL- 712
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHerlngLESELAELDEEIERYEEQREQARETRDEadevleeheERREELETLe 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 713 -------------FRIREELRK-----------LQELNSHEQAEkvqifQELDRLHQE--QNAQSAKLRLEKRRLEEEEK 766
Cdd:PRK02224 258 aeiedlretiaetEREREELAEevrdlrerleeLEEERDDLLAE-----AGLDDADAEavEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 767 EQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFlEFKRRQLVK 846
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDL--EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF-GDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 847 LASLEKDLVQQKDLLSKEVQEEKVALEHV--------------KCDAGGDPsflatddgniLGGPPDLDKIKTAETRLQS 912
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTArerveeaealleagKCPECGQP----------VEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 913 REHQLQDLLQNHlpALLEEKqrvLDALDSGVlgldttlcqvekevgEKEEQIAQYQANASQLQQLRATFEFTANVARQEE 992
Cdd:PRK02224 480 LEAELEDLEEEV--EEVEER---LERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2507456505 993 KVRRKEKEILESQEKQQREA-----------------LEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1047
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAaaeaeeeaeeareevaeLNSKLAELKERIESLERIRTLLAAIADAEDEIERL 611
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
608-1086 |
3.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQREELEKLESKRKLIEEMEEKQKSD---KAELERMQQEV---ETRRKETEIVQR--------QIRKQEESLKRRS 673
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADEAkkaEEKKKADEAKKKaeeakkadEAKKKAEEAKKKA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 674 FHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE--QNAQS 751
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--KKAEEKKKADEAKKKAEEdkKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 752 AKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIR---EALLQAKEMRAGgdhtcrDE 828
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---------EAKKADEAKKKAEEAKkaeEAKKKAEEAKKA------DE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 829 LERAQQyflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDpsflaTDDGNILGGPPDLDKIKTAET 908
Cdd:PTZ00121 1475 AKKKAE-----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 909 RLQSREHQLQDLLQNhlpalLEEKQRVLDALDSgvlgldttlcQVEKEVGEKEEQIAQyQANASQLQQLRATFE----FT 984
Cdd:PTZ00121 1545 KKKADELKKAEELKK-----AEEKKKAEEAKKA----------EEDKNMALRKAEEAK-KAEEARIEEVMKLYEeekkMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 985 ANVARQEEKVRRKEKEILESQE-----KQQREALEQAVAKLEQRRSALQ----RCSTLDLEIQEQRQKLGSLHTSEWSGW 1055
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEekkkvEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
490 500 510
....*....|....*....|....*....|.
gi 2507456505 1056 QASLETDGEALEmdparlEHEIHQLKQKICE 1086
Cdd:PTZ00121 1689 KAAEALKKEAEE------AKKAEELKKKEAE 1713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
605-816 |
3.71e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 605 LRLEFeRQQREELEKLESKR-----------KLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS 673
Cdd:TIGR02168 815 LNEEA-ANLRERLESLERRIaaterrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 674 FHIENKLKDLlaekerfeeerlreqQGLEQQRRQEEESLFRIREELRKLQElnsHEQAEKVQIFQELDRLHQEQNAQSAK 753
Cdd:TIGR02168 894 SELEELSEEL---------------RELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEYSLTLEE 955
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2507456505 754 LRLEKRRLEEEEKEQVQRVAHLEEQLrKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKE 816
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI-KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
605-679 |
4.44e-04 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 42.73 E-value: 4.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507456505 605 LRLEFERQQREELEKLESKRKliEEMEEKQKsdKAELERmQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK 679
Cdd:pfam15346 71 RKEEEERKKREELERILEENN--RKIEEAQR--KEAEER-LAMLEEQRRMKEERQRREKEEEEREKREQQKILNK 140
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
899-1084 |
4.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 899 DLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSGVlgldtTLCQVEKEVGEKEEQIAQYQANASQLQQL 977
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAAL-----RLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 978 RATFEftANVARQEEKVRRKEKEILES------QEKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSLHT- 1049
Cdd:COG4913 311 LERLE--ARLDALREELDELEAQIRGNggdrleQLEREIERLERELEERERRRARLEAlLAALGLPLPASAEEFAALRAe 388
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2507456505 1050 -----SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKI 1084
Cdd:COG4913 389 aaallEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
608-1023 |
4.96e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 608 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRR-----------KETEIVQRQIRKQEESLKRRSFHI 676
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRageakqlaeaqKEAELLRKQLSKTQEELEAQVTLV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 677 ENklkdlLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQ--------------ELNSHEQAEKVQIFQELDR 742
Cdd:pfam07111 221 ES-----LRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqsltHMLALQEEELTRKIQPSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 743 LHQE--QNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLlcpgeaQRAQEEKRELESIREALLQAK----E 816
Cdd:pfam07111 296 LEPEfpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL------QEQVTSQSQEQAILQRALQDKaaevE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 817 MRAGGDHTCRDELERAQqyflEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSF-----LATDDG 891
Cdd:pfam07111 370 VERMSAKGLQMELSRAQ----EARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLsnrlsYAVRKV 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 892 NILGGPPdLDKIKTAETRLQS-----REHQLQDLLQNHLPALLEEKQRvLDAldsgVLGLDTTLCQVEKEVGEKEEQIAQ 966
Cdd:pfam07111 446 HTIKGLM-ARKVALAQLRQEScppppPAPPVDADLSLELEQLREERNR-LDA----ELQLSAHLIQQEVGRAREQGEAER 519
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 967 YQAN--ASQL-QQLRATFEFTANVARQEEKVRRKEKEILES-----QE-KQQRE----ALEQAVAKLEQR 1023
Cdd:pfam07111 520 QQLSevAQQLeQELQRAQESLASVGQQLEVARQGQQESTEEaaslrQElTQQQEiygqALQEKVAEVETR 589
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
607-1017 |
8.30e-04 |
|
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: 44.40 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 607 LEFERQQREELEKLesKRKLIEEMEekqkSDKAELE------RMQQEVETRRkETEIVQRQIRKQEES---------LKR 671
Cdd:pfam01576 280 LESERAARNKAEKQ--RRDLGEELE----ALKTELEdtldttAAQQELRSKR-EQEVTELKKALEEETrsheaqlqeMRQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 672 RSFHIENKLKDLLAEKERFEEERLREQQGLE-------------QQRRQEEESlfRIREELRKLQELNS-HEQAEKVQif 737
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAKQALEsenaelqaelrtlQQAKQDSEH--KRKKLEGQLQELQArLSESERQR-- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 738 QEL-DRLHQEQNAQSAKLRLEKRRLEEEEKEQvQRVAHLEEQLrkrQDTAPLLcpgeaqraQEEKRE----------LES 806
Cdd:pfam01576 429 AELaEKLSKLQSELESVSSLLNEAEGKNIKLS-KDVSSLESQL---QDTQELL--------QEETRQklnlstrlrqLED 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 807 IREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHvKCDAggdpsfl 886
Cdd:pfam01576 497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEE-KAAA------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 887 atddgnilggppdLDKIKTAETRLQsreHQLQDLL-----QNHLPALLEEKQRVLDALdsgvlgldttlcqvekevgeke 961
Cdd:pfam01576 568 -------------YDKLEKTKNRLQ---QELDDLLvdldhQRQLVSNLEKKQKKFDQM---------------------- 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2507456505 962 eqIAQYQANASQLQQLRATFEFTA--------NVARQEEKVRRKEKEiLESQEKQQREALEQAV 1017
Cdd:pfam01576 610 --LAEEKAISARYAEERDRAEAEAreketralSLARALEEALEAKEE-LERTNKQLRAEMEDLV 670
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
606-861 |
8.43e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEK----LESKRKLIEEMEE---KQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS-FHIE 677
Cdd:PRK04863 895 RVEEIREQLDEAEEakrfVQQHGNALAQLEPivsVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhFSYE 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 678 NKLKDLlaekerfeEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNaqsaklrle 757
Cdd:PRK04863 975 DAAEML--------AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA----QLAQYNQVLASLKSSYDAKR--------- 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 758 krrleeeekeqvQRVAHLEEQLrkrQDTAPLLCPGEAQRAQEEKRELesirEALLQAKEMRaggdhtcRDELERaQQYFL 837
Cdd:PRK04863 1034 ------------QMLQELKQEL---QDLGVPADSGAEERARARRDEL----HARLSANRSR-------RNQLEK-QLTFC 1086
|
250 260
....*....|....*....|....*
gi 2507456505 838 EFKRRQLVK-LASLEKDLVQQKDLL 861
Cdd:PRK04863 1087 EAEMDNLTKkLRKLERDYHEMREQV 1111
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
606-1172 |
9.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQrEELEKLESKRKLIE-----EMEEKQKSDKAELERMQQEV----ETRRKETEIVQRQIRKQEESLKRRSfhi 676
Cdd:PTZ00121 1165 KAEEARKA-EDAKKAEAARKAEEvrkaeELRKAEDARKAEAARKAEEErkaeEARKAEDAKKAEAVKKAEEAKKDAE--- 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 677 enklkdllaEKERFEEERLREQQGLEQQRRQEEESLFRIR---EELRKLQELnshEQAEKVQIFQELDRLHQEQNAQSAK 753
Cdd:PTZ00121 1241 ---------EAKKAEEERNNEEIRKFEEARMAHFARRQAAikaEEARKADEL---KKAEEKKKADEAKKAEEKKKADEAK 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 754 LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRelesiREALLQAKEMRAGGDHTCRDELERAQ 833
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAE--------EAKKAAEAAK-----AEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 834 qyflEFKRRQLVKLASLEKdlvQQKDLLSKEVQEEKVALEHVKCDAGgdpsflATDDGNILGGPPDlDKIKTAETRLQSR 913
Cdd:PTZ00121 1376 ----AKKKADAAKKKAEEK---KKADEAKKKAEEDKKKADELKKAAA------AKKKADEAKKKAE-EKKKADEAKKKAE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 914 EHQLQDLLQNHlpalLEEKQRVLDALDSGvlgldttlcqVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEK 993
Cdd:PTZ00121 1442 EAKKADEAKKK----AEEAKKAEEAKKKA----------EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 994 VRRKEKEILESQEKQQREALEQAvaklEQRRSALQrcstldLEIQEQRQKLGSLHTSEwsgwqaSLETDGEALEMDPARL 1073
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKA----EEAKKADE------AKKAEEKKKADELKKAE------ELKKAEEKKKAEEAKK 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1074 EHEIHQLKQKICEVdgVQRPHHGILEGQAVLSSLPPSGGNSHLAPLMDARISA---YIEEEVQRRLHDLHRAIGDANHTP 1150
Cdd:PTZ00121 1572 AEEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
570 580
....*....|....*....|..
gi 2507456505 1151 ADVMKSNEELHNGTTQRKLKYE 1172
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAE 1671
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
611-710 |
9.33e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.98 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQevetrRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerf 690
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFE-----REREEIRESYEEKLRTELERQAEAHEEHLKDVLV----- 386
|
90 100
....*....|....*....|
gi 2507456505 691 eeerlreQQGLEQQRRQEEE 710
Cdd:pfam09731 387 -------EQEIELQREFLQD 399
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
478-543 |
9.52e-04 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 39.10 E-value: 9.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507456505 478 TYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQ-CSVNGVQI-VDATQLNQGAVILL 543
Cdd:pfam00498 1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNgTFVNGQRLgPEPVRLKDGDVIRL 66
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
706-1027 |
1.49e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 706 RQEEESLFRiREELRKLQElnSHEQAEKVqiFQELDRLHQEQNAQSAKlrlekrrleeeekeqvqrvahLEEQLrkrQDT 785
Cdd:pfam01576 2 RQEEEMQAK-EEELQKVKE--RQQKAESE--LKELEKKHQQLCEEKNA---------------------LQEQL---QAE 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 786 APLLCPGEAQRAQ--EEKRELESIrealLQAKEMRAGgdhtcrDELERAQQYFLEFKRRQlVKLASLEKDLVQQKDLLSK 863
Cdd:pfam01576 53 TELCAEAEEMRARlaARKQELEEI----LHELESRLE------EEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 864 eVQEEKVALEhVKCDAGGDPSFLATDDGNILGGPPDL--DKIKTAETRLQSREHQLQDL--LQNHLPALLEEKQRVLDAL 939
Cdd:pfam01576 122 -LQLEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLleERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 940 DSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATF-----EFTANVARQEE----------KVRRKEKEILES 1004
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQA---QIAELRAQLakkeeELQAALARLEEetaqknnalkKIRELEAQISEL 276
|
330 340
....*....|....*....|...
gi 2507456505 1005 QEKQQREalEQAVAKLEQRRSAL 1027
Cdd:pfam01576 277 QEDLESE--RAARNKAEKQRRDL 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
612-685 |
1.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2507456505 612 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 685
Cdd:PRK12704 68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
610-798 |
1.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK---------- 679
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 680 -----LKDLLAEKERFEEERLREQQGLEQQRRQeeeslfriREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 754
Cdd:COG3883 109 lgsesFSDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2507456505 755 RLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQ 798
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
452-554 |
1.83e-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: 39.78 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFE-------NAGGTVTLIPLRGSQCSV 524
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvrlpkhRSEEKLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 2507456505 525 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
610-950 |
1.84e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETRRKETEIVQRQIRKQEeslkrrsfhienKLKDLLAEKER 689
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 690 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKeqv 769
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKA---EEAKRKAEEEAKRKAEEERKAAEAEAAAK--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 849
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 850 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLPALL 929
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340
....*....|....*....|.
gi 2507456505 930 EEKQRVLDALDSGVLGLDTTL 950
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGG 332
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
704-1086 |
1.90e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 704 QRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRL-----HQEQNAQSAklrlekrrleeeekeqvqrvahlEEQ 778
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsaresDLEQDYQAA-----------------------SDH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 779 LRKRQdtapllcpgEAQRAQEE----KRELESIREALLQAKEMRAGGDH---TCRDELERAQQYFLEFKrrqlVKLASLE 851
Cdd:COG3096 336 LNLVQ---------TALRQQEKieryQEDLEELTERLEEQEEVVEEAAEqlaEAEARLEAAEEEVDSLK----SQLADYQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 852 KDL-VQQKDLLskEVQEEKVALEHVKcdaggdpsflatddgnILGGPPDLDkIKTAETRLQSREHQLQDLLQnhlpALLE 930
Cdd:COG3096 403 QALdVQQTRAI--QYQQAVQALEKAR----------------ALCGLPDLT-PENAEDYLAAFRAKEQQATE----EVLE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 931 EKQRVLDA------------LDSGVLGlDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATF-EFTANVARQEEKVR-- 995
Cdd:COG3096 460 LEQKLSVAdaarrqfekayeLVCKIAG-EVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERll 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 996 -------------RKEKEILESQEKQQREALEQAVAKLEQRRSALQRcsTLDlEIQEQRQKLGSLhTSEWSGWQASLET- 1061
Cdd:COG3096 539 eefcqrigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ--QLE-QLRARIKELAAR-APAWLAAQDALERl 614
|
410 420 430
....*....|....*....|....*....|....*..
gi 2507456505 1062 ---DGEALEMDPA---------RLEHEIHQLKQKICE 1086
Cdd:COG3096 615 reqSGEALADSQEvtaamqqllEREREATVERDELAA 651
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
599-873 |
2.03e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 599 IKGPICLRLEFERQQREELEKLESKRKLIeEMEEKQKSdkAELERMQQEVETRRKETEIVQRQIRKQEESLKrrsfhiEN 678
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKII-TMELQKKS--SELEEMTKFKNNKEVELEELKKILAEDEKLLD------EK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 679 KLKDLLAEKERFEEERLReqqGLEQQRRQEEESL------FRIREE--LRKLQELNSHEQAEK---VQIFQELDRLHQEq 747
Cdd:pfam05483 425 KQFEKIAEELKGKEQELI---FLLQAREKEIHDLeiqltaIKTSEEhyLKEVEDLKTELEKEKlknIELTAHCDKLLLE- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 748 NAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpgeAQRAQEEKRELESIREALLQAK-EMRAGGDHTcr 826
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL-------EEKEMNLRDELESVREEFIQKGdEVKCKLDKS-- 571
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2507456505 827 DELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSK---EVQEEKVALE 873
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALK 621
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
968-1051 |
2.16e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 968 QANASQLQQLRAtfEFTANVARQEEKvRRKEKEILESQEKQQrealeqavAKLEQRRSALQRC-STLDLEIQEQRQKLGS 1046
Cdd:PRK11637 169 QETIAELKQTRE--ELAAQKAELEEK-QSQQKTLLYEQQAQQ--------QKLEQARNERKKTlTGLESSLQKDQQQLSE 237
|
....*
gi 2507456505 1047 LHTSE 1051
Cdd:PRK11637 238 LRANE 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
615-1092 |
2.53e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 615 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrqirKQEESLKRRSFHIENKLKDLLAEKERFEEER 694
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 695 LREQQGLEQQRRQEEESLFR-IREELrkLQELNSHEQAEKVQIFQELD----RLHQEQnaqsaklrlekrrleeeekEQV 769
Cdd:pfam12128 534 GTLLHFLRKEAPDWEQSIGKvISPEL--LHRTDLDPEVWDGSVGGELNlygvKLDLKR-------------------IDV 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 770 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL--LQAKEMRAGgdHTCRDELERAQQYFLEFKRRQLvkl 847
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELekASREETFAR--TALKNARLDLRRLFDEKQSEKD--- 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 848 aSLEKDLVQQKDLLSKEVQE---EKVALEHvkcdagGDPSFLatddgnilggppdldkiktAETRLQSREHQLQdlLQNH 924
Cdd:pfam12128 668 -KKNKALAERKDSANERLNSleaQLKQLDK------KHQAWL-------------------EEQKEQKREARTE--KQAY 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 925 LPALLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeqiaQYQANASQLQQLRATfeFTANVARQEEKVRRKEKEILES 1004
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRS-----------------GAKAELKALETWYKR--DLASLGVDPDVIAKLKREIRTL 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 1005 QEKQQR-EALEQAVAKLEQ--------RRSALQ-RCSTLDLEIQEQRQKLGSLhtsewsgwQASLETDGEALEMDPARLE 1074
Cdd:pfam12128 781 ERKIERiAVRRQEVLRYFDwyqetwlqRRPRLAtQLSNIERAISELQQQLARL--------IADTKLRRAKLEMERKASE 852
|
490
....*....|....*...
gi 2507456505 1075 HEIHQLKQKICEVDGVQR 1092
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMS 870
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
610-670 |
2.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2507456505 610 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 670
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
605-1009 |
2.79e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 605 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQ--EVETRR-----KETEIVQRQIR---KQEESLKRRSF 674
Cdd:pfam10174 350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDmlDVKERKinvlqKKIENLQEQLRdkdKQLAGLKERVK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 675 HIEN----------KLKDLLAEKERFEEERLREQQGLEQQRRQEEESLfriREELRKLQELNSHEQAEKVQIFQELDRL- 743
Cdd:pfam10174 426 SLQTdssntdtaltTLEEALSEKERIIERLKEQREREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDLk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 744 -HQEQNAQSAKLRLEKRRLEEEEKEQ-VQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQAKEMRAGg 821
Cdd:pfam10174 503 eHASSLASSGLKKDSKLKSLEIAVEQkKEECSKLENQLKKAHNAE------EAVRTNPEINDRIRLLEQEVARYKEESG- 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 822 dhTCRDELERaqqyflefkrrqlvkLASLEKDLVQQKDLLSKEVQE-EKVALEHVKCdaggdpsfLATDDGNILGGPPDL 900
Cdd:pfam10174 576 --KAQAEVER---------------LLGILREVENEKNDKDKKIAElESLTLRQMKE--------QNKKVANIKHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 901 DKIKTAETRLQSREHqlQDLLQNHLPALLEEkqrVLDALDSGVLGLDTTlcqvekevgekeeqiaqyQANASQLQQLRAT 980
Cdd:pfam10174 631 KKKGAQLLEEARRRE--DNLADNSQQLQLEE---LMGALEKTRQELDAT------------------KARLSSTQQSLAE 687
|
410 420 430
....*....|....*....|....*....|
gi 2507456505 981 FEFTANVARQEekvRRKE-KEILESqeKQQ 1009
Cdd:pfam10174 688 KDGHLTNLRAE---RRKQlEEILEM--KQE 712
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
605-739 |
2.93e-03 |
|
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: 40.44 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 605 LRLEFERQQREELEKLESKRkliEEMEEKQKSDKAELERMQQEVETRRKEteivqRQIRKQEESLKRRSFHIENKLKDLL 684
Cdd:pfam11600 16 QRLEKDKERLRRQLKLEAEK---EEKERLKEEAKAEKERAKEEARRKKEE-----EKELKEKERREKKEKDEKEKAEKLR 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2507456505 685 AEKERFEEERLREQQGLEQQRRQEEESlfRIREELRKLQElnshEQAEKVQIFQE 739
Cdd:pfam11600 88 LKEEKRKEKQEALEAKLEEKRKKEEEK--RLKEEEKRIKA----EKAEITRFLQK 136
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
702-1029 |
3.00e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 702 EQQRRQEEEslFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRV--------- 772
Cdd:pfam15558 35 EELRRRDQK--RQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQenqrqekle 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 773 -AHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREA---LLQAKEMRAggdhtCRDELERAQQyflEFKRRQLVKLA 848
Cdd:pfam15558 113 rARQEAEQRKQC---------QEQRLKEKEEELQALREQnslQLQERLEEA-----CHKRQLKERE---EQKKVQENNLS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 849 SLEKDLVQQKDLLSKEVQEE---KVALEHvkcdaggdpSFLATDDgnilgGPPDLDKIKTAETRLQSREHQLQdLLQNHL 925
Cdd:pfam15558 176 ELLNHQARKVLVDCQAKAEEllrRLSLEQ---------SLQRSQE-----NYEQLVEERHRELREKAQKEEEQ-FQRAKW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 926 PALLEEKQRV--LDALdsgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARqeEKVRRKEKEILE 1003
Cdd:pfam15558 241 RAEEKEEERQehKEAL-----------------AELADRKIQQARQVAHKTVQDKAQRARELNLER--EKNHHILKLKVE 301
|
330 340
....*....|....*....|....*.
gi 2507456505 1004 SQEKQQREALEQAVAKLEQRRSALQR 1029
Cdd:pfam15558 302 KEEKCHREGIKEAIKKKEQRSEQISR 327
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
606-1029 |
3.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQ-REELEKLESKRKLIEEMEEKQKsdkaELERMQQEVETRRKETEIVqRQIRKQEESLKRR--SFHIEnKLKD 682
Cdd:PRK03918 318 RLEEEINGiEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA-KAKKEELERLKKRltGLTPE-KLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 683 LLAEKERFEEERLREQQGLEQQR---RQEEESLFRIREELRKLQ--------ELNSHEQAEKVQIF-QELDRLHQEqnaq 750
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKELLEEYtAELKRIEKE---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 751 saklrlekrrleeeekeqVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELE 830
Cdd:PRK03918 468 ------------------LKEIEEKERKLRKELR--------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 831 RAQQYFLEFKRRqLVKL----ASLEKDLVQQKDLLSK---------EVQEEKVALEHVKCDAGgdpsFLATDDGN----- 892
Cdd:PRK03918 522 KKAEEYEKLKEK-LIKLkgeiKSLKKELEKLEELKKKlaelekkldELEEELAELLKELEELG----FESVEELEerlke 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 893 ----------ILGGPPDL------------------DKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVL 944
Cdd:PRK03918 597 lepfyneyleLKDAEKELereekelkkleeeldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 945 GLDttlcqvekevgekeeqiAQYQANASQLQQLRATFEftaNVARQEEKVRRKEKEIlesqekqqrEALEQAVAKLEQRR 1024
Cdd:PRK03918 677 GLR-----------------AELEELEKRREEIKKTLE---KLKEELEEREKAKKEL---------EKLEKALERVEELR 727
|
....*
gi 2507456505 1025 SALQR 1029
Cdd:PRK03918 728 EKVKK 732
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
798-1032 |
3.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 798 QEEKRELESI-REALLQAKEMRaggdHTCRDELERaqqyflEFKRRQlVKLASLEKDLVQQKDLLSKEvqeekvalehvk 876
Cdd:PRK12704 45 EEAKKEAEAIkKEALLEAKEEI----HKLRNEFEK------ELRERR-NELQKLEKRLLQKEENLDRK------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 877 cdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhlpalLEEKQRVLDALdsgvlgldttlcqvEKE 956
Cdd:PRK12704 102 -----------------------LELLEKREEELEKKEKELEQKQQE-----LEKKEEELEEL--------------IEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 957 VGEKEEQIAQY---QANASQLQQLRATfeftanvARQE--EKVRRKEKEILESQEKQQREALEQAVakleqrrsalQRCS 1031
Cdd:PRK12704 140 QLQELERISGLtaeEAKEILLEKVEEE-------ARHEaaVLIKEIEEEAKEEADKKAKEILAQAI----------QRCA 202
|
.
gi 2507456505 1032 T 1032
Cdd:PRK12704 203 A 203
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
611-711 |
3.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 690
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
90 100
....*....|....*....|.
gi 2507456505 691 EEERLREQQGLEQQRRQEEES 711
Cdd:COG3883 216 AAAAAAAAAAAAAAAAAAAAA 236
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
611-685 |
3.27e-03 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 39.58 E-value: 3.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2507456505 611 RQQREELEKLESKRKLIEEM-EEKQKSDKAELERMQ-QEVETRRKETEIVQRQIRKQEESLKR-RSFHIENKLKDLLA 685
Cdd:pfam04696 22 KKEESKQKEKEERRAEIEKRlEEKAKQEKEELEERKrEEREELFEERRAEQIELRALEEKLELkELMETWHENLKALA 99
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
605-750 |
3.38e-03 |
|
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: 42.25 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 605 LRLEFERQQREELEKLESKRKLIEEMEEKQksdkaELERMQQEvETRRKeteIVQRQIRKQEESLKRRSFHiENKLKDL- 683
Cdd:pfam15709 389 IRLRKQRLEEERQRQEEEERKQRLQLQAAQ-----ERARQQQE-EFRRK---LQELQRKKQQEEAERAEAE-KQRQKELe 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2507456505 684 --LAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVqIFQELDRLHQEQNAQ 750
Cdd:pfam15709 459 mqLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARL-ALEEAMKQAQEQARQ 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
611-711 |
3.92e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 690
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
90 100
....*....|....*....|.
gi 2507456505 691 EEERLREQQGLEQQRRQEEES 711
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAA 229
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
702-1059 |
4.16e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 702 EQQRRQEEESLFRIREELRKLQElNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRK 781
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMK-IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 782 RQDTApllcpgeAQRAQEEKRELESIREALLQakemraggdhtCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLL 861
Cdd:pfam12128 295 LDDQW-------KEKRDELNGELSAADAAVAK-----------DRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 862 SkEVQEEKVALE--HVKCDAGGDPSFLATDDGN---ILGGPPDLDKIKTAETR--------LQSREHQLQDLLQNHLPAL 928
Cdd:pfam12128 357 E-NLEERLKALTgkHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEF 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 929 LEEKQRVLDALdsgvlgldttlcqvekevGEKEEQIAQYQANASQLQQLRAtFEFTANVARQEEKVRRKEKEILESQEKQ 1008
Cdd:pfam12128 436 NEEEYRLKSRL------------------GELKLRLNQATATPELLLQLEN-FDERIERAREEQEAANAEVERLQSELRQ 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2507456505 1009 QREALEQAVAKLEQRRSALQRCSTLDLEIQEQ-RQKLGSLH---TSEWSGWQASL 1059
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLhflRKEAPDWEQSI 551
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
607-672 |
4.32e-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: 41.12 E-value: 4.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2507456505 607 LEFERQQREEleklESKRKLIEEmEEKQKSDKAELE------RMQQEVETRRKETEivqRQIRKQEESLKRR 672
Cdd:pfam12037 76 LKIERQRVEY----EERRKTLQE-ETKQKQQRAQYQdelarkRYQDQLEAQRRRNE---ELLRKQEESVAKQ 139
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
606-873 |
4.47e-03 |
|
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: 41.87 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrRSFHIENKLKDL 683
Cdd:COG5185 254 KLEKLVEQNTDLrlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 684 LAEKERFEEERlreQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvQIFQELD-------RLHQEQNAQSAKLRL 756
Cdd:COG5185 331 KRETETGIQNL---TAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE-ELDSFKDtiestkeSLDEIPQNQRGYAQE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 757 EKRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREallqaKEMRAGGDhtcrDELERAQQYF 836
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATS--------SNEEVSKLLNELISELN-----KVMREADE----ESQSRLEEAY 469
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2507456505 837 LEFKRRQLVKLASLEKDLVQ---QKDLLSKEVQEEKVALE 873
Cdd:COG5185 470 DEINRSVRSKKEDLNEELTQiesRVSTLKATLEKLRAKLE 509
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
606-739 |
5.87e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 39.26 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 606 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELER-MQQEV-ETRRKETEIvqRQIRKQ-EESLKRRSFHIEnklkd 682
Cdd:pfam15346 23 RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEReREAELeEERRKEEEE--RKKREElERILEENNRKIE----- 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2507456505 683 llaekerfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQE 739
Cdd:pfam15346 96 -------------------EAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
611-746 |
6.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLLAEk 687
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2507456505 688 erfeeerlreqqgLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQELDRLHQE 746
Cdd:COG1340 169 -------------LKELRKEAEE----IHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
611-813 |
7.45e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 611 RQQREELEKLESKRKLIEE--MEEKQKSDK-AELERMQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLL 684
Cdd:COG1340 88 NELREELDELRKELAELNKagGSIDKLRKEiERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 685 AEKERFEEERLREQQGLE------QQRRQEEESLFRIREELRKlqELNS-HEQAekVQIFQELDRLHQEQNAQSaklrle 757
Cdd:COG1340 167 AELKELRKEAEEIHKKIKelaeeaQELHEEMIELYKEADELRK--EADElHKEI--VEAQEKADELHEEIIELQ------ 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2507456505 758 krrleeeekeqvQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQ 813
Cdd:COG1340 237 ------------KELRELRKELKKLRKKQ------RALKREKEKEELEEKAEEIFE 274
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
604-852 |
8.42e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 604 CLRLEFERQQREELEKLESKRKLIEEMEE--KQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENKL 680
Cdd:pfam13868 106 IVERIQEEDQAEAEEKLEKQRQLREEIDEfnEEQAEWKELEKEEEREEDERILEYLKEKAEREEErEAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 681 KDLLAEkerfeeerlreQQGLEQQRRQEEESLF--RIREELRKLQELNSHEQAEK-VQIFQELDRLHQEQNAQSAKLRLE 757
Cdd:pfam13868 186 IARLRA-----------QQEKAQDEKAERDELRakLYQEEQERKERQKEREEAEKkARQRQELQQAREEQIELKERRLAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2507456505 758 KRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELES-IREALLQAKEMRAggdhtcRDELERAQQYF 836
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKqIEEREEQRAAERE------EELEEGERLRE 322
|
250
....*....|....*.
gi 2507456505 837 LEFKRRQLVKLASLEK 852
Cdd:pfam13868 323 EEAERRERIEEERQKK 338
|
|
| |
