|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
51-399 |
2.31e-176 |
|
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: 538.48 E-value: 2.31e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01365 16 EKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 131 CVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDLL-RRKSSKTFNLRVR 209
Cdd:cd01365 95 CLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDLLnPKPKKNKGNLKVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE--MPCETVSKIHLVDL 287
Cdd:cd01365 174 EHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEtnLTTEKVSKISLVDL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 288 AGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIA 367
Cdd:cd01365 254 AGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329
|
330 340 350
....*....|....*....|....*....|..
gi 1907135704 368 TISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:cd01365 330 AISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
47-392 |
1.56e-144 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 450.10 E-value: 1.56e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 47 LFSGEKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFE 126
Cdd:pfam00225 5 LNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVESVLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNL 206
Cdd:pfam00225 72 GYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSKIHLV 285
Cdd:pfam00225 150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 286 DLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTI 364
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGNSKTL 298
|
330 340
....*....|....*....|....*...
gi 1907135704 365 MIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:pfam00225 299 MIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
47-399 |
1.57e-142 |
|
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: 445.09 E-value: 1.57e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 47 LFSGEKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFE 126
Cdd:smart00129 11 LNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEETAAPLVDSVLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfnL 206
Cdd:smart00129 78 GYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLLNPSSKK---L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVD 286
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 287 LAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMI 366
Cdd:smart00129 233 LAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDSLGGNSKTLMI 302
|
330 340 350
....*....|....*....|....*....|...
gi 1907135704 367 ATISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:smart00129 303 ANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
51-390 |
7.14e-132 |
|
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: 415.12 E-value: 7.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd00106 15 EARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 131 CVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEALFSRINETtRWDEASFRTEVSYLEIYNERVRDLLRRKSSKtfNLRVR 209
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDLLSPVPKK--PLSLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 1907135704 370 SPADVNYGETLSTLRYANRAK 390
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
85-392 |
4.83e-110 |
|
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: 354.33 E-value: 4.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 85 ERTKTFTYDFSFysaDTKSPdyvsQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPR 158
Cdd:cd01372 37 GTDKSFTFDYVF---DPSTE----QEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 159 ICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDA 238
Cdd:cd01372 110 AIQHIFKKIEKKK--DTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 239 GNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNIN 310
Cdd:cd01372 188 GSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISIN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 311 KSLVTLGNVISALADLSQDAAnplvkkkqvFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01372 268 SGLLALGNVISALGDESKKGA---------HVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRAR 338
|
..
gi 1907135704 391 NI 392
Cdd:cd01372 339 NI 340
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
51-392 |
5.45e-110 |
|
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: 353.69 E-value: 5.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 51 EKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01371 16 EKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDETARPLVDSVLEGYNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 131 CVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfNLR 207
Cdd:cd01371 84 TIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIRDLLGKDQTK--RLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 208 VREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--DAEMPCeTVSKIHLV 285
Cdd:cd01371 160 LKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeDGENHI-RVGKLNLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 286 DLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIM 365
Cdd:cd01371 239 DLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTRLLQDSLGGNSKTVM 307
|
330 340
....*....|....*....|....*..
gi 1907135704 366 IATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01371 308 CANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
40-401 |
2.19e-99 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 324.08 E-value: 2.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 40 VEILAAVLFSGEKDLEAKFIIQMEK-SKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLGT 118
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKlSSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVGK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 119 DVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEALFSRIN--ETTRWDEASFRTEVSYLEIY 188
Cdd:cd01373 65 PIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 189 NERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQA 268
Cdd:cd01373 145 NEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 269 KFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaanplvkkKQVFVPYRDSV 348
Cdd:cd01373 222 EKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDSK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907135704 349 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 401
Cdd:cd01373 294 LTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
82-392 |
4.06e-99 |
|
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: 323.14 E-value: 4.06e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 82 SGRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICE 161
Cdd:cd01370 55 KRRNKELKYVFDRVF-------DETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 162 ALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNI 241
Cdd:cd01370 128 ELFKRIESLK--DEKEFEVSMSYLEIYNETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 242 NRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCET-VSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVI 320
Cdd:cd01370 203 NRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVrQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCI 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 321 SALADLsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01370 283 NALADP---------GKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
72-394 |
1.92e-98 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 320.70 E-value: 1.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 72 LKIPEGGTG----DSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVVKSAFEGYNACVFAYGQTGSGKSYTMM 147
Cdd:cd01366 25 ITFPDEDGQtielTSIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LVQSALDGYNVCIFAYGQTGSGKTYTME 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 148 GNSGDSGLIPRICEALFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGP-YVEDLSKH 224
Cdd:cd01366 97 GPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPGNAPQKKLEIRHDSEKGDtTVTNLTEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 225 LVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfdaempceTVSKIHLVDLAGSERADATGA 298
Cdd:cd01366 174 KVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--------SVGKLNLVDLAGSERLNKSGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 299 TGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGE 378
Cdd:cd01366 246 TGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNE 313
|
330
....*....|....*.
gi 1907135704 379 TLSTLRYANRAKNIIN 394
Cdd:cd01366 314 TLNSLRFASKVNSCEL 329
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
90-392 |
1.20e-97 |
|
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: 318.12 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 90 FTYDFSFysaDTKSPDYVsqemVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINE 169
Cdd:cd01374 41 FTFDHVF---GGDSTNRE----VYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 170 TTRWDeasFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATG 249
Cdd:cd01374 114 TPDRE---FLLRVSYLEIYNEKINDLL---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 250 MNDVSSRSHAIFTIK-FTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsq 328
Cdd:cd01374 188 MNERSSRSHTIFRITiESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE--- 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135704 329 daanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01374 265 -------GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
82-392 |
7.20e-96 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 313.11 E-value: 7.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 82 SGRERTKTFTYDFSFYsADTkspdyvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPR 158
Cdd:cd01369 37 ATSETGKTFSFDRVFD-PNT------TQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 159 ICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDA 238
Cdd:cd01369 110 IVQDIFETIYSMD--ENLEFHVKVSYFEIYMEKIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 239 GNINRTTAATGMNDVSSRSHAIFTIKFTQAkfDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGN 318
Cdd:cd01369 185 GKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGN 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135704 319 VISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01369 263 VINALTD-----------GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
61-541 |
4.09e-89 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 302.81 E-value: 4.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 61 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 129
Cdd:COG5059 18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 130 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 209
Cdd:COG5059 91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:COG5059 244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 370 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 439
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 440 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 510
Cdd:COG5059 394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907135704 511 QT-----YVGREDASTEQDIVLHGLDLES--EHCVFEN 541
Cdd:COG5059 474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRD 511
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
79-401 |
9.47e-85 |
|
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: 282.29 E-value: 9.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 79 TGDSGRERTKTFTYDFSFYSAdtkspdyVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN--------- 149
Cdd:cd01364 40 GGLADKSSTKTYTFDMVFGPE-------AKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytw 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 150 --SGDSGLIPRICEALFSRINETtrwdEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHL 225
Cdd:cd01364 113 elDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVSYLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEIT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 226 VQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETV---SKIHLVDLAGSERADATGATGVR 302
Cdd:cd01364 189 VHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSI--TIHIKETTIDGEELvkiGKLNLVDLAGSENIGRSGAVDKR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 303 LKEGGNINKSLVTLGNVISALADlsqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLST 382
Cdd:cd01364 267 AREAGNINQSLLTLGRVITALVE------------RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLST 334
|
330
....*....|....*....
gi 1907135704 383 LRYANRAKNIINKPTINED 401
Cdd:cd01364 335 LEYAHRAKNIKNKPEVNQK 353
|
|
| FHA_KIF16B |
cd22732 |
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ... |
480-596 |
1.32e-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: 249.08 E-value: 1.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907135704 560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
49-426 |
2.94e-75 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 276.82 E-value: 2.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 49 SGEKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDfsfYSADTKSpdyvSQEMVFKTLGTDVVKSAFEGY 128
Cdd:PLN03188 93 NGVSDSGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQTFTFD---SIADPES----TQEDIFQLVGAPLVENCLAGF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 129 NACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTEVSYLEIYNERVR 193
Cdd:PLN03188 166 NSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCRCSFLEIYNEQIT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 194 DLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFT-IKFTQAKFDA 272
Cdd:PLN03188 244 DLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTcVVESRCKSVA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 273 E-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQVFVPYRDSVLTW 351
Cdd:PLN03188 321 DgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQRHIPYRDSRLTF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 352 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAEIARLKtllAQGN 425
Cdd:PLN03188 394 LLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVK---ANGN 470
|
.
gi 1907135704 426 Q 426
Cdd:PLN03188 471 N 471
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
105-390 |
8.29e-72 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 244.41 E-value: 8.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 105 DYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEALFSRINEttRWDEAsFRTE 181
Cdd:cd01375 57 HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVH 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 182 VSYLEIYNERVRDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSH 258
Cdd:cd01375 134 VSYLEIYNEQLYDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 259 AIFTIKFTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKK 338
Cdd:cd01375 214 CIFTIHLEAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KD 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 339 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01375 283 RTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
64-390 |
5.89e-70 |
|
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: 239.22 E-value: 5.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 64 KSKTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKS 143
Cdd:cd01368 28 INSTTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 144 YTMMGNSGDSGLIPRICEALFSRINETTRWdeasfrteVSYLEIYNERVRDLLRRKSSKTF----NLRVREHPKEGPYVE 219
Cdd:cd01368 104 YTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLEPSPSSPTkkrqSLRLREDHNGNMYVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 220 DLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE------TVSKIHLVDLAGSERA 293
Cdd:cd01368 176 GLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVDqdkdqiTVSQLSLVDLAGSERT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 294 DATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaANPLVKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPAD 373
Cdd:cd01368 256 SRTQNTGERLKEAGNINTSLMTLGTCIEVL-------RENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCA 328
|
330
....*....|....*..
gi 1907135704 374 VNYGETLSTLRYANRAK 390
Cdd:cd01368 329 SDYDETLHVMKFSAIAQ 345
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
84-390 |
9.09e-68 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 232.01 E-value: 9.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 84 RERTKTFTYDF-SFYSADTkspdyvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEA 162
Cdd:cd01376 38 RNHGETLKYQFdAFYGEES------TQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 163 LFsRINETTRWdeaSFRTEVSYLEIYNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNIN 242
Cdd:cd01376 112 LL-QMTRKEAW---ALSFTMSYLEIYQEKILDLLEPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 243 RTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISA 322
Cdd:cd01376 185 RTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNA 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135704 323 LadlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01376 264 L------------NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
89-390 |
3.49e-66 |
|
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: 227.56 E-value: 3.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 89 TFTYDFSFYSAdtkspdyVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG----NSGDSGLIPRICEALF 164
Cdd:cd01367 51 TFRFDYVFDES-------SSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 165 SRINETTRWDEasFRTEVSYLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRT 244
Cdd:cd01367 124 RLLNKLPYKDN--LGVTVSFFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 245 TAATGMNDVSSRSHAIFTIKFTQAKFDAempceTVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISAL 323
Cdd:cd01367 198 TGQTSANSQSSRSHAILQIILRDRGTNK-----LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRAL 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135704 324 AdlsqdaanplvkKKQVFVPYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01367 273 G------------QNKAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
|
|
| FHA_KIF16 |
cd22708 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ... |
480-588 |
3.05e-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: 216.37 E-value: 3.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 1907135704 560 GVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22708 81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
|
|
| FHA_KIF16A_STARD9 |
cd22731 |
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ... |
480-598 |
1.81e-49 |
|
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438783 [Multi-domain] Cd Length: 119 Bit Score: 171.50 E-value: 1.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907135704 560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLREKR 598
Cdd:cd22731 81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
|
|
| FHA_PHLB1 |
cd22713 |
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ... |
472-595 |
1.53e-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: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 472 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTeqdIVLHGLDLESEHCVFENAGGTVTLIPL 551
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907135704 552 rGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLR 595
Cdd:cd22713 78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
|
|
| FHA_KIF1 |
cd22705 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ... |
487-587 |
3.09e-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: 118.88 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 487 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDA 566
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 1907135704 567 TQLNQGAVILLGRTNMFRFNH 587
Cdd:cd22705 81 TRLKTGSRVILGKNHVFRFNH 101
|
|
| FHA_KIF1A |
cd22726 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ... |
488-596 |
1.24e-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: 106.17 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGT-----VTLIPLRGSQCSVNGVQ 562
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 1907135704 563 IVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22726 82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
|
|
| FHA_KIF14 |
cd22707 |
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ... |
484-588 |
1.25e-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: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 484 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQI 563
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 1907135704 564 VDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22707 84 SEPTVLHHGDRVILGGDHYFRFNHP 108
|
|
| FHA_KIF1B |
cd22727 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ... |
488-590 |
3.99e-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: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 562
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 1907135704 563 IVDATQLNQGAVILLGRTNMFRFNHPKE 590
Cdd:cd22727 83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
|
|
| FHA_KIF28P |
cd22709 |
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ... |
488-588 |
1.25e-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: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDA 566
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 1907135704 567 TQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22709 81 TELHHLDRVILGSNHLYVFVGP 102
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
106-322 |
6.70e-24 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 100.11 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 106 YVSQEMVFKTLGtDVVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEALFSRIN--ETTRWDEASFRTev 182
Cdd:cd01363 29 SESQPHVFAIAD-PAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 183 syleiynervrdllrrkssktfnlrvrehpkegpyvedlskhlVQNYSDVEELMDAGNINRtTAATGMNDVSSRSHAIFT 262
Cdd:cd01363 100 -------------------------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 263 IkftqakfdaempcetvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 322
Cdd:cd01363 136 I--------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| FHA_KIF13 |
cd22706 |
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ... |
505-588 |
2.01e-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: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 505 YHLKEgQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFR 584
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 1907135704 585 FNHP 588
Cdd:cd22706 98 LNCP 101
|
|
| FHA_KIF1C |
cd22728 |
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ... |
488-587 |
4.87e-19 |
|
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438780 [Multi-domain] Cd Length: 102 Bit Score: 84.15 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAsteqDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 562
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFrsipnPSGEVVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 1907135704 563 IVDATQLNQGAVILLGRTNMFRFNH 587
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
644-1118 |
1.43e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 803
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG1196 446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 884 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:COG1196 521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 944 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 1022
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1023 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1102
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
490
....*....|....*.
gi 1907135704 1103 DPARLEHEIHQLKQKI 1118
Cdd:COG1196 761 DLEELERELERLEREI 776
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
487-588 |
2.90e-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: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 487 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRG-SQCSV 558
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 1907135704 559 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22711 77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
64-196 |
4.69e-15 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 74.18 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 64 KSKTTITNLKIPEGGTGDSG-RERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTdVVKSAFEGYNACVFAYGQTGSGk 142
Cdd:pfam16796 30 PELLSEAQIDYPDETSSDGKiGSKNKSFSFDRVFPPESE-------QEDVFQEISQ-LVQSCLDGYNVCIFAYGQTGSG- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135704 143 sytmmgnsGDSGLIPRICEALFSRINETTR-WDeasFRTEVSYLEIYNERVRDLL 196
Cdd:pfam16796 101 --------SNDGMIPRAREQIFRFISSLKKgWK---YTIELQFVEIYNESSQDLL 144
|
|
| FHA_KIF13A |
cd22729 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ... |
490-598 |
9.37e-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: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 490 LIGIDDDLLSTGIILYHLKeGQTYVGredASTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 568
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 1907135704 569 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 598
Cdd:cd22729 80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
|
|
| FHA_KIF13B |
cd22730 |
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ... |
490-588 |
2.55e-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: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 490 LIGIDDDLLSTGIILYHLKEgQTYVGREDAsteQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 568
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 1907135704 569 LNQGAVILLGRTNMFRFNHP 588
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
655-1101 |
8.70e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 655 ESKRKLIEE----MEEKQKSDKAE--LERMQQEVEtrrkETEIVQRQIRKQEESLKR-----RSFH-IENKLKDLLAEKE 722
Cdd:COG1196 155 EERRAIIEEaagiSKYKERKEEAErkLEATEENLE----RLEDILGELERQLEPLERqaekaERYReLKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 723 RFEEERLREQQGLEQQRRQEEESlfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeeekeQ 802
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---------------L 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 803 VQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLA 882
Cdd:COG1196 294 LAELARLEQDIARLEE--------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 883 SLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQnhlpaL 962
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEA-------------------------LRAAAELAAQLEELEEAEEALLE-----R 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 963 LEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQ 1042
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135704 1043 QREALEQAVAKLEQRRSALQRcstldleiqeQRQKLGSLHTSEWSGWQASLETDGEALE 1101
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLL----------AGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
645-1118 |
1.03e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSfhIENKLKDLLAEKERF 724
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 725 EEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIF-QELDRLHQEQNAQSAKLRLEKrrleeeekeqv 803
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQ----------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL------LQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 877
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALlglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 878 LVKLASLEKDLVQQKDLLSKEVQEEkvalehvkCDAGGDPSFLATDDgnILGGPPDLDKIKTAETRLQSREHQLQdllqn 957
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEEL--------LAALGLPPDLSPEE--LLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 958 hLPALLEEKQRVLDALDSGvlgldttlcqvekevgekeeQIAQYQANASQLQQLRatfEFTANVARQEEKVRRKEKEILE 1037
Cdd:COG4717 365 -LEELEQEIAALLAEAGVE--------------------DEEELRAALEQAEEYQ---ELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1038 SQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSewsgwQASLETDGEAlemdpARLEHEIHQLKQK 1117
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEE------ELEELREELAELEAE-----LEQLEEDGEL-----AELLQELEELKAE 484
|
.
gi 1907135704 1118 I 1118
Cdd:COG4717 485 L 485
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
398-510 |
1.84e-11 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 64.86 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 398 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 428
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 429 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 496
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 1907135704 497 LLSTGIILYHLKEG 510
Cdd:pfam16183 163 PLMSECLLYYIKDG 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
642-1120 |
4.37e-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: 68.46 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 708
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 709 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLH---------- 778
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqqkttlt 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 779 -QEQNAQSAKLRLEKRRLEEEEKEQVQRV-----AHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 852
Cdd:TIGR00618 393 qKLQSLCKELDILQREQATIDTRTSAFRDlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 853 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 931
Cdd:TIGR00618 472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 932 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVG---- 992
Cdd:TIGR00618 544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqp 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 993 -EKEEQIAQYQANASQ-LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1068
Cdd:TIGR00618 624 eQDLQDVRLHLQQCSQeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135704 1069 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARLEHEI-HQLKQKICE 1120
Cdd:TIGR00618 704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELmHQARTVLKA 758
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
658-907 |
7.26e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.46 E-value: 7.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 658 RKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkdllaekerfeEERLREQQGLEQ 737
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ------------AAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 738 QRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleeeekeqvQRVAHLEEQLRK 815
Cdd:pfam17380 345 ERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN------------------ERVRQELEAARK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 816 RQdtaplLCPGEAQRA-QEEKRELESIREALLQAK--EMRAGGDHTCRdELERAQQYFLEfKRRQLVKLASLEKDLVQQK 892
Cdd:pfam17380 404 VK-----ILEEERQRKiQQQKVEMEQIRAEQEEARqrEVRRLEEERAR-EMERVRLEEQE-RQQQVERLRQQEEERKRKK 476
|
250
....*....|....*
gi 1907135704 893 DLLSKEVQEEKVALE 907
Cdd:pfam17380 477 LELEKEKRDRKRAEE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
646-1056 |
8.69e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 646 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENkLKDLLAEK 721
Cdd:TIGR02168 674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 722 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeEEKE 801
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-----------EAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 802 QVQRVAHLEEQLRkrqdtaplLCPGEAQRAQEEKRELESIREALlqAKEMRAGGdhTCRDELERAQQYFLEFKRRQLVKL 881
Cdd:TIGR02168 822 LRERLESLERRIA--------ATERRLEDLEEQIEELSEDIESL--AAEIEELE--ELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 882 ASLEKDLvQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPA 961
Cdd:TIGR02168 890 ALLRSEL-EELSEELRELESKRSELRR------------------------ELEELREKLAQLELRLEGLEVRIDNLQER 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 962 LLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeQIAQYQANASQLQQ---------LRATFEFtanvarQEEKVRRKE 1032
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIED--------------DEEEARRRLKRLENkikelgpvnLAAIEEY------EELKERYDF 1004
|
410 420
....*....|....*....|....
gi 1907135704 1033 KEilesqekQQREALEQAVAKLEQ 1056
Cdd:TIGR02168 1005 LT-------AQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
657-1063 |
1.98e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 657 KRKLIEEM-------EEKQKSdKAELErmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEEERL 729
Cdd:TIGR02169 155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 730 REQ-QGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKEQVQ-RVA 807
Cdd:TIGR02169 229 LKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQLRVKeKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 808 HLEEQLRKRQDTAPLlCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVKLASLEKD 887
Cdd:TIGR02169 298 ELEAEIASLERSIAE-KERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 888 LVQQKDLLSKEVQEEkvalehvkcdaggDPSFLATddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhLPALLEEKQ 967
Cdd:TIGR02169 362 LKEELEDLRAELEEV-------------DKEFAET-----------RDELKDYREKLEKLKREINELKRE-LDRLQEELQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 968 RvldaldsgvlgldttlcqvekevgeKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE--SQEKQQR 1044
Cdd:TIGR02169 417 R-------------------------LSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAAdlSKYEQEL 471
|
410
....*....|....*....
gi 1907135704 1045 EALEQAVAKLEQRRSALQR 1063
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQR 490
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
640-910 |
3.54e-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: 65.14 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFER--QQREELEKLESKRKLIEEME-------EKQKSDKAELERMQQEvetRRKETEIVQRQIRKQE-ESLKRRSFH 709
Cdd:pfam17380 295 KMEQERlrQEKEEKAREVERRRKLEEAEkarqaemDRQAAIYAEQERMAME---RERELERIRQEERKRElERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 710 IE-NKLKDLlaekerfeeerlreqQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 788
Cdd:pfam17380 372 MEiSRMREL---------------ERLQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 789 RLEKRRLEEEEKEQVQRVaHLEEQlrKRQDTAPLLCPGEAQRaQEEKRELESIREALLQAKEMRAggdHTCRDELERAQQ 868
Cdd:pfam17380 434 QREVRRLEEERAREMERV-RLEEQ--ERQQQVERLRQQEEER-KRKKLELEKEKRDRKRAEEQRR---KILEKELEERKQ 506
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907135704 869 YFLEFKRRQLVklasLEKDLVQQKDLLSKEVQEEKVALEHVK 910
Cdd:pfam17380 507 AMIEEERKRKL----LEKEMEERQKAIYEEERRREAEEERRK 544
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
489-585 |
6.91e-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: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 489 HLIGIDDDllsTGIILYHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQC--SVNGVQIVDA 566
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDL-GSTNgtFVNGKRITPP 73
|
90
....*....|....*....
gi 1907135704 567 TQLNQGAVILLGRTNmFRF 585
Cdd:cd00060 74 VPLQDGDVIRLGDTT-FRF 91
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-1122 |
1.43e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 719
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 720 EKERFEEERLREQQGLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQ---ELDRLHQEQNAQSAKLRLEKRRLE 796
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 797 EEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhTCRDELERAQQYFLEFkRR 876
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-------ELREELEEAEQALDAA-ER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 877 QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDP---SFLATDDG------NILGGppDLDKI--KTAETRLQ 945
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGyeaaieAALGG--RLQAVvvENLNAAKK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 946 SREHQLQD--------LLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEK------EEQIAQYQANAsqLQQL 1011
Cdd:TIGR02168 561 AIAFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllgGVLVVDDLDNA--LELA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1012 RATFEFTANVARQEEKVRR-----------------KEKEILESQEKQQR-----EALEQAVAKLEQRRSALQ-RCSTLD 1068
Cdd:TIGR02168 639 KKLRPGYRIVTLDGDLVRPggvitggsaktnssileRRREIEELEEKIEEleekiAELEKALAELRKELEELEeELEQLR 718
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1907135704 1069 LEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKICEVD 1122
Cdd:TIGR02168 719 KELEELSRQISALRKD-----LARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
589-865 |
1.73e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 589 KEAAKLREKRKSGLLSSFSLSMTDLSKSCEN--LSAVMLYNPGLFPIKGPICLRLEFERQQREELEKLESKRKLIEEMEE 666
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEarIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 667 KQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSfhiENKLKDllaekerfeeerlreqqglEQQRRQEEESL 746
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKA---EEAKKA-------------------EEDEKKAAEAL 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 747 FRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQlrkrqdtap 821
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE--------- 1765
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907135704 822 llcpgEAQRAQEEKRELESIREALLQAKemraggDHTCRDELER 865
Cdd:PTZ00121 1766 -----EEKKAEEIRKEKEAVIEEELDEE------DEKRRMEVDK 1798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
640-1118 |
1.85e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREEL--------EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQR---QIRKQEESLKRRSF 708
Cdd:TIGR02168 324 QLEELESKLDELaeelaeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 709 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQE-EESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAK 787
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 788 LRLEKrrleeeekeqvQRVAHLEEQLRKRQDtapllcPGEAQRAQEEKR-----------ELESIREALLQAKEMRAGG- 855
Cdd:TIGR02168 484 LAQLQ-----------ARLDSLERLQENLEG------FSEGVKALLKNQsglsgilgvlsELISVDEGYEAAIEAALGGr 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 856 -DHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK-------VALEHVKCDAGGDPSF-------- 919
Cdd:TIGR02168 547 lQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgVAKDLVKFDPKLRKALsyllggvl 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 920 --------------------LATDDGNIL-------GGPPDLD--------KIKTAETRLQSREHQLQDLLQNhlpalLE 964
Cdd:TIGR02168 627 vvddldnalelakklrpgyrIVTLDGDLVrpggvitGGSAKTNssilerrrEIEELEEKIEELEEKIAELEKA-----LA 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 965 EKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQR 1044
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135704 1045 EALEQAVAKLEQrrsALQRCSTLDLEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKI 1118
Cdd:TIGR02168 782 AEIEELEAQIEQ---LKEELKALREALDELRAELTLLNEE-----AANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
737-1101 |
5.26e-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: 61.61 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 737 QQRRQEEES-LFRIREELRKLQ----ELNS-----HEQAEKVQIFQELDRlhQEQNAQsaklrlekrrleeeEKEQVQRV 806
Cdd:TIGR02168 171 KERRKETERkLERTRENLDRLEdilnELERqlkslERQAEKAERYKELKA--ELRELE--------------LALLVLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 807 AHLEEQLRKRQDtapllcpgEAQRAQEEKRELES-IREALLQAKEMRAgGDHTCRDELERAQQYFLEFKRRQlvklASLE 885
Cdd:TIGR02168 235 EELREELEELQE--------ELKEAEEELEELTAeLQELEEKLEELRL-EVSELEEEIEELQKELYALANEI----SRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 886 KD---LVQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDLLQNH--LP 960
Cdd:TIGR02168 302 QQkqiLRERLANLERQLEELEAQLEELE------------------------SKLDELAEELAELEEKLEELKEELesLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 961 ALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQyqaNASQLQQLRATFE-FTANVARQEEKVRRKEKEILESQ 1039
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS---LNNEIERLEARLErLEDRRERLQQEIEELLKKLEEAE 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135704 1040 EKQQREAL---EQAVAKLEQRRSAL-QRCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALE 1101
Cdd:TIGR02168 435 LKELQAELeelEEELEELQEELERLeEALEELREELEEAEQALDAAERelAQLQARLDSLERLQENLE 502
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
640-853 |
9.43e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.52 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQeveTRRKETEIVQRQIRKQEESLKRRSFHIENKlkdl 717
Cdd:pfam17380 382 RLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQREVRRLEEERAREMERVRLE---- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 718 laekerfeeeRLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQ---IFQELdrlhqEQNAQSAKLRLEKRR 794
Cdd:pfam17380 455 ----------EQERQQQVERLRQQEEE---RKRKKLELEKEKRDRKRAEEQRrkiLEKEL-----EERKQAMIEEERKRK 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135704 795 LEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKEMRA 853
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAE---------EERRKQQEMEERRRIQEQMRKATEERS 566
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
640-868 |
1.07e-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: 59.97 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetRRKEtEIVQRQIRKQEESLKRRsfhiENKLKDLLa 719
Cdd:pfam15709 347 RLEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ----RRFE-EIRLRKQRLEEERQRQE----EEERKQRL- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 720 ekerfeeerlREQQGLEQQRRQEEEslFRireelRKLQELNSHEQAEkvqifqELDRLHQEQnaqsaklrlekrrleeee 799
Cdd:pfam15709 413 ----------QLQAAQERARQQQEE--FR-----RKLQELQRKKQQE------EAERAEAEK------------------ 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135704 800 keqvQRVAHLEEQLRKRQDTapLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQ 868
Cdd:pfam15709 452 ----QRQKELEMQLAEEQKR--LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMK 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
647-1058 |
1.17e-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: 60.47 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 647 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEE 726
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL-------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 727 ERLREQQGLEQQRRQEEESLFRIREELRKLQE--------LNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleee 798
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleeaLNDLEARLSHSRIPEIQAELSKLEEEVS------------ 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 799 ekEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELErAQQYFLEFKRRQL 878
Cdd:TIGR02169 809 --RIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIE-NLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 879 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDlLQNH 958
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELE------------------------RKIEELEAQIEKKRKRLSE-LKAK 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 959 LPALLEEKQRVLDALDSGVlgldttlcqvekEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE 1037
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDE------------EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEyEEVLKRLDELKE 993
|
410 420
....*....|....*....|...
gi 1907135704 1038 SQEK--QQREALEQAVAKLEQRR 1058
Cdd:TIGR02169 994 KRAKleEERKAILERIEEYEKKK 1016
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-1117 |
1.24e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQI---RKQEESLKRRSFhiENKLKDLL 718
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAE--EKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 719 AEKERFEEERLREQQGLEQQRRQEEEsLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE-QNAQSAKLRLEKRRLEE 797
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKAD 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 798 EEKEQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELERAQqyflEFKR 875
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAKKAeeAKKADEAKKAEEAKKADEAKKAE----EKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 876 RQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLL 955
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 956 QNHlpalLEEKQRVldaldsgvlgldttlcQVEKEVGEKEEQIAQYQANASQLQQLRAtfeftANVARQEEKVRRKEKEi 1035
Cdd:PTZ00121 1626 KKA----EEEKKKV----------------EQLKKKEAEEKKKAEELKKAEEENKIKA-----AEEAKKAEEDKKKAEE- 1679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1036 LESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPARLEHE----I 1111
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkI 1759
|
....*.
gi 1907135704 1112 HQLKQK 1117
Cdd:PTZ00121 1760 AHLKKE 1765
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
640-1077 |
1.36e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEKLESKRKLIEEM----EEKQKSD----KAELERMQQEVETRRKETEIVQRQIRKQEEslKRRSFHIE 711
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAkkkaEEKKKADeakkKAEEAKKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAK 1476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 712 NKLKDLLAEKERFEEERLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLE 791
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 792 KRRLEeeekeQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKReLESIREALLQAKEMRAggdhtcrDELERAQQyfl 871
Cdd:PTZ00121 1554 AEELK-----KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKA-------EEAKKAEE--- 1617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 872 EFKRRQLVKLASLEKDLVQQkdlLSKEVQEEKVALEHVKCDAggdpsflatddgnilggppDLDKIKTAETRLQSREHQL 951
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAE-------------------EENKIKAAEEAKKAEEDKK 1675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 952 QdllQNHLPALLEEKQRVLDALdsgvlgldttlcQVEKEVGEKEEQIAQYQAN-ASQLQQLRATFEFTANVARQEEKVRR 1030
Cdd:PTZ00121 1676 K---AEEAKKAEEDEKKAAEAL------------KKEAEEAKKAEELKKKEAEeKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907135704 1031 KEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQK 1077
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
644-1057 |
1.47e-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: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQ------ELDRLHQEQNAQSAKLRLEKRRLEE 797
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeeeeALLELLAELLEEAALLEAALAELLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 798 EEKEQVQRVAHLEEQLRKRQ------------DTAPLLCPGEAQRAQEEKRELESIREALLqakemrAGGDHTCRDELER 865
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEgflegvkaalllAGLRGLAGAVAVLIGVEAAYEAALEAALA------AALQNIVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 866 AQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKV--ALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 943
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 944 LQSREHQLQDL--------------------LQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQA 1003
Cdd:COG1196 639 AVTLAGRLREVtlegeggsaggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1004 NASQLQQLRATFEFT--------------------------ANVARQEEKVRRKEKEI-------------LESQE---- 1040
Cdd:COG1196 719 EELEEEALEEQLEAEreelleelleeeelleeealeelpepPDLEELERELERLEREIealgpvnllaieeYEELEeryd 798
|
490
....*....|....*....
gi 1907135704 1041 --KQQREALEQAVAKLEQR 1057
Cdd:COG1196 799 flSEQREDLEEARETLEEA 817
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
649-1117 |
2.52e-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: 59.21 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 649 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL------LAEKE 722
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 723 RFEEERLREQQGLEQQRRQEEE--SLFRIREELRKLQELNSH------EQAEKVQIFQELDRLHQEQNAQSAK------- 787
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQAQRIHTELQSKMRSrakllmk 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 788 -LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEK---RELESIREALLQAKEMRAGGDHTCRDel 863
Cdd:TIGR00618 330 rAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhiHTLQQQKTTLTQKLQSLCKELDILQR-- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 864 ERAQQYFLEFKRRQL-VKLASLEKDLV-QQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGppDLDKIKTAE 941
Cdd:TIGR00618 408 EQATIDTRTSAFRDLqGQLAHAKKQQElQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--TKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 942 TRLQSREHQLQDLLQNhLPALLEEKQRVLDA--LDSGVLGLDTTLCQVEKEVGEKEEQ-IAQYQANASQLQQLRATFEFT 1018
Cdd:TIGR00618 486 TRKKAVVLARLLELQE-EPCPLCGSCIHPNParQDIDNPGPLTRRMQRGEQTYAQLETsEEDVYHQLTSERKQRASLKEQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1019 ANVARQEEKV----RRKEKEILE--SQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLgSLHTSEWSGWQAS 1092
Cdd:TIGR00618 565 MQEIQQSFSIltqcDNRSKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELAL 643
|
490 500
....*....|....*....|....*
gi 1907135704 1093 LETDGEALEMDPARLEHEIHQLKQK 1117
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
804-1118 |
4.93e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA---QQYFLEFKRRQLVK 880
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 881 LASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsfLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLP 960
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAE-----------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 961 ALLEEKQRVLDALDSgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQE 1040
Cdd:TIGR02168 825 RLESLERRIAATERR---------------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1041 KQQREALEQAVAKL---EQRRSALQR--------CSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGE---ALEMDPAR 1106
Cdd:TIGR02168 890 ALLRSELEELSEELrelESKRSELRReleelrekLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenKIEDDEEE 969
|
330
....*....|..
gi 1907135704 1107 LEHEIHQLKQKI 1118
Cdd:TIGR02168 970 ARRRLKRLENKI 981
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
485-588 |
6.77e-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: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 485 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDASTEQ-DIVLHGLDLESEHCV-----------FENAGGT-- 545
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907135704 546 --VTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22712 76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
640-901 |
1.30e-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: 57.00 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETRRKETEIVQRQI---RKQEESLKRRSFHIENKL 714
Cdd:TIGR02169 202 RLRREREKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEIselEKRLEEIEQLLEELNKKI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 715 KDL------------------LAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDR 776
Cdd:TIGR02169 282 KDLgeeeqlrvkekigeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 777 LHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELESireallqakemrAGGD 856
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK-----RELDRLQEELQRLSE------------ELAD 424
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907135704 857 HtcRDELERAQQYFLEFKRRQLVKLASLEKD---LVQQKDLLSKEVQE 901
Cdd:TIGR02169 425 L--NAAIAGIEAKINELEEEKEDKALEIKKQewkLEQLAADLSKYEQE 470
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-948 |
2.41e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQRE---ELEKLESKRKLIEEmEEKQKSDKAELERMQQEV-----ETRRKETEIVQRQIRKQEESLKR---RSFHI 710
Cdd:PTZ00121 1078 DFDFDAKEdnrADEATEEAFGKAEE-AKKTETGKAEEARKAEEAkkkaeDARKAEEARKAEDARKAEEARKAedaKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 711 ENKLKDllaEKERFEEERLREQQGLEQQRRQEEeslFRIREELRKLQELNSHEQA---EKVQIFQELDRLHQEQNAQsAK 787
Cdd:PTZ00121 1157 ARKAED---ARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAArkaEEERKAEEARKAEDAKKAE-AV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 788 LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELER 865
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeeKKKADEAKKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 866 AQQyflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGdpsflATDDGNILGGPPDLDKIKTAETRLQ 945
Cdd:PTZ00121 1310 KAE-----EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA-----AADEAEAAEEKAEAAEKKKEEAKKK 1379
|
...
gi 1907135704 946 SRE 948
Cdd:PTZ00121 1380 ADA 1382
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
639-1117 |
2.71e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 639 LRLEFERQQREElEKLESKRKLIEEMEEKQK--------------SDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 704
Cdd:pfam02463 253 IESSKQEIEKEE-EKLAQVLKENKEEEKEKKlqeeelkllakeeeELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 705 RRSFHIENKLKDLLAEKERFEEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQifQELDRLHQEQNAQ 784
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE--ELELKSEEEKEAQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 785 SAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEA---QRAQEEKRELESIREALLQAKEMRAGGDHTCRD 861
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEElekQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 862 ELERAQQYFLEFKRRQLVK-LASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTA 940
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSgLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 941 ETR-----LQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQ-------ANASQL 1008
Cdd:pfam02463 569 ALTelplgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTklkesakAKESGL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1009 QQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREalEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEwsg 1088
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA--ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL--- 723
|
490 500
....*....|....*....|....*....
gi 1907135704 1089 wQASLETDGEALEMDPARLEHEIHQLKQK 1117
Cdd:pfam02463 724 -ADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
644-1118 |
3.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETeiVQRQIRKQEESLKRRsfhiENKLKDLLAEKER 723
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEER----ERRRARLEALLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRleeeekeQV 803
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR-------LL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLC------PGEAQ--------------------------------------------RAQE 833
Cdd:COG4913 444 ALRDALAEALGLDEAELPFVGelievrPEEERwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 834 EKRELESIREALLQAK--------------EMRAGGDHTC---RDELER--------------------------AQQYF 870
Cdd:COG4913 524 PDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdsPEELRRhpraitragqvkgngtrhekddrrriRSRYV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 871 LEFKRRQlvKLASLEKDLVQQKDLLSkEVQEEKVALEhvkcDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQ 950
Cdd:COG4913 604 LGFDNRA--KLAALEAELAELEEELA-EAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 951 LQDLLQNhlPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRR 1030
Cdd:COG4913 677 LERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1031 KEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMdPARLEHE 1110
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREWPAETADLDADLESLPEYLAL-LDRLEED 827
|
....*....
gi 1907135704 1111 -IHQLKQKI 1118
Cdd:COG4913 828 gLPEYEERF 836
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
644-957 |
3.96e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKER 723
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEeekeqv 803
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEkRELESIREALLQAKEMRAGGDHTcRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLP-RELAEELLEAKDSLEAKLGLALS-ALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135704 884 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQN 957
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
505-585 |
4.64e-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: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 505 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 582
Cdd:COG1716 16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90
|
...
gi 1907135704 583 FRF 585
Cdd:COG1716 91 LRF 93
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
645-1062 |
5.74e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQ---QEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEK 721
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALE----AELAELPerlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 722 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKL-QELNSHE-QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEE 799
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELeEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 800 KEQ--------VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFL 871
Cdd:COG4717 271 LILtiagvlflVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 872 EFKRRQLVKLASLEKDLVQQkdllskEVQEEKVALEHvKCDAGGDPSFLAtddgnilggppdLDKIKTAETRLQSREHQL 951
Cdd:COG4717 347 EELQELLREAEELEEELQLE------ELEQEIAALLA-EAGVEDEEELRA------------ALEQAEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 952 QDLLQNHLPALLEEkqrvLDALDSGVLgldttlcqvekevgekEEQIAQYQANASQLQQLRAtfEFTANVARQEEKVRRK 1031
Cdd:COG4717 408 EEQLEELLGELEEL----LEALDEEEL----------------EEELEELEEELEELEEELE--ELREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|.
gi 1907135704 1032 EKEILESQEKQQREALEQAVAKLEQRRSALQ 1062
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
645-1041 |
6.15e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELE-KLESKRK-------LIEEMEEKQKSdkaeLERmQQEVETRRKEteivqrqIRKQEESLKRRSFHIE-NKLK 715
Cdd:TIGR02168 171 KERRKETErKLERTREnldrledILNELERQLKS----LER-QAEKAERYKE-------LKAELRELELALLVLRlEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 716 DLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLhqEQNAQsaklrlekrrl 795
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQ----------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 796 eeeekEQVQRVAHLEEQLRKRQDTAPLLcpgeAQRAQEEKRELESIREALLQAKEMRAGgdhtCRDELERAQQYFLEFKR 875
Cdd:TIGR02168 306 -----ILRERLANLERQLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELES----LEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 876 R------QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdldkiktAETRLQSREH 949
Cdd:TIGR02168 373 RleeleeQLETLRSKVAQLELQIASLNNEIERLEARLER-------------------------------LEDRRERLQQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 950 QLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQ----YQANASQLQQLRATFEFTANVARQE 1025
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQENL 501
|
410
....*....|....*.
gi 1907135704 1026 EKVRRKEKEILESQEK 1041
Cdd:TIGR02168 502 EGFSEGVKALLKNQSG 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
648-1181 |
1.07e-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: 53.92 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 648 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF---HIENKLKDLLAEKERF 724
Cdd:TIGR02169 363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 725 EEERLREQQGLEQQRRQ----------EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRR 794
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKleqlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 795 L-----EEEEKEQV--QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDH---------- 857
Cdd:TIGR02169 520 IqgvhgTVAQLGSVgeRYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDlsilsedgvi 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 858 -------TCRDELERAQQYF---------LEFKRRQL--VKLASLEKDLVQQ-------------KDLLSKEVQEEKVAL 906
Cdd:TIGR02169 600 gfavdlvEFDPKYEPAFKYVfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 907 EHVKCDAGGDPSFLATDDGNILGGPPDL-DKIKTAETRLQSREHQLQDLLQNH--LPALLEEKQRVLDALDSGVLGLDTT 983
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEekLKERLEELEEDLSSLEQEIENVKSE 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 984 LCQVEKEVGEKEEQIAQYQA---------NASQLQQLRATFEFT-ANVARQEEKVRRKEKEIleSQEKQQREALEQAVAK 1053
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEalndlearlSHSRIPEIQAELSKLeEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQE 837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1054 LEQRRSALQ-RCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKICEVDG-VQRPHH 1129
Cdd:TIGR02169 838 LQEQRIDLKeQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAqIEKKRK 917
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135704 1130 GILEGQAVLSSL---------PPSGGNSHLAPLMDARISAYIEEEVQRRLhdlhRAIGDAN 1181
Cdd:TIGR02169 918 RLSELKAKLEALeeelseiedPKGEDEEIPEEELSLEDVQAELQRVEEEI----RALEPVN 974
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
648-1181 |
1.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 648 REELEKLESKRKLIEEMEE------KQKSDKAELERMQQ--EVETRRKETEIVQRQIRKQEESLKRrsfhienkLKDLLA 719
Cdd:COG4913 241 HEALEDAREQIELLEPIRElaeryaAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR--------LEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 720 EKERFEEERLREQQGLEQQRRQEE-ESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEE 798
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 799 EKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAqqyfLEFKRRQ- 877
Cdd:COG4913 389 AAALLEALEEELEALEEALAEA----EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA----LGLDEAEl 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 878 -----LVKLASLEKD----------------LVQQKDLlsKEVQE--------EKVALEHVKcDAGGDPSFLATDDGNIL 928
Cdd:COG4913 461 pfvgeLIEVRPEEERwrgaiervlggfaltlLVPPEHY--AAALRwvnrlhlrGRLVYERVR-TGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 929 GgppdldKIKTAETRLQSRehqLQDLLQNHLPALLEEKQRVLDALDSGVlgldTTLCQVEKEVGEKEEQIAQYQANASQL 1008
Cdd:COG4913 538 G------KLDFKPHPFRAW---LEAELGRRFDYVCVDSPEELRRHPRAI----TRAGQVKGNGTRHEKDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1009 QqlratFEFTANVARQEEKVRRKEKEILESQEkqQREALEQAVAKLEQRRSALQRCS----------TLDLEIQEQRQKL 1078
Cdd:COG4913 605 G-----FDNRAKLAALEAELAELEEELAEAEE--RLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1079 GSLHTSewSGWQASLETDGEALEMDPARLEHEIHQLKQKIcevDGVQRPHHGILEGQAVLSSL---PPSGGNSHLAPLMD 1155
Cdd:COG4913 678 ERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRleaAEDLARLELRALLE 752
|
570 580
....*....|....*....|....*..
gi 1907135704 1156 ARISAYIEEEVQRRLHD-LHRAIGDAN 1181
Cdd:COG4913 753 ERFAAALGDAVERELREnLEERIDALR 779
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
644-1081 |
1.61e-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: 53.43 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETR---------------RKETEIVQRQIRKQEES--LKRR 706
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqqlqtkeqihlqetRKKAVVLARLLELQEEPcpLCGS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 707 SFHIENKLKDLLaekerFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 786
Cdd:TIGR00618 510 CIHPNPARQDID-----NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 787 KLRLEKRRleeeekeqVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA 866
Cdd:TIGR00618 585 DIPNLQNI--------TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 867 QQYflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQS 946
Cdd:TIGR00618 657 QER----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 947 REHQLQDLLQNHLPALLEEKQRVLDAL-------DSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRAtfefta 1019
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARteahfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA------ 806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 1020 nvaRQEEKVRRKEKEILESQEKQQREaLEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1081
Cdd:TIGR00618 807 ---EIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
644-1115 |
2.08e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIE--EMEEKQKSD----KAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL 717
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEakKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 718 LAEKERFEEERLREQQGLEQQRRQEEEsLFRIREELRKLQELNSHEQAEKVQIfQELDRLHQEQNAQSAKLRLEKRRLEE 797
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 798 EEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIR---EALLQAKEMRAGGDhtCRDELERAQQYFLEFK 874
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAE--------EAKKAEEAKKKAEEAKkadEAKKKAEEAKKADE--AKKKAEEAKKKADEAK 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 875 RRQLVKLASLEKDLVQQKdllsKEVQEEKVALEHVKCDAGGDPSFLATDDgnilggppDLDK---IKTAETRLQSREHQL 951
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEA----KKADEAKKAEEAKKADEAKKAEEKKKAD--------ELKKaeeLKKAEEKKKAEEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 952 QDLLQNHLPALLEEKQRVLDALDSGVLGLDTtlcQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRK 1031
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYE---EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1032 EKEILESQEKQQREALEQAVAKLEQRRSALQrcstLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPA---RLE 1108
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKA 1724
|
....*..
gi 1907135704 1109 HEIHQLK 1115
Cdd:PTZ00121 1725 EEENKIK 1731
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
642-847 |
2.08e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERM-------QQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKl 714
Cdd:pfam13868 170 EREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELraklyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELK- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 715 kdllaekerfeeerlreQQGLEQQRRQEEESLFRIREELRKLQELnshEQAEKVQIFQELDRLHQEQNAQsaklrlekrr 794
Cdd:pfam13868 249 -----------------ERRLAEEAEREEEEFERMLRKQAEDEEI---EQEEAEKRRMKRLEHRRELEKQ---------- 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907135704 795 leeEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQ 847
Cdd:pfam13868 299 ---IEEREEQRAAEREEELEEGER--------LREEEAERRERIEEERQKKLK 340
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
640-837 |
2.17e-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: 52.65 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 719
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 720 EKERFEEERLREQQGLEQQRRQEEEslFRIREELRKLQELNSHEQaekvqifqeLDRLHQEQNAQSaklrlekrrleeee 799
Cdd:pfam15709 434 ELQRKKQQEEAERAEAEKQRQKELE--MQLAEEQKRLMEMAEEER---------LEYQRQKQEAEE-------------- 488
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907135704 800 keqvQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRE 837
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 ... |
646-968 |
3.35e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 646 QQREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFE 725
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEE---EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 726 EERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQA-----EKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEK 800
Cdd:pfam02463 269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 801 EQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK 880
Cdd:pfam02463 349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 881 lasLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsFLATDDGNILggppDLDKIKTAETRLQSREHQLQDLLQNHLP 960
Cdd:pfam02463 429 ---LEILEEEEESIELKQGKLTEEKEELEK--------QELKLLKDEL----ELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
....*...
gi 1907135704 961 ALLEEKQR 968
Cdd:pfam02463 494 KLEERSQK 501
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
657-770 |
3.92e-06 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 49.50 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 657 KRKLIEEMEEKQKSdKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEEERLREQQGLE 736
Cdd:pfam12072 52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEK----KEKELEAQQQQLE 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907135704 737 QQRRQEEEslfRIREELRKLQELN--SHEQAEKVQI 770
Cdd:pfam12072 124 EKEEELEE---LIEEQRQELERISglTSEEAKEILL 156
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
645-891 |
4.44e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENK 713
Cdd:pfam13868 2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 714 LKDLLAEKERFEEERLR-EQQGLEQQRRQEEESLFRIREELRK-----------LQELNSHEQAEKVQIFQELDRLHQ-- 779
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKqrqlreeidefNEEQAEWKELEKEEEREEDERILEyl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 780 -EQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLcpgEAQRAQEEKRELESIREALLQAKEMRAggdht 858
Cdd:pfam13868 162 kEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL---RAKLYQEEQERKERQKEREEAEKKARQ----- 233
|
250 260 270
....*....|....*....|....*....|...
gi 1907135704 859 cRDELERAQQYFLEFKRRQLVKLASLEKDLVQQ 891
Cdd:pfam13868 234 -RQELQQAREEQIELKERRLAEEAEREEEEFER 265
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-1118 |
4.66e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 710 IENKLKDLLAEKERFEEERLREQQGLEQQRRQ---EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 786
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 787 KLRLEKRRLEEEEKEqvQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELE-SIREALLQAKEMRAGGDHTCRDELER 865
Cdd:COG4717 131 YQELEALEAELAELP--ERLEELEERLEELRELE-----EELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 866 AQQYFLEFKRRQLV---KLASLEKDLVQ-QKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGN------------ILG 929
Cdd:COG4717 204 LQQRLAELEEELEEaqeELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlsliltiagvlfLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 930 GPPDLDKIKTAETRLQSREHQLQDLLQNHLPALleEKQRVLDALDSgvLGLDTTLcqVEKEVGEKEEQIAQYQANASQLQ 1009
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAA--LGLPPDL--SPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1010 QLRAtfeftanvARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQrqkLGSLHTSEWSGW 1089
Cdd:COG4717 358 ELEE--------ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL---LGELEELLEALD 426
|
410 420
....*....|....*....|....*....
gi 1907135704 1090 QASLETDGEALEMDPARLEHEIHQLKQKI 1118
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREEL 455
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
666-903 |
5.04e-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: 50.92 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 666 EKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhIENKLKDLlaekerfeeerLREQQGLEQQRRQEEES 745
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAAL-----------ARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 746 LFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRqdtapllcp 825
Cdd:COG4942 85 LAELEKEIAELRA----ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ--------- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135704 826 geAQRAQEEKRELESIREALLQAKEMRAGGdhtcRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK 903
Cdd:COG4942 152 --AEELRADLAELAALRAELEAERAELEAL----LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
639-766 |
5.11e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 48.11 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 639 LRLEFERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETRRKETEivqRQIRKQEESLKRRSFHIENKLKDll 718
Cdd:pfam05672 23 AREQREREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE---RRREEEERQRKAEEEAEEREQRE-- 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907135704 719 aekerfeeerlreQQGLEQQRRQEEESLFRIREEL-RKLQELNSHEQAE 766
Cdd:pfam05672 93 -------------QEEQERLQKQKEEAEAKAREEAeRQRQEREKIMQQE 128
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
644-910 |
5.34e-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: 50.69 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 723
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 feeerlrEQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIfqELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 803
Cdd:pfam13868 167 -------REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL--RAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKE---MRAGGDHTCRDELERAQQYFLEFKRRQlvK 880
Cdd:pfam13868 238 QQAREEQIELKERR---------LAEEAEREEEEFERMLRKQAEDEEieqEEAEKRRMKRLEHRRELEKQIEEREEQ--R 306
|
250 260 270
....*....|....*....|....*....|
gi 1907135704 881 LASLEKDLvQQKDLLSKEVQEEKVALEHVK 910
Cdd:pfam13868 307 AAEREEEL-EEGERLREEEAERRERIEEER 335
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
827-1081 |
5.73e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 827 EAQRAQEEKRELESIREALLQAKEmraggdhtCRDELERAQQYFLEFkRRQLVKLASLEkdlvQQKDLLSKEVQEEKVAL 906
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERY-AAARERLAELE----YLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 907 EHVKCDAGGDpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLcq 986
Cdd:COG4913 293 LEAELEELRA----------------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL-- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 987 vekevgekeeqiAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILEsQEKQQREALEQAVAKLEQRRSALQRcs 1065
Cdd:COG4913 355 ------------EERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLE-ALEEELEALEEALAEAEAALRDLRR-- 419
|
250
....*....|....*.
gi 1907135704 1066 tldlEIQEQRQKLGSL 1081
Cdd:COG4913 420 ----ELRELEAEIASL 431
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
640-971 |
9.10e-06 |
|
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: 50.66 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEE---SLKRRSFH 709
Cdd:pfam07888 68 REQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdikTLTQRVLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 710 IENKLKDLlaekerfeeerLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEkvqiFQELDRLHQEQNAQSAKLR 789
Cdd:pfam07888 148 RETELERM-----------KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 790 LEKRRLEEEEKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELES-----------IREALLQAKEMR--- 852
Cdd:pfam07888 213 DTITTLTQKLTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSSmaaqrdrtqaeLHQARLQAAQLTlql 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 853 AGGDHTCRDELERAQQyflefKRRQLVKLASLEKDLVQQ--KDLLSKE--VQEEKVALEHVKCDaggdpsflatddgniL 928
Cdd:pfam07888 289 ADASLALREGRARWAQ-----ERETLQQSAEADKDRIEKlsAELQRLEerLQEERMEREKLEVE---------------L 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907135704 929 GGPPDLDKIKTAETRLQSREHQL-QDLLQNHLPALLEEKQRVLD 971
Cdd:pfam07888 349 GREKDCNRVQLSESRRELQELKAsLRVAQKEKEQLQAEKQELLE 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
645-903 |
9.86e-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: 50.15 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhienklkdllaeker 723
Cdd:COG4942 26 EAELEQLQQeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 feeerlreqqgLEQQRRQEEESLFRIREELRK-LQELNSHEQAEKVQIFqeldrLHQEQNAQSAKLRLEKRRLEEEEKEQ 802
Cdd:COG4942 88 -----------LEKEIAELRAELEAQKEELAElLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 803 VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELERAQQYFLEfKRRQLVKLA 882
Cdd:COG4942 152 AEELRADLAELAALRAEL----EAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAE-LAAELAELQ 219
|
250 260
....*....|....*....|.
gi 1907135704 883 SLEKDLVQQKDLLSKEVQEEK 903
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAA 240
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
640-1081 |
1.13e-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: 50.56 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEKLesKRKLIEEMEEKQKsdkaELERMQQEVETRR-----KETEIVQRQIRKQEESLKRRSFHIENK- 713
Cdd:pfam01576 195 RLKKEEKGRQELEKA--KRKLEGESTDLQE----QIAELQAQIAELRaqlakKEEELQAALARLEEETAQKNNALKKIRe 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 714 LKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQ--EQNAQSaklrle 791
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKalEEETRS------ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 792 krrleeeEKEQVQrvahleeQLRKRQDTApllcpgeaqraqeekreLESIREALLQAKEMRAGgdhtcrdeLERAQQYfL 871
Cdd:pfam01576 343 -------HEAQLQ-------EMRQKHTQA-----------------LEELTEQLEQAKRNKAN--------LEKAKQA-L 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 872 EFKRRQLVK----LASLEKDLVQQKDLLSKEVQEEKVAL---EHVKCDAGGDPSFLATDDGNILGGPPDLDK--IKTAEt 942
Cdd:pfam01576 383 ESENAELQAelrtLQQAKQDSEHKRKKLEGQLQELQARLsesERQRAELAEKLSKLQSELESVSSLLNEAEGknIKLSK- 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 943 RLQSREHQLQD---LLQNHLPALLEEKQRvLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATFEFTA 1019
Cdd:pfam01576 462 DVSSLESQLQDtqeLLQEETRQKLNLSTR-LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA---QLSDMKKKLEEDA 537
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135704 1020 NVARQEEKVRRKEKEILESQeKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSL 1081
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEAL-TQQLEEKAAAYDKLEKTKNRLQQeLDDLLVDLDHQRQLVSNL 599
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
647-774 |
1.16e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 647 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEE 726
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK----KEK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907135704 727 ERLREQQGLEQQRRQEEEslfRIREELRKLQELN--SHEQAeKVQIFQEL 774
Cdd:PRK12704 118 ELEQKQQELEKKEEELEE---LIEEQLQELERISglTAEEA-KEILLEKV 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
820-1081 |
1.27e-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: 49.76 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 820 APLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAQQyflefKRRQLVK-LASLEKDLVQQKDLLsKE 898
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEK-----------ELAALKK-----EEKALLKqLAALERRIAALARRI-RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 899 VQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSG- 976
Cdd:COG4942 74 LEQELAALEA------------------------ELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPe 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 977 -VLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLE 1055
Cdd:COG4942 130 dFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
250 260
....*....|....*....|....*.
gi 1907135704 1056 QRRSALQrcstldlEIQEQRQKLGSL 1081
Cdd:COG4942 210 ELAAELA-------ELQQEAEELEAL 228
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
642-765 |
1.57e-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: 50.12 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLiEEMEEKQKSDKAELERMQQEvetrRKETEIVQRQIRKQE-ESLKRRSFHIENKLKDLLAE 720
Cdd:pfam17380 447 EMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKE 521
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907135704 721 KERFEEERLREQQG--LEQQRR--QEEESLFRIREELRKLQELNSHEQA 765
Cdd:pfam17380 522 MEERQKAIYEEERRreAEEERRkqQEMEERRRIQEQMRKATEERSRLEA 570
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
648-908 |
2.96e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 648 REELEKLESKRKLIEEMEEK-QKSDKAELERMQQEVETRRKETEIVQRQIRKQEES------LKRRSFHIENKLKDLlae 720
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELeeeyllYLDYLKLNEERIDLL--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 721 kerfeeerlreqQGLEQQRRQEEESLFRIRE-ELRKL-QELNSHEQAEKVQIFQELDRLHQEqnAQSAKLRLEKRRLEEE 798
Cdd:pfam02463 243 ------------QELLRDEQEEIESSKQEIEkEEEKLaQVLKENKEEEKEKKLQEEELKLLA--KEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 799 EKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGgdhtcRDELERAQQYFLEFKRRQL 878
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-----QEKLEQLEEELLAKKKLES 383
|
250 260 270
....*....|....*....|....*....|
gi 1907135704 879 VKLASLEKDLVQQKDLLSKEVQEEKVALEH 908
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
648-1121 |
4.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 648 REELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEN--KLKDLLAEKE 722
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 723 RFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELnsheQAEKVQIFQELDRL---HQEQNAQSAKLRLEKRRLEEEE 799
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL----KKKLKELEKRLEELeerHELYEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 800 KEQVQRVAHLEEQLRKRQDTAPLlcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTC---------RDELERAQQYF 870
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEE----EISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 871 LEFK----------------RRQLVKLASL---EKDLVQQKDLLS--KEVQEE--KVALEHVKCDAG---GDPSFLATDD 924
Cdd:PRK03918 459 AELKriekelkeieekerklRKELRELEKVlkkESELIKLKELAEqlKELEEKlkKYNLEELEKKAEeyeKLKEKLIKLK 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 925 GNILGGPPDLDKIKTAETRLQSREHQLQDllqnhlpaLLEEKQRVLDALDSgvLGLDTtlcqvekevgekeeqiaqYQAN 1004
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDE--------LEEELAELLKELEE--LGFES------------------VEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1005 ASQLQQLRATF-EFTanvarqEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQrcstldlEIQEQRQKLGSLHT 1083
Cdd:PRK03918 591 EERLKELEPFYnEYL------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------ELRKELEELEKKYS 657
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907135704 1084 SEwsgWQASLETDGEALEMDPARLEHEIHQLKQKICEV 1121
Cdd:PRK03918 658 EE---EYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
646-903 |
6.57e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 646 QQREELEKLESKRK-LIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLlaekerf 724
Cdd:COG4372 10 KARLSLFGLRPKTGiLIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 725 eeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlEKRRLEEEEKEQVQ 804
Cdd:COG4372 83 --------EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA----QIAELQSEIAEREE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 805 RVAHLEEQLRKRQDTAPLLcpGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASL 884
Cdd:COG4372 151 ELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
250
....*....|....*....
gi 1907135704 885 EKDLVQQKDLLSKEVQEEK 903
Cdd:COG4372 229 AKLGLALSALLDALELEED 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
639-705 |
6.93e-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: 47.81 E-value: 6.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135704 639 LRLEFERQQREELEKlESKRKLIE-EMEEKQKSDKAELERMQQEvETRRKETEI-----VQRQIRKQEESLKR 705
Cdd:pfam17380 497 LEKELEERKQAMIEE-ERKRKLLEkEMEERQKAIYEEERRREAE-EERRKQQEMeerrrIQEQMRKATEERSR 567
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
735-1078 |
6.99e-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: 47.81 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 735 LEQQR-RQEEESLFRIREELRKLQELNSHEQAE---KVQIFQELDRLHQEQNaqsaklrlekrrleeeekEQVQRVaHLE 810
Cdd:pfam17380 296 MEQERlRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERE------------------RELERI-RQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 811 EqlRKRQDtapllcpgEAQRAQEEKRELESIREalLQAKEM-RAGGDHTCRDELERAQQYFLEFKRRQlvklaslekdlv 889
Cdd:pfam17380 357 E--RKREL--------ERIRQEEIAMEISRMRE--LERLQMeRQQKNERVRQELEAARKVKILEEERQ------------ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 890 qqkdllsKEVQEEKVALEHVKCDaggdpsflatddgnilggppdldkiktaetRLQSREHQLQdllqnhlpALLEEKQRV 969
Cdd:pfam17380 413 -------RKIQQQKVEMEQIRAE------------------------------QEEARQREVR--------RLEEERARE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 970 LDALDSgvlgldttlcqvekevgekeeqiaQYQANASQLQQLRatfeftanvarQEEKVRRKEKEILESQEKQQREAleq 1049
Cdd:pfam17380 448 MERVRL------------------------EEQERQQQVERLR-----------QQEEERKRKKLELEKEKRDRKRA--- 489
|
330 340
....*....|....*....|....*....
gi 1907135704 1050 avakLEQRRSALQRcstldlEIQEQRQKL 1078
Cdd:pfam17380 490 ----EEQRRKILEK------ELEERKQAM 508
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
644-878 |
9.40e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREEleklESKRKLIEEMEEKQK---------SDKAELERMQQEVETR---RKETEIVQRQIRKQEESLKRRSFHI- 710
Cdd:pfam02029 66 DRTAKRE----ERRQKRLQEALERQKefdptiadeKESVAERKENNEEEENsswEKEEKRDSRLGRYKEEETEIREKEYq 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 711 ENKLKDllaekerfeEERLREQQGLEQQRRQEEESLFR----IREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 786
Cdd:pfam02029 142 ENKWST---------EVRQAEEEGEEEEDKSEEAEEVPtenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 787 KLRLEKRRLEEEEKEQVQRVAH---------------LEEQLRKRQDTAPLLCPGEAQRAQEEKRELESI------REAL 845
Cdd:pfam02029 213 EEEVTKLKVTTKRRQGGLSQSQereeeaevfleaeqkLEELRRRRQEKESEEFEKLRQKQQEAELELEELkkkreeRRKL 292
|
250 260 270
....*....|....*....|....*....|...
gi 1907135704 846 LQAKEMRaggdhtcRDELERAQQYFLEFKRRQL 878
Cdd:pfam02029 293 LEEEEQR-------RKQEEAERKLREEEEKRRM 318
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
645-1121 |
1.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRkliEEMEEKQKSDKAELERMQQEVetrrKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERF 724
Cdd:PRK03918 175 KRRIERLEKFIKRT---ENIEELIKEKEKELEEVLREI----NEISSELPELREELEKLEKEVKELE-ELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 725 EEERLREQQGLEQQRRQEEESLFRIREELRKLQEL--NSHEQAEKVQIFQELDRLHQEQNAQSAKLRlekrrleeeekeq 802
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEEYLDELREIE------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 803 vQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREAL--LQAKEMRAGGDHtcrDELERAQQyflefKRRQLVK 880
Cdd:PRK03918 314 -KRLSRLEEEINGIEE--------RIKELEEKEERLEELKKKLkeLEKRLEELEERH---ELYEEAKA-----KKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 881 LASLEKDLVQQKdlLSKEVQEEKVALEHVKcdaggdpsflatddgnilggpPDLDKIKTAETRLQSREHQLQDLLQNhlp 960
Cdd:PRK03918 377 LKKRLTGLTPEK--LEKELEELEKAKEEIE---------------------EEISKITARIGELKKEIKELKKAIEE--- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 961 alLEEKQRVldaldsgvlgldTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEftanvaRQEEKVRRKEKEiLESQE 1040
Cdd:PRK03918 431 --LKKAKGK------------CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE------EKERKLRKELRE-LEKVL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1041 KQQREALEQAvAKLEQRRSALQRCSTLDLEIQEQ--------RQKLGSLhtsewSGWQASLETD---GEALEMDPARLEH 1109
Cdd:PRK03918 490 KKESELIKLK-ELAEQLKELEEKLKKYNLEELEKkaeeyeklKEKLIKL-----KGEIKSLKKElekLEELKKKLAELEK 563
|
490
....*....|..
gi 1907135704 1110 EIHQLKQKICEV 1121
Cdd:PRK03918 564 KLDELEEELAEL 575
|
|
| FHA_Ki67 |
cd22673 |
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ... |
507-585 |
1.06e-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: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 507 LKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLrgSQCS---VNGVQIVDATQLNQGAVILLGrTNM 582
Cdd:cd22673 18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENL--STTNptlVNGKAIEKSAELKDGDVITIG-GRS 91
|
...
gi 1907135704 583 FRF 585
Cdd:cd22673 92 FRF 94
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
641-908 |
1.91e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 641 LEFERQQREEL-EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrrsfhiENKLKDLLA 719
Cdd:COG4372 68 LEQARSELEQLeEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ--------RKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 720 EKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKV--QIFQELDRLHQEQNAQSAKLRLEKRRLEE 797
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELlkEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 798 EEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 877
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
250 260 270
....*....|....*....|....*....|.
gi 1907135704 878 LVKLASLEKDLVQQKDLLSKEVQEEKVALEH 908
Cdd:COG4372 300 LLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
642-1057 |
2.30e-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: 46.28 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRR-----------KETEIVQRQIRKQEESLKRRSFHI 710
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRageakqlaeaqKEAELLRKQLSKTQEELEAQVTLV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 711 ENklkdlLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQ--------------ELNSHEQAEKVQIFQELDR 776
Cdd:pfam07111 221 ES-----LRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqsltHMLALQEEELTRKIQPSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 777 LHQE--QNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLlcpgeaQRAQEEKRELESIREALLQAK----E 850
Cdd:pfam07111 296 LEPEfpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL------QEQVTSQSQEQAILQRALQDKaaevE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 851 MRAGGDHTCRDELERAQqyflEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSF-----LATDDG 925
Cdd:pfam07111 370 VERMSAKGLQMELSRAQ----EARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLsnrlsYAVRKV 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 926 NILGGPPdLDKIKTAETRLQS-----REHQLQDLLQNHLPALLEEKQRvLDAldsgVLGLDTTLCQVEKEVGEKEEQIAQ 1000
Cdd:pfam07111 446 HTIKGLM-ARKVALAQLRQEScppppPAPPVDADLSLELEQLREERNR-LDA----ELQLSAHLIQQEVGRAREQGEAER 519
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1001 YQAN--ASQL-QQLRATFEFTANVARQEEKVRRKEKEILES-----QE-KQQRE----ALEQAVAKLEQR 1057
Cdd:pfam07111 520 QQLSevAQQLeQELQRAQESLASVGQQLEVARQGQQESTEEaaslrQElTQQQEiygqALQEKVAEVETR 589
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
642-1120 |
2.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLIEEMEEKQKSD---KAELERMQQEV---ETRRKETEIVQR--------QIRKQEESLKRRS 707
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADEAkkaEEKKKADEAKKKaeeakkadEAKKKAEEAKKKA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 708 FHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE--QNAQS 785
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK--KKAEEKKKADEAKKKAEEdkKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 786 AKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIR---EALLQAKEMRAGgdhtcrDE 862
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---------EAKKADEAKKKAEEAKkaeEAKKKAEEAKKA------DE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 863 LERAQQyflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDpsflaTDDGNILGGPPDLDKIKTAET 942
Cdd:PTZ00121 1475 AKKKAE-----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 943 RLQSREHQLQDLLQNhlpalLEEKQRVLDALDSgvlgldttlcQVEKEVGEKEEQIAQyQANASQLQQLRATFE----FT 1018
Cdd:PTZ00121 1545 KKKADELKKAEELKK-----AEEKKKAEEAKKA----------EEDKNMALRKAEEAK-KAEEARIEEVMKLYEeekkMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1019 ANVARQEEKVRRKEKEILESQE-----KQQREALEQAVAKLEQRRSALQ----RCSTLDLEIQEQRQKLGSLHTSEWSGW 1089
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEekkkvEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
490 500 510
....*....|....*....|....*....|.
gi 1907135704 1090 QASLETDGEALEmdparlEHEIHQLKQKICE 1120
Cdd:PTZ00121 1689 KAAEALKKEAEE------AKKAEELKKKEAE 1713
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
639-713 |
2.33e-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: 43.50 E-value: 2.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907135704 639 LRLEFERQQREELEKLESKRKliEEMEEKQKsdKAELERmQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK 713
Cdd:pfam15346 71 RKEEEERKKREELERILEENN--RKIEEAQR--KEAEER-LAMLEEQRRMKEERQRREKEEEEREKREQQKILNK 140
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
682-1081 |
2.36e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 682 VETRRKETEIVQRQIRKQEESLKRRSFH-----IENKLKDLLAEKERFEEERLREQQGLEQ---------QRRQEEESL- 746
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHerlngLESELAELDEEIERYEEQREQARETRDEadevleeheERREELETLe 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 747 -------------FRIREELRK-----------LQELNSHEQAEkvqifQELDRLHQE--QNAQSAKLRLEKRRLEEEEK 800
Cdd:PRK02224 258 aeiedlretiaetEREREELAEevrdlrerleeLEEERDDLLAE-----AGLDDADAEavEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 801 EQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFlEFKRRQLVK 880
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDL--EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF-GDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 881 LASLEKDLVQQKDLLSKEVQEEKVALEHV--------------KCDAGGDPsflatddgniLGGPPDLDKIKTAETRLQS 946
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTArerveeaealleagKCPECGQP----------VEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 947 REHQLQDLLQNHlpALLEEKqrvLDALDSGVlgldttlcqvekevgEKEEQIAQYQANASQLQQLRATFEFTANVARQEE 1026
Cdd:PRK02224 480 LEAELEDLEEEV--EEVEER---LERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 1027 KVRRKEKEILESQEKQQREA-----------------LEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1081
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAaaeaeeeaeeareevaeLNSKLAELKERIESLERIRTLLAAIADAEDEIERL 611
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
505-589 |
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 1907135704 505 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDAT-QLNQGAVILLGRTnM 582
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGiALRPGDRIELGQT-E 87
|
....*..
gi 1907135704 583 FRFNHPK 589
Cdd:pfam16697 88 FCLVPAD 94
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
639-850 |
2.59e-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: 46.20 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 639 LRLEFeRQQREELEKLESKR-----------KLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS 707
Cdd:TIGR02168 815 LNEEA-ANLRERLESLERRIaaterrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 708 FHIENKLKDLlaekerfeeerlreqQGLEQQRRQEEESLFRIREELRKLQElnsHEQAEKVQIFQELDRLHQEQNAQSAK 787
Cdd:TIGR02168 894 SELEELSEEL---------------RELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEYSLTLEE 955
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135704 788 LRLEKRRLEEEEKEQVQRVAHLEEQLrKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKE 850
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKI-KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
641-1051 |
2.62e-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: 46.32 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 641 LEFERQQREELEKLesKRKLIEEMEekqkSDKAELE------RMQQEVETRRkETEIVQRQIRKQEES---------LKR 705
Cdd:pfam01576 280 LESERAARNKAEKQ--RRDLGEELE----ALKTELEdtldttAAQQELRSKR-EQEVTELKKALEEETrsheaqlqeMRQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 706 RSFHIENKLKDLLAEKERFEEERLREQQGLE-------------QQRRQEEESlfRIREELRKLQELNS-HEQAEKVQif 771
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAKQALEsenaelqaelrtlQQAKQDSEH--KRKKLEGQLQELQArLSESERQR-- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 772 QEL-DRLHQEQNAQSAKLRLEKRRLEEEEKEQvQRVAHLEEQLrkrQDTAPLLcpgeaqraQEEKRE----------LES 840
Cdd:pfam01576 429 AELaEKLSKLQSELESVSSLLNEAEGKNIKLS-KDVSSLESQL---QDTQELL--------QEETRQklnlstrlrqLED 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 841 IREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHvKCDAggdpsfl 920
Cdd:pfam01576 497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEE-KAAA------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 921 atddgnilggppdLDKIKTAETRLQsreHQLQDLL-----QNHLPALLEEKQRVLDALdsgvlgldttlcqvekevgeke 995
Cdd:pfam01576 568 -------------YDKLEKTKNRLQ---QELDDLLvdldhQRQLVSNLEKKQKKFDQM---------------------- 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135704 996 eqIAQYQANASQLQQLRATFEFTA--------NVARQEEKVRRKEKEiLESQEKQQREALEQAV 1051
Cdd:pfam01576 610 --LAEEKAISARYAEERDRAEAEAreketralSLARALEEALEAKEE-LERTNKQLRAEMEDLV 670
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
933-1118 |
4.18e-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: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 933 DLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSGVlgldtTLCQVEKEVGEKEEQIAQYQANASQLQQL 1011
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAAL-----RLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1012 RATFEftANVARQEEKVRRKEKEILES------QEKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSLHT- 1083
Cdd:COG4913 311 LERLE--ARLDALREELDELEAQIRGNggdrleQLEREIERLERELEERERRRARLEAlLAALGLPLPASAEEFAALRAe 388
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907135704 1084 -----SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKI 1118
Cdd:COG4913 389 aaallEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
640-895 |
5.32e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEK----LESKRKLIEEMEE---KQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS-FHIE 711
Cdd:PRK04863 895 RVEEIREQLDEAEEakrfVQQHGNALAQLEPivsVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhFSYE 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 712 NKLKDLlaekerfeEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNaqsaklrle 791
Cdd:PRK04863 975 DAAEML--------AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA----QLAQYNQVLASLKSSYDAKR--------- 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 792 krrleeeekeqvQRVAHLEEQLrkrQDTAPLLCPGEAQRAQEEKRELesirEALLQAKEMRaggdhtcRDELERaQQYFL 871
Cdd:PRK04863 1034 ------------QMLQELKQEL---QDLGVPADSGAEERARARRDEL----HARLSANRSR-------RNQLEK-QLTFC 1086
|
250 260
....*....|....*....|....*
gi 1907135704 872 EFKRRQLVK-LASLEKDLVQQKDLL 895
Cdd:PRK04863 1087 EAEMDNLTKkLRKLERDYHEMREQV 1111
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
740-1061 |
5.69e-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: 45.17 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 740 RQEEESLFRiREELRKLQElnSHEQAEKVqiFQELDRLHQEQNAQSAKlrlekrrleeeekeqvqrvahLEEQLrkrQDT 819
Cdd:pfam01576 2 RQEEEMQAK-EEELQKVKE--RQQKAESE--LKELEKKHQQLCEEKNA---------------------LQEQL---QAE 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 820 APLLCPGEAQRAQ--EEKRELESIrealLQAKEMRAGgdhtcrDELERAQQYFLEFKRRQlVKLASLEKDLVQQKDLLSK 897
Cdd:pfam01576 53 TELCAEAEEMRARlaARKQELEEI----LHELESRLE------EEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 898 eVQEEKVALEhVKCDAGGDPSFLATDDGNILGGPPDL--DKIKTAETRLQSREHQLQDL--LQNHLPALLEEKQRVLDAL 973
Cdd:pfam01576 122 -LQLEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLleERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 974 DSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATF-----EFTANVARQEE----------KVRRKEKEILES 1038
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQA---QIAELRAQLakkeeELQAALARLEEetaqknnalkKIRELEAQISEL 276
|
330 340
....*....|....*....|...
gi 1907135704 1039 QEKQQREalEQAVAKLEQRRSAL 1061
Cdd:pfam01576 277 QEDLESE--RAARNKAEKQRRDL 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
640-1206 |
5.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQrEELEKLESKRKLIE-----EMEEKQKSDKAELERMQQEV----ETRRKETEIVQRQIRKQEESLKRRSfhi 710
Cdd:PTZ00121 1165 KAEEARKA-EDAKKAEAARKAEEvrkaeELRKAEDARKAEAARKAEEErkaeEARKAEDAKKAEAVKKAEEAKKDAE--- 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 711 enklkdllaEKERFEEERLREQQGLEQQRRQEEESLFRIR---EELRKLQELnshEQAEKVQIFQELDRLHQEQNAQSAK 787
Cdd:PTZ00121 1241 ---------EAKKAEEERNNEEIRKFEEARMAHFARRQAAikaEEARKADEL---KKAEEKKKADEAKKAEEKKKADEAK 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 788 LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRelesiREALLQAKEMRAGGDHTCRDELERAQ 867
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAE--------EAKKAAEAAK-----AEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 868 qyflEFKRRQLVKLASLEKdlvQQKDLLSKEVQEEKVALEHVKCDAGgdpsflATDDGNILGGPPDlDKIKTAETRLQSR 947
Cdd:PTZ00121 1376 ----AKKKADAAKKKAEEK---KKADEAKKKAEEDKKKADELKKAAA------AKKKADEAKKKAE-EKKKADEAKKKAE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 948 EHQLQDLLQNHlpalLEEKQRVLDALDSGvlgldttlcqVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEK 1027
Cdd:PTZ00121 1442 EAKKADEAKKK----AEEAKKAEEAKKKA----------EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1028 VRRKEKEILESQEKQQREALEQAvaklEQRRSALQrcstldLEIQEQRQKLGSLHTSEwsgwqaSLETDGEALEMDPARL 1107
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKA----EEAKKADE------AKKAEEKKKADELKKAE------ELKKAEEKKKAEEAKK 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1108 EHEIHQLKQKICEVdgVQRPHHGILEGQAVLSSLPPSGGNSHLAPLMDARISA---YIEEEVQRRLHDLHRAIGDANHTP 1184
Cdd:PTZ00121 1572 AEEDKNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
570 580
....*....|....*....|..
gi 1907135704 1185 ADVMKSNEELHNGTTQRKLKYE 1206
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAE 1671
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
645-744 |
7.50e-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: 44.36 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQevetrRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerf 724
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFE-----REREEIRESYEEKLRTELERQAEAHEEHLKDVLV----- 386
|
90 100
....*....|....*....|
gi 1907135704 725 eeerlreQQGLEQQRRQEEE 744
Cdd:pfam09731 387 -------EQEIELQREFLQD 399
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
512-577 |
9.42e-04 |
|
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
Pssm-ID: 459831 [Multi-domain] Cd Length: 66 Bit Score: 39.48 E-value: 9.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135704 512 TYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQ-CSVNGVQI-VDATQLNQGAVILL 577
Cdd:pfam00498 1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNgTFVNGQRLgPEPVRLKDGDVIRL 66
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
644-984 |
9.60e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETRRKETEIVQRQIRKQEeslkrrsfhienKLKDLLAEKER 723
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 724 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVqifQELDRLHQEQNAQSAklrLEKRRLEEEEKEQV 803
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKA---EEAKRKAEEEAKRKA---EEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 883
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 884 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLPALL 963
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340
....*....|....*....|.
gi 1907135704 964 EEKQRVLDALDSGVLGLDTTL 984
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGG 332
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
736-1063 |
9.84e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.49 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 736 EQQRRQEEEslFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRV--------- 806
Cdd:pfam15558 35 EELRRRDQK--RQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQenqrqekle 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 807 -AHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREA---LLQAKEMRAggdhtCRDELERAQQyflEFKRRQLVKLA 882
Cdd:pfam15558 113 rARQEAEQRKQC---------QEQRLKEKEEELQALREQnslQLQERLEEA-----CHKRQLKERE---EQKKVQENNLS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 883 SLEKDLVQQKDLLSKEVQEE---KVALEHvkcdaggdpSFLATDDgnilgGPPDLDKIKTAETRLQSREHQLQdLLQNHL 959
Cdd:pfam15558 176 ELLNHQARKVLVDCQAKAEEllrRLSLEQ---------SLQRSQE-----NYEQLVEERHRELREKAQKEEEQ-FQRAKW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 960 PALLEEKQRV--LDALdsgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARqeEKVRRKEKEILE 1037
Cdd:pfam15558 241 RAEEKEEERQehKEAL-----------------AELADRKIQQARQVAHKTVQDKAQRARELNLER--EKNHHILKLKVE 301
|
330 340
....*....|....*....|....*.
gi 1907135704 1038 SQEKQQREALEQAVAKLEQRRSALQR 1063
Cdd:pfam15558 302 KEEKCHREGIKEAIKKKEQRSEQISR 327
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
738-1120 |
1.02e-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: 44.17 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 738 QRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRL-----HQEQNAQSAklrlekrrleeeekeqvqrvahlEEQ 812
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsaresDLEQDYQAA-----------------------SDH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 813 LRKRQdtapllcpgEAQRAQEE----KRELESIREALLQAKEMRAGGDH---TCRDELERAQQYFLEFKrrqlVKLASLE 885
Cdd:COG3096 336 LNLVQ---------TALRQQEKieryQEDLEELTERLEEQEEVVEEAAEqlaEAEARLEAAEEEVDSLK----SQLADYQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 886 KDL-VQQKDLLskEVQEEKVALEHVKcdaggdpsflatddgnILGGPPDLDkIKTAETRLQSREHQLQDLLQnhlpALLE 964
Cdd:COG3096 403 QALdVQQTRAI--QYQQAVQALEKAR----------------ALCGLPDLT-PENAEDYLAAFRAKEQQATE----EVLE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 965 EKQRVLDA------------LDSGVLGlDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATF-EFTANVARQEEKVR-- 1029
Cdd:COG3096 460 LEQKLSVAdaarrqfekayeLVCKIAG-EVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERll 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1030 -------------RKEKEILESQEKQQREALEQAVAKLEQRRSALQRcsTLDlEIQEQRQKLGSLhTSEWSGWQASLET- 1095
Cdd:COG3096 539 eefcqrigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ--QLE-QLRARIKELAAR-APAWLAAQDALERl 614
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907135704 1096 ---DGEALEMDPA---------RLEHEIHQLKQKICE 1120
Cdd:COG3096 615 reqSGEALADSQEvtaamqqllEREREATVERDELAA 651
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
649-1126 |
1.09e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 649 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrqirKQEESLKRRSFHIENKLKDLLAEKERFEEER 728
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 729 LREQQGLEQQRRQEEESLFR-IREELrkLQELNSHEQAEKVQIFQELD----RLHQEQnaqsaklrlekrrleeeekEQV 803
Cdd:pfam12128 534 GTLLHFLRKEAPDWEQSIGKvISPEL--LHRTDLDPEVWDGSVGGELNlygvKLDLKR-------------------IDV 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 804 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL--LQAKEMRAGgdHTCRDELERAQQYFLEFKRRQLvkl 881
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELekASREETFAR--TALKNARLDLRRLFDEKQSEKD--- 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 882 aSLEKDLVQQKDLLSKEVQE---EKVALEHvkcdagGDPSFLatddgnilggppdldkiktAETRLQSREHQLQdlLQNH 958
Cdd:pfam12128 668 -KKNKALAERKDSANERLNSleaQLKQLDK------KHQAWL-------------------EEQKEQKREARTE--KQAY 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 959 LPALLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeqiaQYQANASQLQQLRATfeFTANVARQEEKVRRKEKEILES 1038
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRS-----------------GAKAELKALETWYKR--DLASLGVDPDVIAKLKREIRTL 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1039 QEKQQR-EALEQAVAKLEQ--------RRSALQ-RCSTLDLEIQEQRQKLGSLhtsewsgwQASLETDGEALEMDPARLE 1108
Cdd:pfam12128 781 ERKIERiAVRRQEVLRYFDwyqetwlqRRPRLAtQLSNIERAISELQQQLARL--------IADTKLRRAKLEMERKASE 852
|
490
....*....|....*...
gi 1907135704 1109 HEIHQLKQKICEVDGVQR 1126
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMS 870
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
639-1043 |
1.24e-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: 43.66 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 639 LRLEFERQQReeleKLESKRKLIEEMEEKQKSDKAELERMQQ--EVETRR-----KETEIVQRQIR---KQEESLKRRSF 708
Cdd:pfam10174 350 LRLRLEEKES----FLNKKTKQLQDLTEEKSTLAGEIRDLKDmlDVKERKinvlqKKIENLQEQLRdkdKQLAGLKERVK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 709 HIEN----------KLKDLLAEKERFEEERLREQQGLEQQRRQEEESLfriREELRKLQELNSHEQAEKVQIFQELDRL- 777
Cdd:pfam10174 426 SLQTdssntdtaltTLEEALSEKERIIERLKEQREREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDLk 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 778 -HQEQNAQSAKLRLEKRRLEEEEKEQ-VQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQAKEMRAGg 855
Cdd:pfam10174 503 eHASSLASSGLKKDSKLKSLEIAVEQkKEECSKLENQLKKAHNAE------EAVRTNPEINDRIRLLEQEVARYKEESG- 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 856 dhTCRDELERaqqyflefkrrqlvkLASLEKDLVQQKDLLSKEVQE-EKVALEHVKCdaggdpsfLATDDGNILGGPPDL 934
Cdd:pfam10174 576 --KAQAEVER---------------LLGILREVENEKNDKDKKIAElESLTLRQMKE--------QNKKVANIKHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 935 DKIKTAETRLQSREHqlQDLLQNHLPALLEEkqrVLDALDSGVLGLDTTlcqvekevgekeeqiaqyQANASQLQQLRAT 1014
Cdd:pfam10174 631 KKKGAQLLEEARRRE--DNLADNSQQLQLEE---LMGALEKTRQELDAT------------------KARLSSTQQSLAE 687
|
410 420 430
....*....|....*....|....*....|
gi 1907135704 1015 FEFTANVARQEekvRRKE-KEILESqeKQQ 1043
Cdd:pfam10174 688 KDGHLTNLRAE---RRKQlEEILEM--KQE 712
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
646-719 |
1.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907135704 646 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 719
Cdd:PRK12704 68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
640-1063 |
1.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQ-REELEKLESKRKLIEEMEEKQKsdkaELERMQQEVETRRKETEIVqRQIRKQEESLKRR--SFHIEnKLKD 716
Cdd:PRK03918 318 RLEEEINGiEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA-KAKKEELERLKKRltGLTPE-KLEK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 717 LLAEKERFEEERLREQQGLEQQR---RQEEESLFRIREELRKLQ--------ELNSHEQAEKVQIF-QELDRLHQEqnaq 784
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKELLEEYtAELKRIEKE---- 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 785 saklrlekrrleeeekeqVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELE 864
Cdd:PRK03918 468 ------------------LKEIEEKERKLRKELR--------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 865 RAQQYFLEFKRRqLVKL----ASLEKDLVQQKDLLSK---------EVQEEKVALEHVKCDAGgdpsFLATDDGN----- 926
Cdd:PRK03918 522 KKAEEYEKLKEK-LIKLkgeiKSLKKELEKLEELKKKlaelekkldELEEELAELLKELEELG----FESVEELEerlke 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 927 ----------ILGGPPDL------------------DKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVL 978
Cdd:PRK03918 597 lepfyneyleLKDAEKELereekelkkleeeldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 979 GLDttlcqvekevgekeeqiAQYQANASQLQQLRATFEftaNVARQEEKVRRKEKEIlesqekqqrEALEQAVAKLEQRR 1058
Cdd:PRK03918 677 GLR-----------------AELEELEKRREEIKKTLE---KLKEELEEREKAKKEL---------EKLEKALERVEELR 727
|
....*
gi 1907135704 1059 SALQR 1063
Cdd:PRK03918 728 EKVKK 732
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
633-907 |
1.47e-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: 43.56 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 633 IKGPICLRLEFERQQREELEKLESKRKLIeEMEEKQKSdkAELERMQQEVETRRKETEIVQRQIRKQEESLKrrsfhiEN 712
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKII-TMELQKKS--SELEEMTKFKNNKEVELEELKKILAEDEKLLD------EK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 713 KLKDLLAEKERFEEERLReqqGLEQQRRQEEESL------FRIREE--LRKLQELNSHEQAEK---VQIFQELDRLHQEq 781
Cdd:pfam05483 425 KQFEKIAEELKGKEQELI---FLLQAREKEIHDLeiqltaIKTSEEhyLKEVEDLKTELEKEKlknIELTAHCDKLLLE- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 782 NAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpgeAQRAQEEKRELESIREALLQAK-EMRAGGDHTcr 860
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENL-------EEKEMNLRDELESVREEFIQKGdEVKCKLDKS-- 571
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907135704 861 DELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSK---EVQEEKVALE 907
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKnieELHQENKALK 621
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
639-773 |
1.49e-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: 41.21 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 639 LRLEFERQQREELEKLESKRkliEEMEEKQKSDKAELERMQQEVETRRKEteivqRQIRKQEESLKRRSFHIENKLKDLL 718
Cdd:pfam11600 16 QRLEKDKERLRRQLKLEAEK---EEKERLKEEAKAEKERAKEEARRKKEE-----EKELKEKERREKKEKDEKEKAEKLR 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135704 719 AEKERFEEERLREQQGLEQQRRQEEESlfRIREELRKLQElnshEQAEKVQIFQE 773
Cdd:pfam11600 88 LKEEKRKEKQEALEAKLEEKRKKEEEK--RLKEEEKRIKA----EKAEITRFLQK 136
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
644-832 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK---------- 713
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 714 -----LKDLLAEKERFEEERLREQQGLEQQRRQeeeslfriREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 788
Cdd:COG3883 109 lgsesFSDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907135704 789 RLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQ 832
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
486-588 |
1.58e-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: 40.17 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 486 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFE-------NAGGTVTLIPLRGSQCSV 558
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvrlpkhRSEEKLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 1907135704 559 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
639-784 |
1.76e-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: 43.02 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 639 LRLEFERQQREELEKLESKRKLIEEMEEKQksdkaELERMQQEvETRRKeteIVQRQIRKQEESLKRRSFHiENKLKDL- 717
Cdd:pfam15709 389 IRLRKQRLEEERQRQEEEERKQRLQLQAAQ-----ERARQQQE-EFRRK---LQELQRKKQQEEAERAEAE-KQRQKELe 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135704 718 --LAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVqIFQELDRLHQEQNAQ 784
Cdd:pfam15709 459 mqLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARL-ALEEAMKQAQEQARQ 522
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1002-1085 |
1.80e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1002 QANASQLQQLRAtfEFTANVARQEEKvRRKEKEILESQEKQQrealeqavAKLEQRRSALQRC-STLDLEIQEQRQKLGS 1080
Cdd:PRK11637 169 QETIAELKQTRE--ELAAQKAELEEK-QSQQKTLLYEQQAQQ--------QKLEQARNERKKTlTGLESSLQKDQQQLSE 237
|
....*
gi 1907135704 1081 LHTSE 1085
Cdd:PRK11637 238 LRANE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
644-704 |
2.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135704 644 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 704
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
645-719 |
2.20e-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: 39.97 E-value: 2.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135704 645 RQQREELEKLESKRKLIEEM-EEKQKSDKAELERMQ-QEVETRRKETEIVQRQIRKQEESLKR-RSFHIENKLKDLLA 719
Cdd:pfam04696 22 KKEESKQKEKEERRAEIEKRlEEKAKQEKEELEERKrEEREELFEERRAEQIELRALEEKLELkELMETWHENLKALA 99
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
832-1066 |
2.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 832 QEEKRELESI-REALLQAKEMRaggdHTCRDELERaqqyflEFKRRQlVKLASLEKDLVQQKDLLSKEvqeekvalehvk 910
Cdd:PRK12704 45 EEAKKEAEAIkKEALLEAKEEI----HKLRNEFEK------ELRERR-NELQKLEKRLLQKEENLDRK------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 911 cdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhlpalLEEKQRVLDALdsgvlgldttlcqvEKE 990
Cdd:PRK12704 102 -----------------------LELLEKREEELEKKEKELEQKQQE-----LEKKEEELEEL--------------IEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 991 VGEKEEQIAQY---QANASQLQQLRATfeftanvARQE--EKVRRKEKEILESQEKQQREALEQAVakleqrrsalQRCS 1065
Cdd:PRK12704 140 QLQELERISGLtaeEAKEILLEKVEEE-------ARHEaaVLIKEIEEEAKEEADKKAKEILAQAI----------QRCA 202
|
.
gi 1907135704 1066 T 1066
Cdd:PRK12704 203 A 203
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
640-907 |
2.49e-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: 42.64 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrRSFHIENKLKDL 717
Cdd:COG5185 254 KLEKLVEQNTDLrlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 718 LAEKERFEEERlreQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvQIFQELD-------RLHQEQNAQSAKLRL 790
Cdd:COG5185 331 KRETETGIQNL---TAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE-ELDSFKDtiestkeSLDEIPQNQRGYAQE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 791 EKRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREallqaKEMRAGGDhtcrDELERAQQYF 870
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATS--------SNEEVSKLLNELISELN-----KVMREADE----ESQSRLEEAY 469
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907135704 871 LEFKRRQLVKLASLEKDLVQ---QKDLLSKEVQEEKVALE 907
Cdd:COG5185 470 DEINRSVRSKKEDLNEELTQiesRVSTLKATLEKLRAKLE 509
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
736-1093 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 736 EQQRRQEEESLFRIREELRKLQElNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRK 815
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMK-IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 816 RQDTApllcpgeAQRAQEEKRELESIREALLQakemraggdhtCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLL 895
Cdd:pfam12128 295 LDDQW-------KEKRDELNGELSAADAAVAK-----------DRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 896 SkEVQEEKVALE--HVKCDAGGDPSFLATDDGN---ILGGPPDLDKIKTAETR--------LQSREHQLQDLLQNHLPAL 962
Cdd:pfam12128 357 E-NLEERLKALTgkHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEF 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 963 LEEKQRVLDALdsgvlgldttlcqvekevGEKEEQIAQYQANASQLQQLRAtFEFTANVARQEEKVRRKEKEILESQEKQ 1042
Cdd:pfam12128 436 NEEEYRLKSRL------------------GELKLRLNQATATPELLLQLEN-FDERIERAREEQEAANAEVERLQSELRQ 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135704 1043 QREALEQAVAKLEQRRSALQRCSTLDLEIQEQ-RQKLGSLH---TSEWSGWQASL 1093
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLhflRKEAPDWEQSI 551
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
640-773 |
2.62e-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: 40.42 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELER-MQQEV-ETRRKETEIvqRQIRKQ-EESLKRRSFHIEnklkd 716
Cdd:pfam15346 23 RVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEReREAELeEERRKEEEE--RKKREElERILEENNRKIE----- 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907135704 717 llaekerfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQE 773
Cdd:pfam15346 96 -------------------EAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
638-886 |
2.87e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 638 CLRLEFERQQREELEKLESKRKLIEEMEE--KQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENKL 714
Cdd:pfam13868 106 IVERIQEEDQAEAEEKLEKQRQLREEIDEfnEEQAEWKELEKEEEREEDERILEYLKEKAEREEErEAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 715 KDLLAEkerfeeerlreQQGLEQQRRQEEESLF--RIREELRKLQELNSHEQAEK-VQIFQELDRLHQEQNAQSAKLRLE 791
Cdd:pfam13868 186 IARLRA-----------QQEKAQDEKAERDELRakLYQEEQERKERQKEREEAEKkARQRQELQQAREEQIELKERRLAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 792 KRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELES-IREALLQAKEMRAggdhtcRDELERAQQYF 870
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKqIEEREEQRAAERE------EELEEGERLRE 322
|
250
....*....|....*.
gi 1907135704 871 LEFKRRQLVKLASLEK 886
Cdd:pfam13868 323 EEAERRERIEEERQKK 338
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
645-745 |
2.93e-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: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 724
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
90 100
....*....|....*....|.
gi 1907135704 725 EEERLREQQGLEQQRRQEEES 745
Cdd:COG3883 216 AAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
645-780 |
3.07e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLLAEk 721
Cdd:COG1340 95 DELRKELAELNKAGGSIDKLRKEI----ERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE- 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135704 722 erfeeerlreqqgLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQELDRLHQE 780
Cdd:COG1340 169 -------------LKELRKEAEE----IHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
641-706 |
3.20e-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: 41.51 E-value: 3.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 641 LEFERQQREEleklESKRKLIEEmEEKQKSDKAELE------RMQQEVETRRKETEivqRQIRKQEESLKRR 706
Cdd:pfam12037 76 LKIERQRVEY----EERRKTLQE-ETKQKQQRAQYQdelarkRYQDQLEAQRRRNE---ELLRKQEESVAKQ 139
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
645-847 |
3.24e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKLIEE--MEEKQKSDK-AELERMQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLL 718
Cdd:COG1340 88 NELREELDELRKELAELNKagGSIDKLRKEiERLEWRQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 719 AEKERFEEERLREQQGLE------QQRRQEEESLFRIREELRKlqELNS-HEQAekVQIFQELDRLHQEQNAQSaklrle 791
Cdd:COG1340 167 AELKELRKEAEEIHKKIKelaeeaQELHEEMIELYKEADELRK--EADElHKEI--VEAQEKADELHEEIIELQ------ 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907135704 792 krrleeeekeqvQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQ 847
Cdd:COG1340 237 ------------KELRELRKELKKLRKKQ------RALKREKEKEELEEKAEEIFE 274
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
645-745 |
3.45e-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: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 724
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
90 100
....*....|....*....|.
gi 1907135704 725 EEERLREQQGLEQQRRQEEES 745
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAA 229
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
652-1120 |
4.10e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 652 EKLESKRKLI---EEMEEKQKSDKAELERMQQEVETRRKETE-----------IVQRQIRKQEESLK-----RRSFHIEN 712
Cdd:pfam01576 47 EQLQAETELCaeaEEMRARLAARKQELEEILHELESRLEEEEersqqlqnekkKMQQHIQDLEEQLDeeeaaRQKLQLEK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 713 -----KLKDLlaekERFEEERLREQQGLEQQRRQEEESLF----RIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNA 783
Cdd:pfam01576 127 vtteaKIKKL----EEDILLLEDQNSKLSKERKLLEERISeftsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 784 QSAKLRLEKRRLEEEEKEQVQ------RVAHLEEQLRKRQDT-APLLCPGE---AQRAQEEK--RELES----IREALLQ 847
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQiaelqaQIAELRAQLAKKEEElQAALARLEeetAQKNNALKkiRELEAqiseLQEDLES 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 848 AKEMRAGGDHTCRDELERaqqyfLEFKRRQLvkLASLEKDLVQQkDLLSKEVQEekvaLEHVKcdaggdpsflatddgni 927
Cdd:pfam01576 283 ERAARNKAEKQRRDLGEE-----LEALKTEL--EDTLDTTAAQQ-ELRSKREQE----VTELK----------------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 928 lggppdldkiKTAETRLQSREHQLQDLLQNHLPAL------LEEKQRVLDALDSGVLGLDT----------TLCQVEKEV 991
Cdd:pfam01576 334 ----------KALEEETRSHEAQLQEMRQKHTQALeelteqLEQAKRNKANLEKAKQALESenaelqaelrTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 992 GE----KEEQIAQYQANASQLQQLRATFE------------FTANVARQEEKVRRKEKEI--LESQ----------EKQQ 1043
Cdd:pfam01576 404 EHkrkkLEGQLQELQARLSESERQRAELAeklsklqselesVSSLLNEAEGKNIKLSKDVssLESQlqdtqellqeETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1044 REALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDG---EALEMDPARLEHEIHQLKQKICE 1120
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAgtlEALEEGKKRLQRELEALTQQLEE 563
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
645-781 |
5.92e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 39.08 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 645 RQQRE--ELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDllaeke 722
Cdd:pfam12474 6 EQQKDrfEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIRAEQKKRLKMFRESLKQEKKELK------ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 723 rfeeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHE---QAEKVQIFQELDRLHQEQ 781
Cdd:pfam12474 80 ----------QEVEKLPKFQRKEAKRQRKEELELEQKHEELeflQAQSEALERELQQLQNEK 131
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
610-1121 |
6.33e-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: 41.63 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 610 MTDLSKSCENL-SAVMLYNPGLFPIKGPICLRLEFERQQ---------REELEKLESkrKLIEEMEEKQK---SDKAELE 676
Cdd:pfam05483 25 KSNLSKNGENIdSDPAFQKLNFLPMLEQVANSGDCHYQEglkdsdfenSEGLSRLYS--KLYKEAEKIKKwkvSIEAELK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 677 RMQQEVETRRKETEIVQRQIR-----------KQEESLKRR---------SFHIENKLKDLLAEKERFEEERLREQQ--- 733
Cdd:pfam05483 103 QKENKLQENRKIIEAQRKAIQelqfenekvslKLEEEIQENkdlikennaTRHLCNLLKETCARSAEKTKKYEYEREetr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 734 ---------------GLEQQRRQEE----ESLFRIREELRKLQELNSHEQAE---------------------------- 766
Cdd:pfam05483 183 qvymdlnnniekmilAFEELRVQAEnarlEMHFKLKEDHEKIQHLEEEYKKEindkekqvsllliqitekenkmkdltfl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 767 ------KVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKR-QDTAPLLCpgeaQRAQEEKRELE 839
Cdd:pfam05483 263 leesrdKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlQIATKTIC----QLTEEKEAQME 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 840 SIREAL----LQAKEMRAGgdhTCR-DELERAQQYFLE-------------------------FKRRQLVKLASLEKDLV 889
Cdd:pfam05483 339 ELNKAKaahsFVVTEFEAT---TCSlEELLRTEQQRLEknedqlkiitmelqkksseleemtkFKNNKEVELEELKKILA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 890 QQKDLLSKEVQEEKVAlEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAE-----------TRLQSREHQLQDLLQNH 958
Cdd:pfam05483 416 EDEKLLDEKKQFEKIA-EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEehylkevedlkTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 959 LPALLEEKQRVLDALDSgVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTanvaRQEEKVRRKE-KEILE 1037
Cdd:pfam05483 495 DKLLLENKELTQEASDM-TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV----REEFIQKGDEvKCKLD 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 1038 SQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGE--ALEMDPARLEHEIHQLK 1115
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELELASAK 649
|
....*.
gi 1907135704 1116 QKICEV 1121
Cdd:pfam05483 650 QKFEEI 655
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
640-1057 |
6.72e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 640 RLEFERQQREEL-EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLL 718
Cdd:pfam07888 35 RLEECLQERAELlQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 719 AEKERFEEERLREQQ----------GLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQI-----------------F 771
Cdd:pfam07888 115 EEKDALLAQRAAHEArireleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqaklqqteeelrslskeF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 772 QELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELESireallqa 848
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSS-------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 849 keMRAGGDHTcRDELERAQqyfLEFKRRQLvKLASLEKDLVQQKDLLSKEVQEEKVALEhvkcdaggdpsflatddgnil 928
Cdd:pfam07888 263 --MAAQRDRT-QAELHQAR---LQAAQLTL-QLADASLALREGRARWAQERETLQQSAE--------------------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 929 ggpPDLDKIKTAETRLQSREHQLQDllqnhlpallEEKQRVldaldsgvlGLDTTLCQVEKEVGekeeqiAQYQANASQL 1008
Cdd:pfam07888 315 ---ADKDRIEKLSAELQRLEERLQE----------ERMERE---------KLEVELGREKDCNR------VQLSESRREL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1907135704 1009 QQLRATFeftanvarqeeKVRRKEKEILESqEKQQreaLEQAVAKLEQR 1057
Cdd:pfam07888 367 QELKASL-----------RVAQKEKEQLQA-EKQE---LLEYIRQLEQR 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
642-852 |
8.50e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 642 EFERQQREELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFH-----IENK 713
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSleqEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAE 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135704 714 LKDLLAEKERFEEERLREQQGLeQQRRQEEESLfriREELRKLQELNSHEQAEKVQIFQELDRLH---QEQNAQSAKLRL 790
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKL-NRLTLEKEYL---EKEIQELQEQRIDLKEQIKSIEKEIENLNgkkEELEEELEELEA 875
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135704 791 EKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELESIREALLQAKEMR 852
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKI-----EELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| |
