|
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 |
2.74e-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: 538.09 E-value: 2.74e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01365 16 EKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 131 CVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTRwDEASFRTEVSYLEIYNERVRDLL-RRKSSKTFNLRVR 209
Cdd:cd01365 95 CLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDLLnPKPKKNKGNLKVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAE--MPCETVSKIHLVDL 287
Cdd:cd01365 174 EHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEtnLTTEKVSKISLVDL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 288 AGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAnplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIA 367
Cdd:cd01365 254 AGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKS----KKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329
|
330 340 350
....*....|....*....|....*....|..
gi 1907135707 368 TISPADVNYGETLSTLRYANRAKNIINKPTIN 399
Cdd:cd01365 330 AISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
47-392 |
1.78e-144 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 450.10 E-value: 1.78e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 47 LFSGEKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFE 126
Cdd:pfam00225 5 LNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVESVLE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNL 206
Cdd:pfam00225 72 GYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE-TVSKIHLV 285
Cdd:pfam00225 150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 286 DLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTI 364
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGNSKTL 298
|
330 340
....*....|....*....|....*...
gi 1907135707 365 MIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:pfam00225 299 MIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
47-399 |
1.75e-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: 1.75e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 47 LFSGEKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFE 126
Cdd:smart00129 11 LNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEETAAPLVDSVLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 127 GYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfnL 206
Cdd:smart00129 78 GYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLLNPSSKK---L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 207 RVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVD 286
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 287 LAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMI 366
Cdd:smart00129 233 LAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDSLGGNSKTLMI 302
|
330 340 350
....*....|....*....|....*....|...
gi 1907135707 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 |
8.20e-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: 8.20e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 51 EKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd00106 15 EARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 131 CVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEALFSRINETtRWDEASFRTEVSYLEIYNERVRDLLRRKSSKtfNLRVR 209
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDLLSPVPKK--PLSLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:cd00106 157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 1907135707 370 SPADVNYGETLSTLRYANRAK 390
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
51-392 |
5.34e-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: 5.34e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 51 EKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTLGTDVVKSAFEGYNA 130
Cdd:cd01371 16 EKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDETARPLVDSVLEGYNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 131 CVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKtfNLR 207
Cdd:cd01371 84 TIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIRDLLGKDQTK--RLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 208 VREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--DAEMPCeTVSKIHLV 285
Cdd:cd01371 160 LKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeDGENHI-RVGKLNLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 286 DLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIM 365
Cdd:cd01371 239 DLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTRLLQDSLGGNSKTVM 307
|
330 340
....*....|....*....|....*..
gi 1907135707 366 IATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01371 308 CANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
85-392 |
5.92e-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: 353.94 E-value: 5.92e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 85 ERTKTFTYDFSFysaDTKSPdyvsQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPR 158
Cdd:cd01372 37 GTDKSFTFDYVF---DPSTE----QEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 159 ICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDA 238
Cdd:cd01372 110 AIQHIFKKIEKKK--DTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 239 GNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNIN 310
Cdd:cd01372 188 GSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISIN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 311 KSLVTLGNVISALADLSQDAAnplvkkkqvFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 390
Cdd:cd01372 268 SGLLALGNVISALGDESKKGA---------HVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRAR 338
|
..
gi 1907135707 391 NI 392
Cdd:cd01372 339 NI 340
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
40-401 |
2.56e-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: 323.69 E-value: 2.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 40 VEILAAVLFSGEKDLEAKFIIQMEK-SKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLGT 118
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKlSSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVGK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 119 DVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEALFSRIN--ETTRWDEASFRTEVSYLEIY 188
Cdd:cd01373 65 PIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEIY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 189 NERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQA 268
Cdd:cd01373 145 NEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 269 KFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaanplvkkKQVFVPYRDSV 348
Cdd:cd01373 222 EKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDSK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907135707 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 |
4.70e-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: 4.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 82 SGRERTKTFTYDFSFysadtksPDYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICE 161
Cdd:cd01370 55 KRRNKELKYVFDRVF-------DETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 162 ALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNI 241
Cdd:cd01370 128 ELFKRIESLK--DEKEFEVSMSYLEIYNETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 242 NRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCET-VSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVI 320
Cdd:cd01370 203 NRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVrQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCI 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 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 |
2.20e-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: 320.31 E-value: 2.20e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 72 LKIPEGGTG----DSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVVKSAFEGYNACVFAYGQTGSGKSYTMM 147
Cdd:cd01366 25 ITFPDEDGQtielTSIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LVQSALDGYNVCIFAYGQTGSGKTYTME 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 148 GNSGDSGLIPRICEALFSRINE--TTRWdeaSFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHPKEGP-YVEDLSKH 224
Cdd:cd01366 97 GPPESPGIIPRALQELFNTIKElkEKGW---SYTIKASMLEIYNETIRDLLAPGNAPQKKLEIRHDSEKGDtTVTNLTEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 225 LVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfdaempceTVSKIHLVDLAGSERADATGA 298
Cdd:cd01366 174 KVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI--------SVGKLNLVDLAGSERLNKSGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 299 TGVRLKEGGNINKSLVTLGNVISALAdlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGE 378
Cdd:cd01366 246 TGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNE 313
|
330
....*....|....*.
gi 1907135707 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 |
1.19e-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: 1.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 90 FTYDFSFysaDTKSPDYVsqemVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINE 169
Cdd:cd01374 41 FTFDHVF---GGDSTNRE----VYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 170 TTRWDeasFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATG 249
Cdd:cd01374 114 TPDRE---FLLRVSYLEIYNEKINDLL---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 250 MNDVSSRSHAIFTIK-FTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsq 328
Cdd:cd01374 188 MNERSSRSHTIFRITiESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE--- 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135707 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 |
7.94e-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: 312.73 E-value: 7.94e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 82 SGRERTKTFTYDFSFYsADTkspdyvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPR 158
Cdd:cd01369 37 ATSETGKTFSFDRVFD-PNT------TQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 159 ICEALFSRINETTrwDEASFRTEVSYLEIYNERVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDA 238
Cdd:cd01369 110 IVQDIFETIYSMD--ENLEFHVKVSYFEIYMEKIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 239 GNINRTTAATGMNDVSSRSHAIFTIKFTQAkfDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGN 318
Cdd:cd01369 185 GKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGN 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135707 319 VISALADlsqdaanplvkKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 392
Cdd:cd01369 263 VINALTD-----------GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
61-541 |
5.66e-89 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 302.43 E-value: 5.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 61 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 129
Cdd:COG5059 18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 130 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEALFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 209
Cdd:COG5059 91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 210 EHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETVSKIHLVDLAG 289
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 290 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 369
Cdd:COG5059 244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 370 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 439
Cdd:COG5059 314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 440 EKLHQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 510
Cdd:COG5059 394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907135707 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 |
1.24e-84 |
|
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: 281.91 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 79 TGDSGRERTKTFTYDFSFYSAdtkspdyVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN--------- 149
Cdd:cd01364 40 GGLADKSSTKTYTFDMVFGPE-------AKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytw 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 150 --SGDSGLIPRICEALFSRINETtrwdEASFRTEVSYLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHL 225
Cdd:cd01364 113 elDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVSYLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEIT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 226 VQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDAEMPCETV---SKIHLVDLAGSERADATGATGVR 302
Cdd:cd01364 189 VHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSI--TIHIKETTIDGEELvkiGKLNLVDLAGSENIGRSGAVDKR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 303 LKEGGNINKSLVTLGNVISALADlsqdaanplvkkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLST 382
Cdd:cd01364 267 AREAGNINQSLLTLGRVITALVE------------RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLST 334
|
330
....*....|....*....
gi 1907135707 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 |
1.39e-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: 1.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22732 1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907135707 560 GVQIVDATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 596
Cdd:cd22732 81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
49-426 |
3.61e-75 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 276.43 E-value: 3.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 49 SGEKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTKTFTYDfsfYSADTKSpdyvSQEMVFKTLGTDVVKSAFEGY 128
Cdd:PLN03188 93 NGVSDSGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQTFTFD---SIADPES----TQEDIFQLVGAPLVENCLAGF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 129 NACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEALFSRINE-----TTRwdEASFRTEVSYLEIYNERVR 193
Cdd:PLN03188 166 NSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCRCSFLEIYNEQIT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 194 DLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFT-IKFTQAKFDA 272
Cdd:PLN03188 244 DLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTcVVESRCKSVA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 273 E-MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAanplvkkKQVFVPYRDSVLTW 351
Cdd:PLN03188 321 DgLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-------KQRHIPYRDSRLTF 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 352 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KLIRELRAEIARLKtllAQGN 425
Cdd:PLN03188 394 LLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEVIRQLRDELQRVK---ANGN 470
|
.
gi 1907135707 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 |
9.70e-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: 244.03 E-value: 9.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 105 DYVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEALFSRINEttRWDEAsFRTE 181
Cdd:cd01375 57 HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVH 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 182 VSYLEIYNERVRDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSH 258
Cdd:cd01375 134 VSYLEIYNEQLYDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 259 AIFTIKFTQAKFDAEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaanplvkKK 338
Cdd:cd01375 214 CIFTIHLEAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KD 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 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 |
6.38e-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: 6.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 64 KSKTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKS 143
Cdd:cd01368 28 INSTTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 144 YTMMGNSGDSGLIPRICEALFSRINETTRWdeasfrteVSYLEIYNERVRDLLRRKSSKTF----NLRVREHPKEGPYVE 219
Cdd:cd01368 104 YTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLEPSPSSPTkkrqSLRLREDHNGNMYVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 220 DLSKHLVQNYSDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCE------TVSKIHLVDLAGSERA 293
Cdd:cd01368 176 GLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDVDqdkdqiTVSQLSLVDLAGSERT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 294 DATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaANPLVKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPAD 373
Cdd:cd01368 256 SRTQNTGERLKEAGNINTSLMTLGTCIEVL-------RENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCA 328
|
330
....*....|....*..
gi 1907135707 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 |
9.11e-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: 9.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 84 RERTKTFTYDF-SFYSADTkspdyvSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEA 162
Cdd:cd01376 38 RNHGETLKYQFdAFYGEES------TQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 163 LFsRINETTRWdeaSFRTEVSYLEIYNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNIN 242
Cdd:cd01376 112 LL-QMTRKEAW---ALSFTMSYLEIYQEKILDLLEPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 243 RTTAATGMNDVSSRSHAIFTIKFTQAKFDAEMPCETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISA 322
Cdd:cd01376 185 RTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNA 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135707 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 |
3.82e-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: 3.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 89 TFTYDFSFYSAdtkspdyVSQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG----NSGDSGLIPRICEALF 164
Cdd:cd01367 51 TFRFDYVFDES-------SSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 165 SRINETTRWDEasFRTEVSYLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYSDVEELMDAGNINRT 244
Cdd:cd01367 124 RLLNKLPYKDN--LGVTVSFFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 245 TAATGMNDVSSRSHAIFTIKFTQAKFDAempceTVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISAL 323
Cdd:cd01367 198 TGQTSANSQSSRSHAILQIILRDRGTNK-----LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRAL 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135707 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 |
2.72e-65 |
|
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.
Pssm-ID: 438760 [Multi-domain] Cd Length: 109 Bit Score: 216.37 E-value: 2.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22708 1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80
|
90 100
....*....|....*....|....*....
gi 1907135707 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 |
1.94e-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: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 480 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVN 559
Cdd:cd22731 1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907135707 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 |
1.52e-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: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 472 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTeqdIVLHGLDLESEHCVFENAGGTVTLIPL 551
Cdd:cd22713 1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907135707 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 |
3.07e-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: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 487 LPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDA 566
Cdd:cd22705 1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80
|
90 100
....*....|....*....|.
gi 1907135707 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 |
1.23e-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: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGT-----VTLIPLRGSQCSVNGVQ 562
Cdd:cd22726 2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81
|
90 100 110
....*....|....*....|....*....|....
gi 1907135707 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 |
1.26e-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: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 484 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQI 563
Cdd:cd22707 4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83
|
90 100
....*....|....*....|....*
gi 1907135707 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 |
3.97e-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: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 562
Cdd:cd22727 3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82
|
90 100
....*....|....*....|....*...
gi 1907135707 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 |
1.24e-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: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDA 566
Cdd:cd22709 1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80
|
90 100
....*....|....*....|..
gi 1907135707 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 |
6.65e-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: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 106 YVSQEMVFKTLGtDVVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEALFSRIN--ETTRWDEASFRTev 182
Cdd:cd01363 29 SESQPHVFAIAD-PAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 183 syleiynervrdllrrkssktfnlrvrehpkegpyvedlskhlVQNYSDVEELMDAGNINRtTAATGMNDVSSRSHAIFT 262
Cdd:cd01363 100 -------------------------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIE 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 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 |
2.00e-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: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 505 YHLKEgQTYVGREDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFR 584
Cdd:cd22706 19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97
|
....
gi 1907135707 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 |
4.94e-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: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 488 PHLIGIDDDLLSTGIILYHLKEGQTYVGREDAsteqDIVLHGLDLESEHCVF-----ENAGGTVTLIPLRGSQCSVNGVQ 562
Cdd:cd22728 2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFrsipnPSGEVVVTLEPCEGAETYVNGKQ 77
|
90 100
....*....|....*....|....*
gi 1907135707 563 IVDATQLNQGAVILLGRTNMFRFNH 587
Cdd:cd22728 78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
633-1107 |
1.65e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 712
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 713 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKvqifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 792
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQDTAPLLcpgeaQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 872
Cdd:COG1196 446 EAAEEEAELEEEEEALLELL-----AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 873 LEKDLVQQ--------------------KDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 932
Cdd:COG1196 521 GLAGAVAVligveaayeaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 933 LQSREHQLQDLLQNHLPALLEEKQRVLDALDS-GVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVA 1011
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1012 RQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEM 1091
Cdd:COG1196 681 LEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
490
....*....|....*.
gi 1907135707 1092 DPARLEHEIHQLKQKI 1107
Cdd:COG1196 761 DLEELERELERLEREI 776
|
|
| FHA_AFDN |
cd22711 |
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ... |
487-588 |
2.89e-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: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 487 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--REDASTEQDIVLHGLDLESEHCVFENAGGTVTLIPLRG-SQCSV 558
Cdd:cd22711 1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76
|
90 100 110
....*....|....*....|....*....|
gi 1907135707 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 |
4.66e-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: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 64 KSKTTITNLKIPEGGTGDSG-RERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTdVVKSAFEGYNACVFAYGQTGSGk 142
Cdd:pfam16796 30 PELLSEAQIDYPDETSSDGKiGSKNKSFSFDRVFPPESE-------QEDVFQEISQ-LVQSCLDGYNVCIFAYGQTGSG- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135707 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 |
9.32e-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: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 490 LIGIDDDLLSTGIILYHLKeGQTYVGredASTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 568
Cdd:cd22729 4 LVNLNADPALNELLVYYLK-DHTRVG---ADTSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79
|
90 100 110
....*....|....*....|....*....|
gi 1907135707 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 |
2.54e-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: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 490 LIGIDDDLLSTGIILYHLKEgQTYVGREDAsteQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQCSVNGVQIVDATQ 568
Cdd:cd22730 4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79
|
90 100
....*....|....*....|
gi 1907135707 569 LNQGAVILLGRTNMFRFNHP 588
Cdd:cd22730 80 LHHGDRILWGNNHFFRINLP 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
644-1090 |
9.65e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 644 ESKRKLIEE----MEEKQKSDKAE--LERMQQEVEtrrkETEIVQRQIRKQEESLKR-----RSFH-IENKLKDLLAEKE 711
Cdd:COG1196 155 EERRAIIEEaagiSKYKERKEEAErkLEATEENLE----RLEDILGELERQLEPLERqaekaERYReLKEELKELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 712 RFEEERLREQQGLEQQRRQEEESlfRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeeekeQ 791
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEA--ELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---------------L 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 792 VQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLA 871
Cdd:COG1196 294 LAELARLEQDIARLEE--------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 872 SLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQnhlpaL 951
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEA-------------------------LRAAAELAAQLEELEEAEEALLE-----R 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 952 LEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQ 1031
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135707 1032 QREALEQAVAKLEQRRSALQRcstldleiqeQRQKLGSLHTSEWSGWQASLETDGEALE 1090
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLL----------AGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
634-1107 |
1.27e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSfhIENKLKDLLAEKERF 713
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 714 EEERLREQQgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIF-QELDRLHQEQNAQSAKLRLEKrrleeeekeqv 792
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQ----------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREAL------LQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 866
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALlglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 867 LVKLASLEKDLVQQKDLLSKEVQEEkvalehvkCDAGGDPSFLATDDgnILGGPPDLDKIKTAETRLQSREHQLQdllqn 946
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEEL--------LAALGLPPDLSPEE--LLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 947 hLPALLEEKQRVLDALDSGvlgldttlcqvekevgekeeQIAQYQANASQLQQLRatfEFTANVARQEEKVRRKEKEILE 1026
Cdd:COG4717 365 -LEELEQEIAALLAEAGVE--------------------DEEELRAALEQAEEYQ---ELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1027 SQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSewsgwQASLETDGEAlemdpARLEHEIHQLKQK 1106
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEE------ELEELREELAELEAE-----LEQLEEDGEL-----AELLQELEELKAE 484
|
.
gi 1907135707 1107 I 1107
Cdd:COG4717 485 L 485
|
|
| Kinesin_assoc |
pfam16183 |
Kinesin-associated; |
398-510 |
1.83e-11 |
|
Kinesin-associated;
Pssm-ID: 465047 [Multi-domain] Cd Length: 177 Bit Score: 64.86 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 398 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 428
Cdd:pfam16183 3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 429 ---LLDSPTALSMEEKLHQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 496
Cdd:pfam16183 83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162
|
170
....*....|....
gi 1907135707 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 ... |
631-1109 |
5.22e-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: 68.07 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF 697
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 698 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLH---------- 767
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqqqkttlt 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 768 -QEQNAQSAKLRLEKRRLEEEEKEQVQRV-----AHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMr 841
Cdd:TIGR00618 393 qKLQSLCKELDILQREQATIDTRTSAFRDlqgqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 842 aggdhtcRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGP- 920
Cdd:TIGR00618 472 -------EQQLQTKEQIHLQETRKKAVVLARLLE-LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETs 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 921 -PDLDKIKTAET-RLQSREHQLQDLLQN-------------HLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVG---- 981
Cdd:TIGR00618 544 eEDVYHQLTSERkQRASLKEQMQEIQQSfsiltqcdnrskeDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRklqp 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 982 -EKEEQIAQYQANASQ-LQQLRATFEFTA-NVARQEEKVRRKEKEILESQEKQQREALEQAV-AKLEQRRSALQRCSTLD 1057
Cdd:TIGR00618 624 eQDLQDVRLHLQQCSQeLALKLTALHALQlTLTQERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQ 703
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135707 1058 LEIQEQRQKLGSL--HTSEWSGWQASLETDGEALEMDPARLEHEI-HQLKQKICE 1109
Cdd:TIGR00618 704 TLLRELETHIEEYdrEFNEIENASSSLGSDLAAREDALNQSLKELmHQARTVLKA 758
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
626-896 |
5.88e-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: 67.84 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 626 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSFHIENKlkd 705
Cdd:pfam17380 260 YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMDRQ--- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 706 llaekerfeEERLREQQGLEQQRRQEEEslfRIREELRK--LQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrr 783
Cdd:pfam17380 333 ---------AAIYAEQERMAMERERELE---RIRQEERKreLERIRQEEIAMEISRMRELERLQMERQQKN--------- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 784 leeeekeqvQRVAHLEEQLRKRQdtaplLCPGEAQRA-QEEKRELESIREALLQAK--EMRAGGDHTCRdELERAQQYFL 860
Cdd:pfam17380 392 ---------ERVRQELEAARKVK-----ILEEERQRKiQQQKVEMEQIRAEQEEARqrEVRRLEEERAR-EMERVRLEEQ 456
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907135707 861 EfKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALE 896
Cdd:pfam17380 457 E-RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
635-1045 |
1.08e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 635 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENkLKDLLAEK 710
Cdd:TIGR02168 674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 711 ERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleeEEKE 790
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-----------EAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 791 QVQRVAHLEEQLRkrqdtaplLCPGEAQRAQEEKRELESIREALlqAKEMRAGGdhTCRDELERAQQYFLEFKRRQLVKL 870
Cdd:TIGR02168 822 LRERLESLERRIA--------ATERRLEDLEEQIEELSEDIESL--AAEIEELE--ELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 871 ASLEKDLvQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPA 950
Cdd:TIGR02168 890 ALLRSEL-EELSEELRELESKRSELRR------------------------ELEELREKLAQLELRLEGLEVRIDNLQER 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 951 LLEEKQRVLDALDSGVLGLDTtlcqvekevgekeeQIAQYQANASQLQQ---------LRATFEFtanvarQEEKVRRKE 1021
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIED--------------DEEEARRRLKRLENkikelgpvnLAAIEEY------EELKERYDF 1004
|
410 420
....*....|....*....|....
gi 1907135707 1022 KEilesqekQQREALEQAVAKLEQ 1045
Cdd:TIGR02168 1005 LT-------AQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
646-1052 |
2.47e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 646 KRKLIEEM-------EEKQKSdKAELErmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEEERL 718
Cdd:TIGR02169 155 RRKIIDEIagvaefdRKKEKA-LEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 719 REQ-QGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKEQVQ-RVA 796
Cdd:TIGR02169 229 LKEkEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQLRVKeKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 797 HLEEQLRKRQDTAPLlCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVKLASLEKD 876
Cdd:TIGR02169 298 ELEAEIASLERSIAE-KERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 877 LVQQKDLLSKEVQEEkvalehvkcdaggDPSFLATddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhLPALLEEKQ 956
Cdd:TIGR02169 362 LKEELEDLRAELEEV-------------DKEFAET-----------RDELKDYREKLEKLKREINELKRE-LDRLQEELQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 957 RvldaldsgvlgldttlcqvekevgeKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE--SQEKQQR 1033
Cdd:TIGR02169 417 R-------------------------LSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAAdlSKYEQEL 471
|
410
....*....|....*....
gi 1907135707 1034 EALEQAVAKLEQRRSALQR 1052
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQR 490
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
633-899 |
5.11e-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: 64.76 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKR------KLIEEME----------------EKQKSDKAELERMQQEvetRRKETEIVQRQIRKQE- 689
Cdd:pfam17380 286 ERQQQEKFEKMEQERlrqekeEKAREVErrrkleeaekarqaemDRQAAIYAEQERMAME---RERELERIRQEERKREl 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 690 ESLKRRSFHIE-NKLKDLlaekerfeeerlreqQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQIFQELDRLHQ 768
Cdd:pfam17380 363 ERIRQEEIAMEiSRMREL---------------ERLQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 769 EQNAQSAKLRLEKRRLEEEEKEQVQRVaHLEEQlrKRQDTAPLLCPGEAQRaQEEKRELESIREALLQAKEMRAggdHTC 848
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERV-RLEEQ--ERQQQVERLRQQEEER-KRKKLELEKEKRDRKRAEEQRR---KIL 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907135707 849 RDELERAQQYFLEFKRRQLVklasLEKDLVQQKDLLSKEVQEEKVALEHVK 899
Cdd:pfam17380 498 EKELEERKQAMIEEERKRKL----LEKEMEERQKAIYEEERRREAEEERRK 544
|
|
| FHA |
cd00060 |
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ... |
489-585 |
6.87e-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: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 489 HLIGIDDDllsTGIILYHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQC--SVNGVQIVDA 566
Cdd:cd00060 1 RLIVLDGD---GGGREFPLTKGVVTIGR---SPDCDIVLDDPSVSRRHARIEVDGGGVYLEDL-GSTNgtFVNGKRITPP 73
|
90
....*....|....*....
gi 1907135707 567 TQLNQGAVILLGRTNmFRF 585
Cdd:cd00060 74 VPLQDGDVIRLGDTT-FRF 91
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
631-1111 |
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 1907135707 631 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEK 710
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 711 ERFEEERLREQQGLEQQRRQEEEslfrIREELRKLQELNSHEQAEKVQIFQ---ELDRLHQEQNAQSAKLRLEKRRLEEE 787
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 788 EKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhTCRDELERAQQYFLEFkRRQL 867
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-------ELREELEEAEQALDAA-EREL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 868 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDP---SFLATDDG------NILGGppDLDKI--KTAETRLQSR 936
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlsELISVDEGyeaaieAALGG--RLQAVvvENLNAAKKAI 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 937 EHQLQD--------LLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEK------EEQIAQYQANAsqLQQLRA 1002
Cdd:TIGR02168 563 AFLKQNelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllgGVLVVDDLDNA--LELAKK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1003 TFEFTANVARQEEKVRR-----------------KEKEILESQEKQQR-----EALEQAVAKLEQRRSALQ-RCSTLDLE 1059
Cdd:TIGR02168 641 LRPGYRIVTLDGDLVRPggvitggsaktnssileRRREIEELEEKIEEleekiAELEKALAELRKELEELEeELEQLRKE 720
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 1060 IQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKICEVD 1111
Cdd:TIGR02168 721 LEELSRQISALRKD-----LARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-1107 |
3.49e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQREEL--------EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQR---QIRKQEESLKRRSFH 698
Cdd:TIGR02168 325 LEELESKLDELaeelaeleEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIER 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 699 IENKLKDLLAEKERFEEERLREQQGLEQQRRQE-EESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 777
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 778 RLEKrrleeeekeqvQRVAHLEEQLRKRQDtapllcPGEAQRAQEEKR-----------ELESIREALLQAKEMRAGG-- 844
Cdd:TIGR02168 485 AQLQ-----------ARLDSLERLQENLEG------FSEGVKALLKNQsglsgilgvlsELISVDEGYEAAIEAALGGrl 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 845 DHTCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEK-------VALEHVKCDAGGDPSF--------- 908
Cdd:TIGR02168 548 QAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgVAKDLVKFDPKLRKALsyllggvlv 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 909 -------------------LATDDGNIL-------GGPPDLD--------KIKTAETRLQSREHQLQDLLQNhlpalLEE 954
Cdd:TIGR02168 628 vddldnalelakklrpgyrIVTLDGDLVrpggvitGGSAKTNssilerrrEIEELEEKIEELEEKIAELEKA-----LAE 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 955 KQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQRE 1034
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135707 1035 ALEQAVAKLEQrrsALQRCSTLDLEIQEQRQKLGSLHTSewsgwQASLETDGEALEMDPARLEHEIHQLKQKI 1107
Cdd:TIGR02168 783 EIEELEAQIEQ---LKEELKALREALDELRAELTLLNEE-----AANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
589-1066 |
1.21e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 589 KEAAKLR---EKRKSGllssfslsmtDLSKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEM----EEKQKSD- 660
Cdd:PTZ00121 1366 AEAAEKKkeeAKKKAD----------AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAkkkaEEKKKADe 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 661 ---KAELERMQQEVETRRKETEIVQRQIRKQEEslKRRSFHIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEEslfR 737
Cdd:PTZ00121 1436 akkKAEEAKKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK---K 1510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 738 IREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEeeekeQVQRVAHLEEQLRKRQDTAPLLCPGEA 817
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-----KAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 818 QRAQEEKReLESIREALLQAKEMRAggdhtcrDELERAQQyflEFKRRQLVKLASLEKDLVQQkdlLSKEVQEEKVALEH 897
Cdd:PTZ00121 1586 AKKAEEAR-IEEVMKLYEEEKKMKA-------EEAKKAEE---AKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEE 1651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 898 VKCDAggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQdllQNHLPALLEEKQRVLDALdsgvlgldttlcQVE 977
Cdd:PTZ00121 1652 LKKAE-------------------EENKIKAAEEAKKAEEDKKK---AEEAKKAEEDEKKAAEAL------------KKE 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 978 KEVGEKEEQIAQYQAN-ASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQRCSTL 1056
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
490
....*....|
gi 1907135707 1057 DLEIQEQRQK 1066
Cdd:PTZ00121 1778 EAVIEEELDE 1787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
631-1052 |
1.42e-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: 60.08 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIvqrQIRKQEeslkRRSFHIENKLKDLlaek 710
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAL---LKEKRE----YEGYELLKEKEAL---- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 711 erfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrleEEEKE 790
Cdd:TIGR02169 236 --------------ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------EEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 791 QVQ-RVAHLEEQLRKRQDTAPlLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAqqyfLEFKRRQLVK 869
Cdd:TIGR02169 291 RVKeKIGELEAEIASLERSIA-EKERELEDAEERLAKLEAEIDKLLAEIE-----------ELERE----IEEERKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 870 LASLEKDLVQQKDLLSKEVQEEkvalehvkcdaggDPSFLATddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhLP 949
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEV-------------DKEFAET-----------RDELKDYREKLEKLKREINELKRE-LD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 950 ALLEEKQRV----------LDALDSGVLGLDTTLcqvekevGEKEEQIAQYQANASQLQQLRATFEftANVARQEEKVRR 1019
Cdd:TIGR02169 410 RLQEELQRLseeladlnaaIAGIEAKINELEEEK-------EDKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDR 480
|
410 420 430
....*....|....*....|....*....|...
gi 1907135707 1020 KEKEILESQEKqqrealeqaVAKLEQRRSALQR 1052
Cdd:TIGR02169 481 VEKELSKLQRE---------LAEAEAQARASEE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
636-1047 |
1.44e-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: 60.08 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 636 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKERFEE 715
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGL-------KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 716 ERLREQQGLEQQRRQEEESLFRIREELRKLQE--------LNSHEQAEKVQIFQELDRLHQEQNAQSAklrlekrrleee 787
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleeaLNDLEARLSHSRIPEIQAELSKLEEEVS------------ 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 788 ekEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELErAQQYFLEFKRRQL 867
Cdd:TIGR02169 809 --RIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQRIDLKEQIKSI-------EKEIE-NLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 868 VKLASLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsflatddgnilggppdlDKIKTAETRLQSREHQLQDlLQNH 947
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELE------------------------RKIEELEAQIEKKRKRLSE-LKAK 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 948 LPALLEEKQRVLDALDSGVlgldttlcqvekEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILE 1026
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDE------------EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEyEEVLKRLDELKE 993
|
410 420
....*....|....*....|...
gi 1907135707 1027 SQEK--QQREALEQAVAKLEQRR 1047
Cdd:TIGR02169 994 KRAKleEERKAILERIEEYEKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
633-1046 |
1.44e-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: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 712
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 713 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQ------ELDRLHQEQNAQSAKLRLEKRRLEE 786
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEleeeeeALLELLAELLEEAALLEAALAELLE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 787 EEKEQVQRVAHLEEQLRKRQ------------DTAPLLCPGEAQRAQEEKRELESIREALLqakemrAGGDHTCRDELER 854
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEgflegvkaalllAGLRGLAGAVAVLIGVEAAYEAALEAALA------AALQNIVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 855 AQQYFLEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKV--ALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR 932
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgaAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 933 LQSREHQLQDL--------------------LQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQA 992
Cdd:COG1196 639 AVTLAGRLREVtlegeggsaggsltggsrreLLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 993 NASQLQQLRATFEFT--------------------------ANVARQEEKVRRKEKEI-------------LESQE---- 1029
Cdd:COG1196 719 EELEEEALEEQLEAEreelleelleeeelleeealeelpepPDLEELERELERLEREIealgpvnllaieeYEELEeryd 798
|
490
....*....|....*....
gi 1907135707 1030 --KQQREALEQAVAKLEQR 1046
Cdd:COG1196 799 flSEQREDLEEARETLEEA 817
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
614-857 |
2.49e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.81 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 614 SKSCENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETRRKETEivqRQIRKQEESLK 693
Cdd:pfam15709 295 GRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 694 RrsfhiENKLKDLLAEKERFEEERLR-EQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNA 772
Cdd:pfam15709 370 R-----AEKMREELELEQQRRFEEIRlRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 773 QSAKLRLekrrleeeekeqvQRVAHLEEQLRKRQDTapLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDEL 852
Cdd:pfam15709 445 ERAEAEK-------------QRQKELEMQLAEEQKR--LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLAL 509
|
....*
gi 1907135707 853 ERAQQ 857
Cdd:pfam15709 510 EEAMK 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
638-1106 |
2.91e-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: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 638 EELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDL------LAEKE 711
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 712 RFEEERLREQQGLEQQRRQEEE--SLFRIREELRKLQELNSH------EQAEKVQIFQELDRLHQEQNAQSAK------- 776
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKaaplaaHIKAVTQIEQQAQRIHTELQSKMRSrakllmk 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 777 -LRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEK---RELESIREALLQAKEMRAGGDHTCRDel 852
Cdd:TIGR00618 330 rAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhiHTLQQQKTTLTQKLQSLCKELDILQR-- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 853 ERAQQYFLEFKRRQL-VKLASLEKDLV-QQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGppDLDKIKTAE 930
Cdd:TIGR00618 408 EQATIDTRTSAFRDLqGQLAHAKKQQElQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ--TKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 931 TRLQSREHQLQDLLQNhLPALLEEKQRVLDA--LDSGVLGLDTTLCQVEKEVGEKEEQ-IAQYQANASQLQQLRATFEFT 1007
Cdd:TIGR00618 486 TRKKAVVLARLLELQE-EPCPLCGSCIHPNParQDIDNPGPLTRRMQRGEQTYAQLETsEEDVYHQLTSERKQRASLKEQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1008 ANVARQEEKV----RRKEKEILE--SQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLgSLHTSEWSGWQAS 1081
Cdd:TIGR00618 565 MQEIQQSFSIltqcDNRSKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV-RLHLQQCSQELAL 643
|
490 500
....*....|....*....|....*
gi 1907135707 1082 LETDGEALEMDPARLEHEIHQLKQK 1106
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIR 668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
631-850 |
4.00e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtrrkETEIVQRQIRKQEESLKRRSFHIENKlkdllaek 710
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----ENKIKAAEEAKKAEEDKKKAEEAKKA-------- 1683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 711 erfeeerlreqqglEQQRRQEEESLFRIREELRKLQELNSHE-----QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLE 785
Cdd:PTZ00121 1684 --------------EEDEKKAAEALKKEAEEAKKAEELKKKEaeekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907135707 786 EEEKEQVQRVAHLEEQlrkrqdtapllcpgEAQRAQEEKRELESIREALLQAKE--MRAGGDHTCRD 850
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKE--------------EEKKAEEIRKEKEAVIEEELDEEDekRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-1066 |
4.42e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETRRKETEivqrQIRKQEESLKRRSfhiENKLK-DLLAE 709
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAAdeAEAAEEKAEAAEKKKEEAKKKADAAKKKAE----EKKKADEAKKKAE---EDKKKaDELKK 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 710 KERFEEERLREQQGLEQQRRQEEesLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE-QNAQSAKLRLEKRRLEEEE 788
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAK--KKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 789 KEQVQRVAHLEEQLRKRQDTAPllcPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELERAQqyflEFKRRQ 866
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAE----ELKKAE 1561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 867 LVKLASLEKDLVQQKDLLSKEVQE----EKVALEHVKCDAGGDPSFLATDdgnilGGPPDLDKIKTAETRLQSREHQLQD 942
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEakkaEEARIEEVMKLYEEEKKMKAEE-----AKKAEEAKIKAEELKKAEEEKKKVE 1636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 943 LLQNHLpallEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEK 1022
Cdd:PTZ00121 1637 QLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907135707 1023 EILESQEkQQREALEQAVAKLEQ--RRSALQRCSTLDLEIQEQRQK 1066
Cdd:PTZ00121 1713 EEKKKAE-ELKKAEEENKIKAEEakKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
793-1107 |
5.42e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA---QQYFLEFKRRQLVK 869
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 870 LASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsfLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLP 949
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAE-----------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 950 ALLEEKQRVLDALDSgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQE 1029
Cdd:TIGR02168 825 RLESLERRIAATERR---------------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1030 KQQREALEQAVAKL---EQRRSALQR--------CSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGE---ALEMDPAR 1095
Cdd:TIGR02168 890 ALLRSELEELSEELrelESKRSELRReleelrekLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAlenKIEDDEEE 969
|
330
....*....|..
gi 1907135707 1096 LEHEIHQLKQKI 1107
Cdd:TIGR02168 970 ARRRLKRLENKI 981
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
630-842 |
5.73e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQREEL--EKLESKRKLIEEMEEKQKSDKAELERMQQeveTRRKETEIVQRQIRKQEESLKRRSFHIENKlkdll 707
Cdd:pfam17380 383 LQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQREVRRLEEERAREMERVRLE----- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 708 aekerfeeeRLREQQGLEQQRRQEEEslfRIREELRKLQELNSHEQAEKVQ---IFQELdrlhqEQNAQSAKLRLEKRRL 784
Cdd:pfam17380 455 ---------EQERQQQVERLRQQEEE---RKRKKLELEKEKRDRKRAEEQRrkiLEKEL-----EERKQAMIEEERKRKL 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135707 785 EEEEKEQVQRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKEMRA 842
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAE---------EERRKQQEMEERRRIQEQMRKATEERS 566
|
|
| FHA_RADIL-like |
cd22712 |
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ... |
485-588 |
6.73e-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: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 485 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGREDASTEQ-DIVLHGLDLESEHCV-----------FENAGGT-- 545
Cdd:cd22712 1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907135707 546 --VTLIPLRGSQCSVNGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22712 76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
589-1106 |
1.21e-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: 57.29 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 589 KEAAKLREKRKSGLLSSFSLSMTDLSKSCENLSAVM--LYNPGLEFERQQREEL----EKLESKRKLIEEMEEKQK---- 658
Cdd:pfam02463 207 KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLqeLLRDEQEEIESSKQEIekeeEKLAQVLKENKEEEKEKKlqee 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 659 ----------SDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFEEERLREQQgLEQQR 728
Cdd:pfam02463 287 elkllakeeeELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 729 RQEEESLFRIREELRKLQELNSHEQAEKVQifQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDT 808
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEE--ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 809 APLLCPGEA---QRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK-LASLEKDLVQQKDLL 884
Cdd:pfam02463 444 GKLTEEKEElekQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSgLKVLLALIKDGVGGR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 885 SKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETR-----LQSREHQLQDLLQNHLPALLEEKQRVL 959
Cdd:pfam02463 524 IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgARKLRLLIPKLKLPLKSIAVLEIDPIL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 960 DALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQ-------ANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQ 1032
Cdd:pfam02463 604 NLAQLDKATLEADEDDKRAKVVEGILKDTELTklkesakAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE 683
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135707 1033 REalEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEwsgwQASLETDGEALEMDPARLEHEIHQLKQK 1106
Cdd:pfam02463 684 KA--ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL----ADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
634-1051 |
1.61e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 713
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 714 EEERLREQQGLEQQRRQEEESLFRIREELRKL-QELNSHE-QAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQ 791
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELeEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 792 --------VQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFK 863
Cdd:COG4717 274 tiagvlflVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 864 RRQLVKLASLEKDLVQQkdllskEVQEEKVALEHvKCDAGGDPSFLAtddgnilggppdLDKIKTAETRLQSREHQLQDL 943
Cdd:COG4717 350 QELLREAEELEEELQLE------ELEQEIAALLA-EAGVEDEEELRA------------ALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 944 LQNHLPALLEEkqrvLDALDSGVLgldttlcqvekevgekEEQIAQYQANASQLQQLRAtfEFTANVARQEEKVRRKEKE 1023
Cdd:COG4717 411 LEELLGELEEL----LEALDEEEL----------------EEELEELEEELEELEEELE--ELREELAELEAELEQLEED 468
|
410 420
....*....|....*....|....*...
gi 1907135707 1024 ILESQEKQQREALEQAVAKLEQRRSALQ 1051
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
629-1070 |
1.63e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 629 GLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQI----RKQEE------SLKRRSF 697
Cdd:PRK02224 210 GLESELAElDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaeteREREElaeevrDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 698 HIENKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNshEQAEKVQifqeldrlhqeqnaqsakl 777
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN--EEAESLR------------------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 778 rlekrrleeeekeqvQRVAHLEEQLRKRQDTAPLLcPGEAQRAQEEKRELESIREAL---LQAKEMRAGGDHTCRDELER 854
Cdd:PRK02224 349 ---------------EDADDLEERAEELREEAAEL-ESELEEAREAVEDRREEIEELeeeIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 855 AQQYFLEFKRRQLVKLASLEKDLVQQKDllskEVQEEKVALEHVKCDAGGDPsflatddgniLGGPPDLDKIKTAETRLQ 934
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARE----RVEEAEALLEAGKCPECGQP----------VEGSPHVETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 935 SREHQLQDLLQNHlpALLEEKqrvLDALDSGVlgldttlcqvekevgEKEEQIAQYQANASQLQQLRATFEFTANVARQE 1014
Cdd:PRK02224 479 ELEAELEDLEEEV--EEVEER---LERAEDLV---------------EAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907135707 1015 EKVRRKEKEILESQEKQQREA-----------------LEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1070
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAaaeaeeeaeeareevaeLNSKLAELKERIESLERIRTLLAAIADAEDEIERL 611
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
630-826 |
1.75e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.11 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetRRKEtEIVQRQIRKQEESLKRRSFHIENKLKDLLAE 709
Cdd:pfam15709 348 LEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ----RRFE-EIRLRKQRLEEERQRQEEEERKQRLQLQAAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 710 KERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSH--EQAEKVQIFQELDRLHQEQNAQSAKLrlekrrleee 787
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQlaEEQKRLMEMAEEERLEYQRQKQEAEE---------- 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907135707 788 ekeqvQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRE 826
Cdd:pfam15709 489 -----KARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
642-1030 |
3.06e-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: 55.83 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 642 KLESKRKLIEE----MEEKQKSDKAE--LERMQQEVEtrrkETEIVQRQIRKQEESLKRRS-----FH-IENKLKDL-LA 708
Cdd:TIGR02168 153 KPEERRAIFEEaagiSKYKERRKETErkLERTRENLD----RLEDILNELERQLKSLERQAekaerYKeLKAELRELeLA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 709 EKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEeee 788
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 789 kEQVQRVAHLEEQLRKRQDTAPLLcpgeAQRAQEEKRELESIREALLQAKEMRAGgdhtCRDELERAQQYFLEFKRR--- 865
Cdd:TIGR02168 306 -ILRERLANLERQLEELEAQLEEL----ESKLDELAEELAELEEKLEELKEELES----LEAELEELEAELEELESRlee 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 866 ---QLVKLASLEKDLVQQKDLLSKEVQEEKVALEHvkcdaggdpsflatddgnilggppdldkiktAETRLQSREHQLQD 942
Cdd:TIGR02168 377 leeQLETLRSKVAQLELQIASLNNEIERLEARLER-------------------------------LEDRRERLQQEIEE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 943 LLQNHLPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQ----YQANASQLQQLRATFEFTANVARQEEKVR 1018
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEaeqaLDAAERELAQLQARLDSLERLQENLEGFS 505
|
410
....*....|..
gi 1907135707 1019 RKEKEILESQEK 1030
Cdd:TIGR02168 506 EGVKALLKNQSG 517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
570-1106 |
3.16e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 570 NQGAVILLGRTNMFRFNHPKEAAKLREKRKSGllssfslsmtDLSKSCENLSAVmlynpglefERQQREELEKLESKRKL 649
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKAD----------ELKKAEEKKKAD---------EAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 650 IEEM-----------EEKQKSD--KAELERMQQEVETRRKETEIVQRQIRKQE---ESLKRRSFHIENKLKDLLAEKERF 713
Cdd:PTZ00121 1311 AEEAkkadeakkkaeEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEekaEAAEKKKEEAKKKADAAKKKAEEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 714 EEERLREQQGLEQQRRQEE-----------ESLFRIREELRKLQELNshEQAEKVQIFQELDRLHQE-QNAQSAKLRLEK 781
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADElkkaaaakkkaDEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEaKKAEEAKKKAEE 1468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 782 RRLEEEEKEQVQRVAHLEEQLRKRQDTAPLlcPGEAQRAQEEKRELESIREA--LLQAKEMRAGGDHTCRDELERAQqyf 859
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAKKAeeAKKADEAKKAEEAKKADEAKKAE--- 1543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 860 lEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflATDDGNILGGPPDLDKIKTAETRLQSREHQ 939
Cdd:PTZ00121 1544 -EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 940 LQDLLQNHlpalLEEKQRVldaldsgvlgldttlcQVEKEVGEKEEQIAQYQANASQLQQLRAtfeftANVARQEEKVRR 1019
Cdd:PTZ00121 1621 KAEELKKA----EEEKKKV----------------EQLKKKEAEEKKKAEELKKAEEENKIKA-----AEEAKKAEEDKK 1675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1020 KEKEiLESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMDPARLEHE 1099
Cdd:PTZ00121 1676 KAEE-AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
570
....*....|.
gi 1907135707 1100 ----IHQLKQK 1106
Cdd:PTZ00121 1755 ekkkIAHLKKE 1765
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
633-1107 |
3.54e-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: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETeiVQRQIRKQEESLKRRsfhiENKLKDLLAEKER 712
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--LEREIERLERELEER----ERRRARLEALLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 713 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRleeeekeQV 792
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR-------LL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQDTAPLLC------PGEAQ--------------------------------------------RAQE 822
Cdd:COG4913 444 ALRDALAEALGLDEAELPFVGelievrPEEERwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyervRTGL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 823 EKRELESIREALLQAK--------------EMRAGGDHTC---RDELER--------------------------AQQYF 859
Cdd:COG4913 524 PDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdsPEELRRhpraitragqvkgngtrhekddrrriRSRYV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 860 LEFKRRQlvKLASLEKDLVQQKDLLSkEVQEEKVALEhvkcDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQ 939
Cdd:COG4913 604 LGFDNRA--KLAALEAELAELEEELA-EAEERLEALE----AELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 940 LQDLLQNhlPALLEEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRR 1019
Cdd:COG4913 677 LERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1020 KEKEILESQEKQQREALEQAVAKLEQRRSALQRcstldlEIQEQRQKLGSLHTSEWSGWQASLETDGEALEMdPARLEHE 1099
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEE------ELERAMRAFNREWPAETADLDADLESLPEYLAL-LDRLEED 827
|
....*....
gi 1907135707 1100 -IHQLKQKI 1107
Cdd:COG4913 828 gLPEYEERF 836
|
|
| FHA |
COG1716 |
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms]; |
505-585 |
4.61e-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: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 505 YHLKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFENAGGTVTLIPLrGSQ--CSVNGVQIVDATQLNQGAVILLGRTnM 582
Cdd:COG1716 16 FPLDGGPLTIGR---APDNDIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90
|
...
gi 1907135707 583 FRF 585
Cdd:COG1716 91 LRF 93
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
633-946 |
5.17e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEnKLKDLLAEKER 712
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA-QAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 713 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEeekeqv 792
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEkRELESIREALLQAKEMRAGGDHTcRDELERAQQYFLEFKRRQLVKLAS 872
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLP-RELAEELLEAKDSLEAKLGLALS-ALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135707 873 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQN 946
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
637-1170 |
1.21e-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: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 637 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSF---HIENKLKDLLAEKERF 713
Cdd:TIGR02169 363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEelaDLNAAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 714 EEERLREQQGLEQQRRQ----------EEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRR 783
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKleqlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 784 L-----EEEEKEQV--QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDH---------- 846
Cdd:TIGR02169 520 IqgvhgTVAQLGSVgeRYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDlsilsedgvi 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 847 -------TCRDELERAQQYF---------LEFKRRQL--VKLASLEKDLVQQ-------------KDLLSKEVQEEKVAL 895
Cdd:TIGR02169 600 gfavdlvEFDPKYEPAFKYVfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRL 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 896 EHVKCDAGGDPSFLATDDGNILGGPPDL-DKIKTAETRLQSREHQLQDLLQNH--LPALLEEKQRVLDALDSGVLGLDTT 972
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEekLKERLEELEEDLSSLEQEIENVKSE 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 973 LCQVEKEVGEKEEQIAQYQA---------NASQLQQLRATFEFT-ANVARQEEKVRRKEKEIleSQEKQQREALEQAVAK 1042
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEalndlearlSHSRIPEIQAELSKLeEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQE 837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1043 LEQRRSALQ-RCSTLDLEIQEQRQKLGSLHT--SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKICEVDG-VQRPHH 1118
Cdd:TIGR02169 838 LQEQRIDLKeQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAqIEKKRK 917
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135707 1119 GILEGQAVLSSL---------PPSGGNSHLAPLMDARISAYIEEEVQRRLhdlhRAIGDAN 1170
Cdd:TIGR02169 918 RLSELKAKLEALeeelseiedPKGEDEEIPEEELSLEDVQAELQRVEEEI----RALEPVN 974
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
634-1107 |
1.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLESKRKLI--EEMEEKQKsdkaELERMQQEVETRRKETEIVQrQIRKQEESLKRRSFHIENKLKDLLAEKE 711
Cdd:COG4717 52 EKEADELFKPQGRKPELnlKELKELEE----ELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 712 RFEEERLREQqgLEQQRRQEEESLFRIREELRKLQELnsheQAEKVQIFQELDRLHQEqnaqsaklrlekrrleeeekeq 791
Cdd:COG4717 127 LLPLYQELEA--LEAELAELPERLEELEERLEELREL----EEELEELEAELAELQEE---------------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 792 vqrvahLEEQLRKrqdtaplLCPGEAQRAQEEKRELESIREALLQAKEMRAggdhTCRDELERAQQyflefkrrqlvKLA 871
Cdd:COG4717 179 ------LEELLEQ-------LSLATEEELQDLAEELEELQQRLAELEEELE----EAQEELEELEE-----------ELE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 872 SLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILG------GPPDLDKIKTAETRLQSREHQLQDLLQ 945
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlGLLALLFLLLAREKASLGKEAEELQAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 946 NHLPALleEKQRVLDALDSgvLGLDTTLcqVEKEVGEKEEQIAQYQANASQLQQLRAtfeftanvARQEEKVRRKEKEIL 1025
Cdd:COG4717 311 PALEEL--EEEELEELLAA--LGLPPDL--SPEELLELLDRIEELQELLREAEELEE--------ELQLEELEQEIAALL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1026 ESQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQrqkLGSLHTSEWSGWQASLETDGEALEMDPARLEHEIHQLKQ 1105
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL---LGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
..
gi 1907135707 1106 KI 1107
Cdd:COG4717 454 EL 455
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
637-1170 |
1.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 637 REELEKLESKRKLIEEMEE------KQKSDKAELERMQQ--EVETRRKETEIVQRQIRKQEESLKRrsfhienkLKDLLA 708
Cdd:COG4913 241 HEALEDAREQIELLEPIRElaeryaAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELAR--------LEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 709 EKERFEEERLREQQGLEQQRRQEE-ESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEE 787
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLER----ELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 788 EKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAqqyfLEFKRRQ- 866
Cdd:COG4913 389 AAALLEALEEELEALEEALAEA----EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA----LGLDEAEl 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 867 -----LVKLASLEKD----------------LVQQKDLlsKEVQE--------EKVALEHVKcDAGGDPSFLATDDGNIL 917
Cdd:COG4913 461 pfvgeLIEVRPEEERwrgaiervlggfaltlLVPPEHY--AAALRwvnrlhlrGRLVYERVR-TGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 918 GgppdldKIKTAETRLQSRehqLQDLLQNHLPALLEEKQRVLDALDSGVlgldTTLCQVEKEVGEKEEQIAQYQANASQL 997
Cdd:COG4913 538 G------KLDFKPHPFRAW---LEAELGRRFDYVCVDSPEELRRHPRAI----TRAGQVKGNGTRHEKDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 998 QqlratFEFTANVARQEEKVRRKEKEILESQEkqQREALEQAVAKLEQRRSALQRCS----------TLDLEIQEQRQKL 1067
Cdd:COG4913 605 G-----FDNRAKLAALEAELAELEEELAEAEE--RLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1068 GSLHTSewSGWQASLETDGEALEMDPARLEHEIHQLKQKIcevDGVQRPHHGILEGQAVLSSL---PPSGGNSHLAPLMD 1144
Cdd:COG4913 678 ERLDAS--SDDLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRleaAEDLARLELRALLE 752
|
570 580
....*....|....*....|....*..
gi 1907135707 1145 ARISAYIEEEVQRRLHD-LHRAIGDAN 1170
Cdd:COG4913 753 ERFAAALGDAVERELREnLEERIDALR 779
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
633-1070 |
1.76e-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: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETR---------------RKETEIVQRQIRKQEES--LKRR 695
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEReqqlqtkeqihlqetRKKAVVLARLLELQEEPcpLCGS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 696 SFHIENKLKDLLaekerFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSA 775
Cdd:TIGR00618 510 CIHPNPARQDID-----NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 776 KLRLEKRRleeeekeqVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERA 855
Cdd:TIGR00618 585 DIPNLQNI--------TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 856 QQYflefKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQS 935
Cdd:TIGR00618 657 QER----VREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 936 REHQLQDLLQNHLPALLEEKQRVLDAL-------DSGVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRAtfefta 1008
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQARTVLKARteahfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEA------ 806
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 1009 nvaRQEEKVRRKEKEILESQEKQQREaLEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSL 1070
Cdd:TIGR00618 807 ---EIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
631-836 |
2.41e-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: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERM-------QQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKl 703
Cdd:pfam13868 170 EREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELraklyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELK- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 704 kdllaekerfeeerlreQQGLEQQRRQEEESLFRIREELRKLQELnshEQAEKVQIFQELDRLHQEQNAQsaklrlekrr 783
Cdd:pfam13868 249 -----------------ERRLAEEAEREEEEFERMLRKQAEDEEI---EQEEAEKRRMKRLEHRRELEKQ---------- 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907135707 784 leeEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQ 836
Cdd:pfam13868 299 ---IEEREEQRAAEREEELEEGER--------LREEEAERRERIEEERQKKLK 340
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
635-957 |
3.56e-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: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 635 QQREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERFE 714
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEE---EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 715 EERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQA-----EKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEK 789
Cdd:pfam02463 269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkvddeEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 790 EQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVK 869
Cdd:pfam02463 349 IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 870 lasLEKDLVQQKDLLSKEVQEEKVALEHVKcdaggdpsFLATDDGNILggppDLDKIKTAETRLQSREHQLQDLLQNHLP 949
Cdd:pfam02463 429 ---LEILEEEEESIELKQGKLTEEKEELEK--------QELKLLKDEL----ELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
....*...
gi 1907135707 950 ALLEEKQR 957
Cdd:pfam02463 494 KLEERSQK 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
620-892 |
4.36e-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: 51.30 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 620 LSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRrsfhI 699
Cdd:COG4942 6 LLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 700 ENKLKDLlaekerfeeerlreQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVqifqeldrLHQEQNAQSAKLRL 779
Cdd:COG4942 82 EAELAEL--------------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 780 EKRRLEEEEKEQVQRVAHLEEQLRKRQDTApllcPGEAQRAQEEKRELESIREALLQAKEMRaggdhtcRDELERAQQYF 859
Cdd:COG4942 140 YLKYLAPARREQAEELRADLAELAALRAEL----EAERAELEALLAELEEERAALEALKAER-------QKLLARLEKEL 208
|
250 260 270
....*....|....*....|....*....|...
gi 1907135707 860 LEfKRRQLVKLASLEKDLVQQKDLLSKEVQEEK 892
Cdd:COG4942 209 AE-LAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
646-759 |
4.52e-06 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 49.50 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 646 KRKLIEEMEEKQKSdKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEEERLREQQGLE 725
Cdd:pfam12072 52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEK----KEKELEAQQQQLE 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907135707 726 QQRRQEEEslfRIREELRKLQELN--SHEQAEKVQI 759
Cdd:pfam12072 124 EKEEELEE---LIEEQRQELERISglTSEEAKEILL 156
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
634-880 |
5.65e-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: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLESKRKL----------IEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENK 702
Cdd:pfam13868 2 RENSDELRELNSKLLAakcnkerdaqIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERkEERKRYRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 703 LKDLLAEKERFEEERLR-EQQGLEQQRRQEEESLFRIREELRK-----------LQELNSHEQAEKVQIFQELDRLHQ-- 768
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKqrqlreeidefNEEQAEWKELEKEEEREEDERILEyl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 769 -EQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLcpgEAQRAQEEKRELESIREALLQAKEMRAggdht 847
Cdd:pfam13868 162 kEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL---RAKLYQEEQERKERQKEREEAEKKARQ----- 233
|
250 260 270
....*....|....*....|....*....|...
gi 1907135707 848 cRDELERAQQYFLEFKRRQLVKLASLEKDLVQQ 880
Cdd:pfam13868 234 -RQELQQAREEQIELKERRLAEEAEREEEEFER 265
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
633-899 |
5.95e-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: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKER 712
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 713 feeerlrEQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIfqELDRLHQEQNAQSAKLRLEKRRLEEEEKEQV 792
Cdd:pfam13868 167 -------REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL--RAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREALLQAKE---MRAGGDHTCRDELERAQQYFLEFKRRQlvK 869
Cdd:pfam13868 238 QQAREEQIELKERR---------LAEEAEREEEEFERMLRKQAEDEEieqEEAEKRRMKRLEHRRELEKQIEEREEQ--R 306
|
250 260 270
....*....|....*....|....*....|
gi 1907135707 870 LASLEKDLvQQKDLLSKEVQEEKVALEHVK 899
Cdd:pfam13868 307 AAEREEEL-EEGERLREEEAERRERIEEER 335
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
816-1070 |
6.47e-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: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 816 EAQRAQEEKRELESIREALLQAKEmraggdhtCRDELERAQQYFLEFkRRQLVKLASLEkdlvQQKDLLSKEVQEEKVAL 895
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE--------QIELLEPIRELAERY-AAARERLAELE----YLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 896 EHVKCDAGGDpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALDSGVLGLDTTLcq 975
Cdd:COG4913 293 LEAELEELRA----------------ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLEREL-- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 976 vekevgekeeqiAQYQANASQLQQLRATFEFTANVARQE-EKVRRKEKEILEsQEKQQREALEQAVAKLEQRRSALQRcs 1054
Cdd:COG4913 355 ------------EERERRRARLEALLAALGLPLPASAEEfAALRAEAAALLE-ALEEELEALEEALAEAEAALRDLRR-- 419
|
250
....*....|....*.
gi 1907135707 1055 tldlEIQEQRQKLGSL 1070
Cdd:COG4913 420 ----ELRELEAEIASL 431
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
584-754 |
1.07e-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: 50.51 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 584 RFNHPKEAA---KLREKRKSGLLSSFSLSMTDLSKSCENLSAVMLY----NPGLEFERQQREELEKLESKRKLiEEMEEK 656
Cdd:pfam17380 393 RVRQELEAArkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeERAREMERVRLEEQERQQQVERL-RQQEEE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 657 QKSDKAELERMQQEvetrRKETEIVQRQIRKQE-ESLKRRSFHIENKLKDLLAEKERFEEERLREQQG--LEQQRR--QE 731
Cdd:pfam17380 472 RKRKKLELEKEKRD----RKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRreAEEERRkqQE 547
|
170 180
....*....|....*....|...
gi 1907135707 732 EESLFRIREELRKLQELNSHEQA 754
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEA 570
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
636-763 |
1.24e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 636 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerFEE 715
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK----KEK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907135707 716 ERLREQQGLEQQRRQEEEslfRIREELRKLQELN--SHEQAeKVQIFQEL 763
Cdd:PRK12704 118 ELEQKQQELEKKEEELEE---LIEEQLQELERISglTAEEA-KEILLEKV 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
809-1070 |
1.38e-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: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 809 APLLCPGEAQRAQEEKRELESIREALLQAKEmraggdhtcrdELERAQQyflefKRRQLVK-LASLEKDLVQQKDLLsKE 887
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEK-----------ELAALKK-----EEKALLKqLAALERRIAALARRI-RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 888 VQEEKVALEHvkcdaggdpsflatddgnilggppDLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSG- 965
Cdd:COG4942 74 LEQELAALEA------------------------ELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPe 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 966 -VLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRKEKEILESQEKQQREALEQAVAKLE 1044
Cdd:COG4942 130 dFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
250 260
....*....|....*....|....*.
gi 1907135707 1045 QRRSALQrcstldlEIQEQRQKLGSL 1070
Cdd:COG4942 210 ELAAELA-------ELQQEAEELEAL 228
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
633-755 |
2.41e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.19 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETRRKETEivqRQIRKQEESLKRRSFHIENKLKDllaeker 712
Cdd:pfam05672 28 EREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE---RRREEEERQRKAEEEAEEREQRE------- 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907135707 713 feeerlreQQGLEQQRRQEEESLFRIREEL-RKLQELNSHEQAE 755
Cdd:pfam05672 93 --------QEEQERLQKQKEEAEAKAREEAeRQRQEREKIMQQE 128
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
612-1110 |
2.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 612 DLSKSCENLSAVMLYnpgLEFERqqrEELEKLESKRkliEEMEEKQKSDKAELERMQQEVetrrKETEIVQRQIRKQEES 691
Cdd:PRK03918 159 DYENAYKNLGEVIKE---IKRRI---ERLEKFIKRT---ENIEELIKEKEKELEEVLREI----NEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 692 LKRRSFHIEnKLKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQEL--NSHEQAEKVQIFQELDRLHQE 769
Cdd:PRK03918 226 LEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 770 QNAQSAKLRlekrrleeeekeqvQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREAL--LQAKEMRAGGDHt 847
Cdd:PRK03918 305 YLDELREIE--------------KRLSRLEEEINGIEE--------RIKELEEKEERLEELKKKLkeLEKRLEELEERH- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 848 crDELERAQQyflefKRRQLVKLASLEKDLVQQKdlLSKEVQEEKVALEHVKcdaggdpsflatddgnilggpPDLDKIK 927
Cdd:PRK03918 362 --ELYEEAKA-----KKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIE---------------------EEISKIT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 928 TAETRLQSREHQLQDLLQNhlpalLEEKQRVldaldsgvlgldTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEft 1007
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEE-----LKKAKGK------------CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE-- 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1008 anvaRQEEKVRRKEKEiLESQEKQQREALEQAvAKLEQRRSALQRCSTLDLEIQEQ--------RQKLGSLhtsewSGWQ 1079
Cdd:PRK03918 473 ----EKERKLRKELRE-LEKVLKKESELIKLK-ELAEQLKELEEKLKKYNLEELEKkaeeyeklKEKLIKL-----KGEI 541
|
490 500 510
....*....|....*....|....*....|....
gi 1907135707 1080 ASLETD---GEALEMDPARLEHEIHQLKQKICEV 1110
Cdd:PRK03918 542 KSLKKElekLEELKKKLAELEKKLDELEEELAEL 575
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
628-867 |
3.76e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 628 PGLEFERQQREELEKLESKR-KLIEEMEEKQK---------SDKAELERMQQEVETR---RKETEIVQRQIRKQEESLKR 694
Cdd:pfam02029 56 GGLDEEEAFLDRTAKREERRqKRLQEALERQKefdptiadeKESVAERKENNEEEENsswEKEEKRDSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 695 RSFHI-ENKLKDllaekerfeEERLREQQGLEQQRRQEEESLFR----IREELRKLQELNSHEQAEKVQIFQELDRLHQE 769
Cdd:pfam02029 136 REKEYqENKWST---------EVRQAEEEGEEEEDKSEEAEEVPtenfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 770 QNAQSAKLRLEKRRLEEEEKEQVQRVAH---------------LEEQLRKRQDTAPLLCPGEAQRAQEEKRELESI---- 830
Cdd:pfam02029 207 VKSQNGEEEVTKLKVTTKRRQGGLSQSQereeeaevfleaeqkLEELRRRRQEKESEEFEKLRQKQQEAELELEELkkkr 286
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907135707 831 --REALLQAKEMRaggdhtcRDELERAQQYFLEFKRRQL 867
Cdd:pfam02029 287 eeRRKLLEEEEQR-------RKQEEAERKLREEEEKRRM 318
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
630-960 |
4.57e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQRE------ELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEE---SLKRRSFHI 699
Cdd:pfam07888 69 EQWERQRRElesrvaELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEdikTLTQRVLER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 700 ENKLKDLlaekerfeeerLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEkvqiFQELDRLHQEQNAQSAKLRL 779
Cdd:pfam07888 149 ETELERM-----------KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE----FQELRNSLAQRDTQVLQLQD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 780 EKRRLEEEEKEQVQRVAHLE---EQLRKRQDtapLLCPGEaQRAQEEKRELES-----------IREALLQAKEMR---A 842
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEallEELRSLQE---RLNASE-RKVEGLGEELSSmaaqrdrtqaeLHQARLQAAQLTlqlA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 843 GGDHTCRDELERAQQyflefKRRQLVKLASLEKDLVQQ--KDLLSKE--VQEEKVALEHVKCDaggdpsflatddgniLG 918
Cdd:pfam07888 290 DASLALREGRARWAQ-----ERETLQQSAEADKDRIEKlsAELQRLEerLQEERMEREKLEVE---------------LG 349
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907135707 919 GPPDLDKIKTAETRLQSREHQL-QDLLQNHLPALLEEKQRVLD 960
Cdd:pfam07888 350 REKDCNRVQLSESRRELQELKAsLRVAQKEKEQLQAEKQELLE 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
637-1110 |
5.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 637 REELEKLESKRKLIEEMEEKQKS---DKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIEN--KLKDLLAEKE 711
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 712 RFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELnsheQAEKVQIFQELDRL---HQEQNAQSAKLRLEKRRLEEEE 788
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL----KKKLKELEKRLEELeerHELYEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 789 KEQVQRVAHLEEQLRKRQDTAPLlcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTC---------RDELERAQQYF 859
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEE----EISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteEHRKELLEEYT 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 860 LEFKR------------RQLVK-LASLEKDLVQQKDLLS--------KEVQEE--KVALEHVKCDAG---GDPSFLATDD 913
Cdd:PRK03918 459 AELKRiekelkeieekeRKLRKeLRELEKVLKKESELIKlkelaeqlKELEEKlkKYNLEELEKKAEeyeKLKEKLIKLK 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 914 GNILGGPPDLDKIKTAETRLQSREHQLQDllqnhlpaLLEEKQRVLDALDSgvLGLDTtlcqvekevgekeeqiaqYQAN 993
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDE--------LEEELAELLKELEE--LGFES------------------VEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 994 ASQLQQLRATF-EFTanvarqEEKVRRKEKEILESQEKQQREALEQAVAKLEQRRSALQrcstldlEIQEQRQKLGSLHT 1072
Cdd:PRK03918 591 EERLKELEPFYnEYL------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE-------ELRKELEELEKKYS 657
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907135707 1073 SEwsgWQASLETDGEALEMDPARLEHEIHQLKQKICEV 1110
Cdd:PRK03918 658 EE---EYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
726-1068 |
6.18e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 726 QQRRQEEES-LFRIREELRKLQ----ELNS-----HEQAEKVQIFQELDRlhQEQNAQsaklrlekrrleeeEKEQVQRV 795
Cdd:TIGR02168 171 KERRKETERkLERTRENLDRLEdilnELERqlkslERQAEKAERYKELKA--ELRELE--------------LALLVLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 796 AHLEEQLRKRQDtapllcpgEAQRAQEEKRELES-IREALLQAKEMRAGgDHTCRDELERAQQYFLEFKRRQlvklasle 874
Cdd:TIGR02168 235 EELREELEELQE--------ELKEAEEELEELTAeLQELEEKLEELRLE-VSELEEEIEELQKELYALANEI-------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 875 KDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSflatddgnilggppdldKIKTAETRLQSREHQLQDLLQNH--LPALL 952
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELES-----------------KLDELAEELAELEEKLEELKEELesLEAEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 953 EEKQRVLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQyqaNASQLQQLRATFE--------------------FTANVAR 1012
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIAS---LNNEIERLEARLErledrrerlqqeieellkklEEAELKE 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135707 1013 QEEKVRRKEKEILESQE------------KQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLG 1068
Cdd:TIGR02168 438 LQAELEELEEELEELQEelerleealeelREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
635-892 |
8.70e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 635 QQREELEKLESKRK-LIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLlaekerf 713
Cdd:COG4372 10 KARLSLFGLRPKTGiLIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 714 eeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAklrlEKRRLEEEEKEQVQ 793
Cdd:COG4372 83 --------EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEA----QIAELQSEIAEREE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 794 RVAHLEEQLRKRQDTAPLLcpGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASL 873
Cdd:COG4372 151 ELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
250
....*....|....*....
gi 1907135707 874 EKDLVQQKDLLSKEVQEEK 892
Cdd:COG4372 229 AKLGLALSALLDALELEED 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
724-1067 |
9.27e-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: 47.43 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 724 LEQQR-RQEEESLFRIREELRKLQELNSHEQAE---KVQIFQELDRLHQEQNaqsaklrlekrrleeeekEQVQRVaHLE 799
Cdd:pfam17380 296 MEQERlRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERE------------------RELERI-RQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 800 EqlRKRQDtapllcpgEAQRAQEEKRELESIREalLQAKEM-RAGGDHTCRDELERAQQYFLEFKRRQlvklaslekdlv 878
Cdd:pfam17380 357 E--RKREL--------ERIRQEEIAMEISRMRE--LERLQMeRQQKNERVRQELEAARKVKILEEERQ------------ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 879 qqkdllsKEVQEEKVALEHVKCDaggdpsflatddgnilggppdldkiktaetRLQSREHQLQdllqnhlpALLEEKQRV 958
Cdd:pfam17380 413 -------RKIQQQKVEMEQIRAE------------------------------QEEARQREVR--------RLEEERARE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 959 LDALDSgvlgldttlcqvekevgekeeqiaQYQANASQLQQLRatfeftanvarQEEKVRRKEKEILESQEKQQREAleq 1038
Cdd:pfam17380 448 MERVRL------------------------EEQERQQQVERLR-----------QQEEERKRKKLELEKEKRDRKRA--- 489
|
330 340
....*....|....*....|....*....
gi 1907135707 1039 avakLEQRRSALQRcstldlEIQEQRQKL 1067
Cdd:pfam17380 490 ----EEQRRKILEK------ELEERKQAM 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
630-1070 |
1.00e-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: 47.48 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQREELEKLesKRKLIEEMEEKQKsdkaELERMQQEVETRR-----KETEIVQRQIRKQEESLKRRSFHIENK-L 703
Cdd:pfam01576 196 LKKEEKGRQELEKA--KRKLEGESTDLQE----QIAELQAQIAELRaqlakKEEELQAALARLEEETAQKNNALKKIReL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 704 KDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQ--EQNAQSaklrlek 781
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKalEEETRS------- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 782 rrleeeEKEQVQrvahleeQLRKRQDTApllcpgeaqraqeekreLESIREALLQAKEMRAGgdhtcrdeLERAQQYfLE 861
Cdd:pfam01576 343 ------HEAQLQ-------EMRQKHTQA-----------------LEELTEQLEQAKRNKAN--------LEKAKQA-LE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 862 FKRRQLVK----LASLEKDLVQQKDLLSKEVQEEKVAL---EHVKCDAGGDPSFLATDDGNILGGPPDLDK--IKTAEtR 932
Cdd:pfam01576 384 SENAELQAelrtLQQAKQDSEHKRKKLEGQLQELQARLsesERQRAELAEKLSKLQSELESVSSLLNEAEGknIKLSK-D 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 933 LQSREHQLQD---LLQNHLPALLEEKQRvLDALDSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATFEFTAN 1009
Cdd:pfam01576 463 VSSLESQLQDtqeLLQEETRQKLNLSTR-LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA---QLSDMKKKLEEDAG 538
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 1010 VARQEEKVRRKEKEILESQeKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSL 1070
Cdd:pfam01576 539 TLEALEEGKKRLQRELEAL-TQQLEEKAAAYDKLEKTKNRLQQeLDDLLVDLDHQRQLVSNL 599
|
|
| 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 1907135707 507 LKEGQTYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLrgSQCS---VNGVQIVDATQLNQGAVILLGrTNM 582
Cdd:cd22673 18 LTKKSCTFGR---DLSCDIRIQLPGVSREHCRIEvDENGKAYLENL--STTNptlVNGKAIEKSAELKDGDVITIG-GRS 91
|
...
gi 1907135707 583 FRF 585
Cdd:cd22673 92 FRF 94
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
633-891 |
1.31e-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: 46.57 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKL----------ESKRKLIEEMEEKQKSDKAELERMQQEVETRRKEteivqRQIRKQEESLKRrsfhiENK 702
Cdd:pfam15558 72 ARLGREERRRAdrrekqviekESRWREQAEDQENQRQEKLERARQEAEQRKQCQE-----QRLKEKEEELQA-----LRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 703 LKDLLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEkvqifQELDRLHQEQNAQSAKLRLEKR 782
Cdd:pfam15558 142 QNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAE-----ELLRRLSLEQSLQRSQENYEQL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 783 RLEEEEKEQvQRVAHLEEQLRKRQdtapllcpgeaQRAQEEKRELESIREALLQAKEMRaggdhtcrdeLERAQQYFLEF 862
Cdd:pfam15558 217 VEERHRELR-EKAQKEEEQFQRAK-----------WRAEEKEEERQEHKEALAELADRK----------IQQARQVAHKT 274
|
250 260 270
....*....|....*....|....*....|.
gi 1907135707 863 KRR--QLVKLASLEKDLVQQkdLLSKEVQEE 891
Cdd:pfam15558 275 VQDkaQRARELNLEREKNHH--ILKLKVEKE 303
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
631-902 |
2.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQRE---ELEKLESKRKLIEEmEEKQKSDKAELERMQQEVETRRKETEIVQrQIRKQEESLKrrsfhIENKLKdll 707
Cdd:PTZ00121 1078 DFDFDAKEdnrADEATEEAFGKAEE-AKKTETGKAEEARKAEEAKKKAEDARKAE-EARKAEDARK-----AEEARK--- 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 708 aekeRFEEERLREQQGLEQQRRQEEEslfRIREELRKLQELnshEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEE 787
Cdd:PTZ00121 1148 ----AEDAKRVEIARKAEDARKAEEA---RKAEDAKKAEAA---RKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 788 EKEQVQRVAHL---EEQLRKRQDTAPllcPGEAQRAQEEKRELE-------SIREALLQAKEMRAGGDHTCRDELERAQq 857
Cdd:PTZ00121 1218 RKAEDAKKAEAvkkAEEAKKDAEEAK---KAEEERNNEEIRKFEearmahfARRQAAIKAEEARKADELKKAEEKKKAD- 1293
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907135707 858 yflEFKRRQLVKLASLEKDLVQQK---DLLSKEVQEEKVALEHVKCDA 902
Cdd:PTZ00121 1294 ---EAKKAEEKKKADEAKKKAEEAkkaDEAKKKAEEAKKKADAAKKKA 1338
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
630-897 |
2.40e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQREEL-EKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrrsfhiENKLKDLLA 708
Cdd:COG4372 68 LEQARSELEQLeEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ--------RKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 709 EKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKV--QIFQELDRLHQEQNAQSAKLRLEKRRLEE 786
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELlkEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 787 EEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQ 866
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
250 260 270
....*....|....*....|....*....|.
gi 1907135707 867 LVKLASLEKDLVQQKDLLSKEVQEEKVALEH 897
Cdd:COG4372 300 LLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| Yop-YscD_cpl |
pfam16697 |
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ... |
505-589 |
2.45e-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: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 505 YHLKEGQTYVGREDastEQDIVLHGLDLESEHCVFENAGGTVTLIPLR-GSQCSVNGVQIVDAT-QLNQGAVILLGRTnM 582
Cdd:pfam16697 12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGsGNGTLVNGQRVTELGiALRPGDRIELGQT-E 87
|
....*..
gi 1907135707 583 FRFNHPK 589
Cdd:pfam16697 88 FCLVPAD 94
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
631-1046 |
3.40e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRR-----------KETEIVQRQIRKQEESLKRRSFHI 699
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRageakqlaeaqKEAELLRKQLSKTQEELEAQVTLV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 700 ENklkdlLAEKERFEEERLREQQGLEQQRRQEEESLFRIREELRKLQ--------------ELNSHEQAEKVQIFQELDR 765
Cdd:pfam07111 221 ES-----LRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqsltHMLALQEEELTRKIQPSDS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 766 LHQE--QNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLlcpgeaQRAQEEKRELESIREALLQAK----E 839
Cdd:pfam07111 296 LEPEfpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL------QEQVTSQSQEQAILQRALQDKaaevE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 840 MRAGGDHTCRDELERAQqyflEFKRRQLVKLASLEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSF-----LATDDG 914
Cdd:pfam07111 370 VERMSAKGLQMELSRAQ----EARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLsnrlsYAVRKV 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 915 NILGGPPdLDKIKTAETRLQS-----REHQLQDLLQNHLPALLEEKQRvLDAldsgVLGLDTTLCQVEKEVGEKEEQIAQ 989
Cdd:pfam07111 446 HTIKGLM-ARKVALAQLRQEScppppPAPPVDADLSLELEQLREERNR-LDA----ELQLSAHLIQQEVGRAREQGEAER 519
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 990 YQAN--ASQL-QQLRATFEFTANVARQEEKVRRKEKEILES-----QE-KQQRE----ALEQAVAKLEQR 1046
Cdd:pfam07111 520 QQLSevAQQLeQELQRAQESLASVGQQLEVARQGQQESTEEaaslrQElTQQQEiygqALQEKVAEVETR 589
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
634-839 |
4.02e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLESKR-----------KLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK 702
Cdd:TIGR02168 820 ANLRERLESLERRIaaterrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 703 LKDLlaekerfeeerlreqQGLEQQRRQEEESLFRIREELRKLQElnsHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKR 782
Cdd:TIGR02168 900 SEEL---------------RELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907135707 783 RLEEEEKEQVQRVAHLEEQLrKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKE 839
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENKI-KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
631-702 |
4.09e-04 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 42.73 E-value: 4.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 631 EFERQQREELEKLESKRKliEEMEEKQKsdKAELERmQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK 702
Cdd:pfam15346 74 EEERKKREELERILEENN--RKIEEAQR--KEAEER-LAMLEEQRRMKEERQRREKEEEEREKREQQKILNK 140
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
630-1040 |
4.17e-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: 45.55 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 630 LEFERQQREELEKLesKRKLIEEMEekqkSDKAELE------RMQQEVETRRkETEIVQRQIRKQEES---------LKR 694
Cdd:pfam01576 280 LESERAARNKAEKQ--RRDLGEELE----ALKTELEdtldttAAQQELRSKR-EQEVTELKKALEEETrsheaqlqeMRQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 695 RSFHIENKLKDLLAEKERFEEERLREQQGLE-------------QQRRQEEESlfRIREELRKLQELNS-HEQAEKVQif 760
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAKQALEsenaelqaelrtlQQAKQDSEH--KRKKLEGQLQELQArLSESERQR-- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 761 QEL-DRLHQEQNAQSAKLRLEKRRLEEEEKEQvQRVAHLEEQLrkrQDTAPLLcpgeaqraQEEKRE----------LES 829
Cdd:pfam01576 429 AELaEKLSKLQSELESVSSLLNEAEGKNIKLS-KDVSSLESQL---QDTQELL--------QEETRQklnlstrlrqLED 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 830 IREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLASLEKdLVQQKDLLSKEVQEEKVALEHvKCDAggdpsfl 909
Cdd:pfam01576 497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEE-KAAA------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 910 atddgnilggppdLDKIKTAETRLQsreHQLQDLL-----QNHLPALLEEKQRVLDALdsgvlgldttlcqvekevgeke 984
Cdd:pfam01576 568 -------------YDKLEKTKNRLQ---QELDDLLvdldhQRQLVSNLEKKQKKFDQM---------------------- 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907135707 985 eqIAQYQANASQLQQLRATFEFTA--------NVARQEEKVRRKEKEiLESQEKQQREALEQAV 1040
Cdd:pfam01576 610 --LAEEKAISARYAEERDRAEAEAreketralSLARALEEALEAKEE-LERTNKQLRAEMEDLV 670
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
643-830 |
4.18e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 42.72 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 643 LESKRKLIEEMEEKQksdkaELERMQQEVETRRKETEIVQR----QIRKQEESLKrrsfhienklkdllaekerfeeerl 718
Cdd:pfam05672 16 LAEKRRQAREQRERE-----EQERLEKEEEERLRKEELRRRaeeeRARREEEARR------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 719 reqqgLEQQRRQEEESLFRIREELRKLQELNshEQAEKVQIFQEldRLHQEQNAQsaklrlekrrleeeekeqvqrvahl 798
Cdd:pfam05672 66 -----LEEERRREEEERQRKAEEEAEEREQR--EQEEQERLQKQ--KEEAEAKAR------------------------- 111
|
170 180 190
....*....|....*....|....*....|..
gi 1907135707 799 EEQLRKRQDTAPLLCPGEAQRaQEEKRELESI 830
Cdd:pfam05672 112 EEAERQRQEREKIMQQEEQER-LERKKRIEEI 142
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
922-1107 |
4.26e-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: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 922 DLDKIKTAETRLQSREHQLQDLLQNHLPAL-LEEKQRVLDALDSGVlgldtTLCQVEKEVGEKEEQIAQYQANASQLQQL 1000
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAAL-----RLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1001 RATFEftANVARQEEKVRRKEKEILES------QEKQQREALEQAVAKLEQRRSALQR-CSTLDLEIQEQRQKLGSLHT- 1072
Cdd:COG4913 311 LERLE--ARLDALREELDELEAQIRGNggdrleQLEREIERLERELEERERRRARLEAlLAALGLPLPASAEEFAALRAe 388
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907135707 1073 -----SEWSGWQASLETDGEALEMDPARLEHEIHQLKQKI 1107
Cdd:COG4913 389 aaallEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-1195 |
7.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIE-----EMEEKQKSDKAELERMQQEV----ETRRKETEIVQRQIRKQEESLKRRSfhienkl 703
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEvrkaeELRKAEDARKAEAARKAEEErkaeEARKAEDAKKAEAVKKAEEAKKDAE------- 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 704 kdllaEKERFEEERLREQQGLEQQRRQEEESLFRIR---EELRKLQELnshEQAEKVQIFQELDRLHQEQNAQSAKLRLE 780
Cdd:PTZ00121 1241 -----EAKKAEEERNNEEIRKFEEARMAHFARRQAAikaEEARKADEL---KKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 781 KRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRelesiREALLQAKEMRAGGDHTCRDELERAQqyfl 860
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAE--------EAKKAAEAAK-----AEAEAAADEAEAAEEKAEAAEKKKEE---- 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 861 EFKRRQLVKLASLEKdlvQQKDLLSKEVQEEKVALEHVKCDAGgdpsflATDDGNILGGPPDlDKIKTAETRLQSREHQL 940
Cdd:PTZ00121 1376 AKKKADAAKKKAEEK---KKADEAKKKAEEDKKKADELKKAAA------AKKKADEAKKKAE-EKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 941 QDLLQNHlpalLEEKQRVLDALDSGvlgldttlcqVEKEVGEKEEQIAQYQANASQLQQLRATFEFTANVARQEEKVRRK 1020
Cdd:PTZ00121 1446 ADEAKKK----AEEAKKAEEAKKKA----------EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1021 EKEILESQEKQQREALEQAvaklEQRRSALQrcstldLEIQEQRQKLGSLHTSEwsgwqaSLETDGEALEMDPARLEHEI 1100
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKA----EEAKKADE------AKKAEEKKKADELKKAE------ELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1101 HQLKQKICEVdgVQRPHHGILEGQAVLSSLPPSGGNSHLAPLMDARISA---YIEEEVQRRLHDLHRAIGDANHTPADVM 1177
Cdd:PTZ00121 1576 KNMALRKAEE--AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
570
....*....|....*...
gi 1907135707 1178 KSNEELHNGTTQRKLKYE 1195
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE 1671
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
634-733 |
8.26e-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: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQevetrRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAekerf 713
Cdd:pfam09731 319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFE-----REREEIRESYEEKLRTELERQAEAHEEHLKDVLV----- 386
|
90 100
....*....|....*....|
gi 1907135707 714 eeerlreQQGLEQQRRQEEE 733
Cdd:pfam09731 387 -------EQEIELQREFLQD 399
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
729-1050 |
9.23e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 729 RQEEESLFRiREELRKLQElnSHEQAEKVqiFQELDRLHQEQNAQSAKlrlekrrleeeekeqvqrvahLEEQLrkrQDT 808
Cdd:pfam01576 2 RQEEEMQAK-EEELQKVKE--RQQKAESE--LKELEKKHQQLCEEKNA---------------------LQEQL---QAE 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 809 APLLCPGEAQRAQ--EEKRELESIrealLQAKEMRAGgdhtcrDELERAQQYFLEFKRRQlVKLASLEKDLVQQKDLLSK 886
Cdd:pfam01576 53 TELCAEAEEMRARlaARKQELEEI----LHELESRLE------EEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 887 eVQEEKVALEhVKCDAGGDPSFLATDDGNILGGPPDL--DKIKTAETRLQSREHQLQDL--LQNHLPALLEEKQRVLDAL 962
Cdd:pfam01576 122 -LQLEKVTTE-AKIKKLEEDILLLEDQNSKLSKERKLleERISEFTSNLAEEEEKAKSLskLKNKHEAMISDLEERLKKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 963 DSGVLGLDTTLCQVEKEVGEKEEQIAQYQAnasQLQQLRATF-----EFTANVARQEE----------KVRRKEKEILES 1027
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQA---QIAELRAQLakkeeELQAALARLEEetaqknnalkKIRELEAQISEL 276
|
330 340
....*....|....*....|...
gi 1907135707 1028 QEKQQREalEQAVAKLEQRRSAL 1050
Cdd:pfam01576 277 QEDLESE--RAARNKAEKQRRDL 297
|
|
| FHA |
pfam00498 |
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif. |
512-577 |
9.36e-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: 9.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907135707 512 TYVGRedaSTEQDIVLHGLDLESEHCVFE-NAGGTVTLIPLRGSQ-CSVNGVQI-VDATQLNQGAVILL 577
Cdd:pfam00498 1 VTIGR---SPDCDIVLDDPSVSRRHAEIRyDGGGRFYLEDLGSTNgTFVNGQRLgPEPVRLKDGDVIRL 66
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
566-896 |
9.69e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.18 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 566 ATQLNQGAVILLGRTNMFRFNHPKEAAKLREKrksgllssfsLSMTDLSKSCENLSAVMLYNPGLEFERQQREEL--EKL 643
Cdd:COG5185 201 SGTVNSIKESETGNLGSESTLLEKAKEIINIE----------EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrlEKL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 644 ESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESlkrRSFHIENKLKDLLAEKERFEEERlreQQG 723
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEESKRETETGIQNL---TAE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 724 LEQQRRQEEESLFRIREELRKLQELNSHEQAEKvQIFQELD-------RLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVA 796
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIENIVGEVELSKSSE-ELDSFKDtiestkeSLDEIPQNQRGYAQEILATLEDTLKAADRQIE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 797 HLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREallqaKEMRAGGDhtcrDELERAQQYFLEFKRRQLVKLASLEKD 876
Cdd:COG5185 424 ELQRQIEQATS--------SNEEVSKLLNELISELN-----KVMREADE----ESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
330 340
....*....|....*....|...
gi 1907135707 877 LVQ---QKDLLSKEVQEEKVALE 896
Cdd:COG5185 487 LTQiesRVSTLKATLEKLRAKLE 509
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
637-884 |
1.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 637 REELEKLESKRK----------LIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRS-FHIENKLKD 705
Cdd:PRK04863 900 REQLDEAEEAKRfvqqhgnalaQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhFSYEDAAEM 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 706 LlaekerfeEERLREQQGLEQQRRQEEESLFRIREELRKLQElnshEQAEKVQIFQELDRLHQEQNaqsaklrlekrrle 785
Cdd:PRK04863 980 L--------AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA----QLAQYNQVLASLKSSYDAKR-------------- 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 786 eeekeqvQRVAHLEEQLrkrQDTAPLLCPGEAQRAQEEKRELesirEALLQAKEMRaggdhtcRDELERaQQYFLEFKRR 865
Cdd:PRK04863 1034 -------QMLQELKQEL---QDLGVPADSGAEERARARRDEL----HARLSANRSR-------RNQLEK-QLTFCEAEMD 1091
|
250 260
....*....|....*....|
gi 1907135707 866 QLVK-LASLEKDLVQQKDLL 884
Cdd:PRK04863 1092 NLTKkLRKLERDYHEMREQV 1111
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
725-1052 |
1.14e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 43.49 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 725 EQQRRQEEEslFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRV--------- 795
Cdd:pfam15558 35 EELRRRDQK--RQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQenqrqekle 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 796 -AHLEEQLRKRQdtapllcpgEAQRAQEEKRELESIREA---LLQAKEMRAggdhtCRDELERAQQyflEFKRRQLVKLA 871
Cdd:pfam15558 113 rARQEAEQRKQC---------QEQRLKEKEEELQALREQnslQLQERLEEA-----CHKRQLKERE---EQKKVQENNLS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 872 SLEKDLVQQKDLLSKEVQEE---KVALEHvkcdaggdpSFLATDDgnilgGPPDLDKIKTAETRLQSREHQLQdLLQNHL 948
Cdd:pfam15558 176 ELLNHQARKVLVDCQAKAEEllrRLSLEQ---------SLQRSQE-----NYEQLVEERHRELREKAQKEEEQ-FQRAKW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 949 PALLEEKQRV--LDALdsgvlgldttlcqvekeVGEKEEQIAQYQANASQLQQLRATFEFTANVARqeEKVRRKEKEILE 1026
Cdd:pfam15558 241 RAEEKEEERQehKEAL-----------------AELADRKIQQARQVAHKTVQDKAQRARELNLER--EKNHHILKLKVE 301
|
330 340
....*....|....*....|....*.
gi 1907135707 1027 SQEKQQREALEQAVAKLEQRRSALQR 1052
Cdd:pfam15558 302 KEEKCHREGIKEAIKKKEQRSEQISR 327
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
633-973 |
1.20e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKsDKAELERMQQEVETRRKETEIVQRQIRKQEeslkrrsfhienKLKDLLAEKER 712
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKAK-EEAEEERLAELEAKRQAEEEAREAKAEAEQ------------RAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 713 FEEERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVqifQELDRLHQEQNAQSAklrLEKRRLEEEEKEQV 792
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKA---EEAKRKAEEEAKRKA---EEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 793 QRVAHLEEQLRKRQDTAPLLCPGEAQRAQEEKRELESIREALLQAKEMRAGGDHTCRDELERAQQYFLEFKRRQLVKLAS 872
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 873 LEKDLVQQKDLLSKEVQEEKVALEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAETRLQSREHQLQDLLQNHLPALL 952
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340
....*....|....*....|.
gi 1907135707 953 EEKQRVLDALDSGVLGLDTTL 973
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGG 332
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
727-1109 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 727 QRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRL-----HQEQNAQSAklrlekrrleeeekeqvqrvahlEEQ 801
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsaresDLEQDYQAA-----------------------SDH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 802 LRKRQdtapllcpgEAQRAQEE----KRELESIREALLQAKEMRAGGDH---TCRDELERAQQYFLEFKrrqlVKLASLE 874
Cdd:COG3096 336 LNLVQ---------TALRQQEKieryQEDLEELTERLEEQEEVVEEAAEqlaEAEARLEAAEEEVDSLK----SQLADYQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 875 KDL-VQQKDLLskEVQEEKVALEHVKcdaggdpsflatddgnILGGPPDLDkIKTAETRLQSREHQLQDLLQnhlpALLE 953
Cdd:COG3096 403 QALdVQQTRAI--QYQQAVQALEKAR----------------ALCGLPDLT-PENAEDYLAAFRAKEQQATE----EVLE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 954 EKQRVLDA------------LDSGVLGlDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATF-EFTANVARQEEKVR-- 1018
Cdd:COG3096 460 LEQKLSVAdaarrqfekayeLVCKIAG-EVERSQAWQTARELLRRYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERll 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1019 -------------RKEKEILESQEKQQREALEQAVAKLEQRRSALQRcsTLDlEIQEQRQKLGSLhTSEWSGWQASLET- 1084
Cdd:COG3096 539 eefcqrigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ--QLE-QLRARIKELAAR-APAWLAAQDALERl 614
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907135707 1085 ---DGEALEMDPA---------RLEHEIHQLKQKICE 1109
Cdd:COG3096 615 reqSGEALADSQEvtaamqqllEREREATVERDELAA 651
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
635-708 |
1.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907135707 635 QQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLA 708
Cdd:PRK12704 68 KLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| FHA_RADIL |
cd22733 |
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ... |
486-588 |
1.54e-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: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 486 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGREDASTEQDIVLHGLDLESEHCVFE-------NAGGTVTLIPLRGSQCSV 558
Cdd:cd22733 4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvrlpkhRSEEKLVLEPIPGAHVSV 83
|
90 100 110
....*....|....*....|....*....|
gi 1907135707 559 NGVQIVDATQLNQGAVILLGRTNMFRFNHP 588
Cdd:cd22733 84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
633-821 |
1.73e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENK---------- 702
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 703 -----LKDLLAEKERFEEERLREQQGLEQQRRQeeeslfriREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSAKL 777
Cdd:COG3883 109 lgsesFSDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907135707 778 RLEKRRLEEEEKEQVQRVAHLEEQLRKRQDTAPLLCPGEAQRAQ 821
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
629-904 |
1.74e-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: 43.52 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 629 GLEFERQQREELEKLESKRKL----IEEMEEKQKsdKAELERMQQEVETRRKETEIvqRQIRKQEESLKRRSFHIENKLK 704
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEIASlersIAEKERELE--DAEERLAKLEAEIDKLLAEI--EELEREIEEERKRRDKLTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 705 DLLAEKERfeeerlreqqgLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNAQSaklrlekrrl 784
Cdd:TIGR02169 361 ELKEELED-----------LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS---------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 785 eeeekeqvQRVAHLEEQL-RKRQDTApllcpgEAQRAQEEKR-ELESIREALLQAKEMRAggdhTCRDELERAQQYFLEF 862
Cdd:TIGR02169 420 --------EELADLNAAIaGIEAKIN------ELEEEKEDKAlEIKKQEWKLEQLAADLS----KYEQELYDLKEEYDRV 481
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907135707 863 KRRqlvkLASLEKDLVQ---QKDLLSKEVQEEKVALEHVKCDAGG 904
Cdd:TIGR02169 482 EKE----LSKLQRELAEaeaQARASEERVRGGRAVEEVLKASIQG 522
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
991-1074 |
2.00e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 991 QANASQLQQLRAtfEFTANVARQEEKvRRKEKEILESQEKQQrealeqavAKLEQRRSALQRC-STLDLEIQEQRQKLGS 1069
Cdd:PRK11637 169 QETIAELKQTRE--ELAAQKAELEEK-QSQQKTLLYEQQAQQ--------QKLEQARNERKKTlTGLESSLQKDQQQLSE 237
|
....*
gi 1907135707 1070 LHTSE 1074
Cdd:PRK11637 238 LRANE 242
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
631-762 |
2.22e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.83 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 631 EFERQQRE-ELEKLESKRKLIEEMEEKQK---SDKAELERMQQEVETRRKEteivqRQIRKQEESLKRRSFHIENKLKDL 706
Cdd:pfam11600 12 EKEKQRLEkDKERLRRQLKLEAEKEEKERlkeEAKAEKERAKEEARRKKEE-----EKELKEKERREKKEKDEKEKAEKL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907135707 707 LAEKERFEEERLREQQGLEQQRRQEEESlfRIREELRKLQElnshEQAEKVQIFQE 762
Cdd:pfam11600 87 RLKEEKRKEKQEALEAKLEEKRKKEEEK--RLKEEEKRIKA----EKAEITRFLQK 136
|
|
| Pinin_SDK_memA |
pfam04696 |
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ... |
634-708 |
2.27e-03 |
|
pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.
Pssm-ID: 461396 [Multi-domain] Cd Length: 130 Bit Score: 39.97 E-value: 2.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907135707 634 RQQREELEKLESKRKLIEEM-EEKQKSDKAELERMQ-QEVETRRKETEIVQRQIRKQEESLKR-RSFHIENKLKDLLA 708
Cdd:pfam04696 22 KKEESKQKEKEERRAEIEKRlEEKAKQEKEELEERKrEEREELFEERRAEQIELRALEEKLELkELMETWHENLKALA 99
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
633-693 |
2.33e-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: 2.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLK 693
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
821-1055 |
2.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 821 QEEKRELESI-REALLQAKEMRaggdHTCRDELERaqqyflEFKRRQlVKLASLEKDLVQQKDLLSKEvqeekvalehvk 899
Cdd:PRK12704 45 EEAKKEAEAIkKEALLEAKEEI----HKLRNEFEK------ELRERR-NELQKLEKRLLQKEENLDRK------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 900 cdaggdpsflatddgnilggppdLDKIKTAETRLQSREHQLQDLLQNhlpalLEEKQRVLDALdsgvlgldttlcqvEKE 979
Cdd:PRK12704 102 -----------------------LELLEKREEELEKKEKELEQKQQE-----LEKKEEELEEL--------------IEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 980 VGEKEEQIAQY---QANASQLQQLRATfeftanvARQE--EKVRRKEKEILESQEKQQREALEQAVakleqrrsalQRCS 1054
Cdd:PRK12704 140 QLQELERISGLtaeEAKEILLEKVEEE-------ARHEaaVLIKEIEEEAKEEADKKAKEILAQAI----------QRCA 202
|
.
gi 1907135707 1055 T 1055
Cdd:PRK12704 203 A 203
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
590-836 |
2.77e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 590 EAAKLREKRKSGLLSsfslsMTDLSKSCENLSAVMlynpglefeRQQREELEKLESKRKLIEE--MEEKQKSDK-AELER 666
Cdd:COG1340 58 EAQELREKRDELNEK-----VKELKEERDELNEKL---------NELREELDELRKELAELNKagGSIDKLRKEiERLEW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 667 MQQ-EVETRRKETEIVQrQIRKQEESLKRR--SFHIENKLKDLLAEKERFEEERLREQQGLE------QQRRQEEESLFR 737
Cdd:COG1340 124 RQQtEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAELKELRKEAEEIHKKIKelaeeaQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 738 IREELRKlqELNS-HEQAekVQIFQELDRLHQEQNAQSaklrlekrrleeeekeqvQRVAHLEEQLRKRQDTApllcpgE 816
Cdd:COG1340 203 EADELRK--EADElHKEI--VEAQEKADELHEEIIELQ------------------KELRELRKELKKLRKKQ------R 254
|
250 260
....*....|....*....|
gi 1907135707 817 AQRAQEEKRELESIREALLQ 836
Cdd:COG1340 255 ALKREKEKEELEEKAEEIFE 274
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
725-1082 |
2.96e-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: 42.52 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 725 EQQRRQEEESLFRIREELRKLQElNSHEQAEKVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRK 804
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMK-IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 805 RQDTApllcpgeAQRAQEEKRELESIREALLQakemraggdhtCRDELERAQQYFLEFKRRQLVKLASLEKDLVQQKDLL 884
Cdd:pfam12128 295 LDDQW-------KEKRDELNGELSAADAAVAK-----------DRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 885 SkEVQEEKVALE--HVKCDAGGDPSFLATDDGN---ILGGPPDLDKIKTAETR--------LQSREHQLQDLLQNHLPAL 951
Cdd:pfam12128 357 E-NLEERLKALTgkHQDVTAKYNRRRSKIKEQNnrdIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEF 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 952 LEEKQRVLDALdsgvlgldttlcqvekevGEKEEQIAQYQANASQLQQLRAtFEFTANVARQEEKVRRKEKEILESQEKQ 1031
Cdd:pfam12128 436 NEEEYRLKSRL------------------GELKLRLNQATATPELLLQLEN-FDERIERAREEQEAANAEVERLQSELRQ 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907135707 1032 QREALEQAVAKLEQRRSALQRCSTLDLEIQEQ-RQKLGSLH---TSEWSGWQASL 1082
Cdd:pfam12128 497 ARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLhflRKEAPDWEQSI 551
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
610-1110 |
3.19e-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: 42.40 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 610 MTDLSKSCENL--------------------SAVMLYNPGL-EFERQQREELEKLESkrKLIEEMEEKQK---SDKAELE 665
Cdd:pfam05483 25 KSNLSKNGENIdsdpafqklnflpmleqvanSGDCHYQEGLkDSDFENSEGLSRLYS--KLYKEAEKIKKwkvSIEAELK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 666 RMQQEVETRRKETEIVQRQIR-----------KQEESLKRR---------SFHIENKLKDLLAEKERFEEERLREQQ--- 722
Cdd:pfam05483 103 QKENKLQENRKIIEAQRKAIQelqfenekvslKLEEEIQENkdlikennaTRHLCNLLKETCARSAEKTKKYEYEREetr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 723 ---------------GLEQQRRQEE----ESLFRIREELRKLQELNSHEQAE---------------------------- 755
Cdd:pfam05483 183 qvymdlnnniekmilAFEELRVQAEnarlEMHFKLKEDHEKIQHLEEEYKKEindkekqvsllliqitekenkmkdltfl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 756 ------KVQIFQELDRLHQEQNAQSAKLRLEKRRLEEEEKEQVQRVAHLEEQLRKR-QDTAPLLCpgeaQRAQEEKRELE 828
Cdd:pfam05483 263 leesrdKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlQIATKTIC----QLTEEKEAQME 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 829 SIREAL----LQAKEMRAGgdhTCR-DELERAQQYFLE-------------------------FKRRQLVKLASLEKDLV 878
Cdd:pfam05483 339 ELNKAKaahsFVVTEFEAT---TCSlEELLRTEQQRLEknedqlkiitmelqkksseleemtkFKNNKEVELEELKKILA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 879 QQKDLLSKEVQEEKVAlEHVKCDAGGDPSFLATDDGNILGGPPDLDKIKTAE-----------TRLQSREHQLQDLLQNH 947
Cdd:pfam05483 416 EDEKLLDEKKQFEKIA-EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEehylkevedlkTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 948 LPALLEEKQRVLDALDSgVLGLDTTLCQVEKEVGEKEEQIAQYQANASQLQQLRATFEFTanvaRQEEKVRRKE-KEILE 1026
Cdd:pfam05483 495 DKLLLENKELTQEASDM-TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV----REEFIQKGDEvKCKLD 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1027 SQEKQQREALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDGE--ALEMDPARLEHEIHQLK 1104
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELELASAK 649
|
....*.
gi 1907135707 1105 QKICEV 1110
Cdd:pfam05483 650 QKFEEI 655
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
636-762 |
3.40e-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: 40.03 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 636 QREELEKLESKRKLIEEMEEKQksdkAELERMQQEVETRRKETEIvqRQIRKQ-EESLKRRSFHIEnklkdllaekerfe 714
Cdd:pfam15346 36 EAEVERRVEEARKIMEKQVLEE----LEREREAELEEERRKEEEE--RKKREElERILEENNRKIE-------------- 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907135707 715 eerlreqqglEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQE 762
Cdd:pfam15346 96 ----------EAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKRE 133
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
630-695 |
3.41e-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: 3.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 630 LEFERQQREEleklESKRKLIEEmEEKQKSDKAELE------RMQQEVETRRKETEivqRQIRKQEESLKRR 695
Cdd:pfam12037 76 LKIERQRVEY----EERRKTLQE-ETKQKQQRAQYQdelarkRYQDQLEAQRRRNE---ELLRKQEESVAKQ 139
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
634-734 |
3.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDLLAEKERF 713
Cdd:COG3883 129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
90 100
....*....|....*....|.
gi 1907135707 714 EEERLREQQGLEQQRRQEEES 734
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAA 229
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
633-875 |
3.90e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 633 ERQQREELEKLESKRKLIEEMEE--KQKSDKAELERMQQEVETRRKETEIVQRQIRKQE-ESLKRRSFHIENKLKDLLAE 709
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEfnEEQAEWKELEKEEEREEDERILEYLKEKAEREEErEAEREEIEEEKEREIARLRA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 710 kerfeeerlreQQGLEQQRRQEEESLF--RIREELRKLQELNSHEQAEK-VQIFQELDRLHQEQNAQSAKLRLEKRRLEE 786
Cdd:pfam13868 192 -----------QQEKAQDEKAERDELRakLYQEEQERKERQKEREEAEKkARQRQELQQAREEQIELKERRLAEEAEREE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 787 EEKEQVQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELES-IREALLQAKEMRAggdhtcRDELERAQQYFLEFKRR 865
Cdd:pfam13868 261 EEFERMLRKQAEDEEIEQEEAEK------RRMKRLEHRRELEKqIEEREEQRAAERE------EELEEGERLREEEAERR 328
|
250
....*....|
gi 1907135707 866 QLVKLASLEK 875
Cdd:pfam13868 329 ERIEEERQKK 338
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
625-1052 |
5.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 625 LYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEE--SLKRRSFHIENK 702
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEakAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 703 LKDLlaekerfeeERLREQQGLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQ-------------ELDRLHQE 769
Cdd:PRK03918 381 LTGL---------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrELTEEHRK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 770 QnaqsakLRLEKRRLEEEEKEQVQRVAHLEEQLRKRQDtapllcpgEAQRAQEEKRELESIREALLQAKEMRAGGDHTCR 849
Cdd:PRK03918 452 E------LLEEYTAELKRIEKELKEIEEKERKLRKELR--------ELEKVLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 850 DELERAQQYFLEFKRRqLVKL----ASLEKDLVQQKDLLSK---------EVQEEKVALEHVKCDAGgdpsFLATDDGN- 915
Cdd:PRK03918 518 EELEKKAEEYEKLKEK-LIKLkgeiKSLKKELEKLEELKKKlaelekkldELEEELAELLKELEELG----FESVEELEe 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 916 --------------ILGGPPDL------------------DKIKTAETRLQSREHQLQDLLQNHLPALLEEKQRVLDALD 963
Cdd:PRK03918 593 rlkelepfyneyleLKDAEKELereekelkkleeeldkafEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELS 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 964 SGVLGLDttlcqvekevgekeeqiAQYQANASQLQQLRATFEftaNVARQEEKVRRKEKEIlesqekqqrEALEQAVAKL 1043
Cdd:PRK03918 673 RELAGLR-----------------AELEELEKRREEIKKTLE---KLKEELEEREKAKKEL---------EKLEKALERV 723
|
....*....
gi 1907135707 1044 EQRRSALQR 1052
Cdd:PRK03918 724 EELREKVKK 732
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
634-770 |
6.91e-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: 38.70 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQRE--ELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETRRKETEIVQRQIRKQEESLKRRSFHIENKLKDllaeke 711
Cdd:pfam12474 6 EQQKDrfEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIRAEQKKRLKMFRESLKQEKKELK------ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907135707 712 rfeeerlreqQGLEQQRRQEEESLFRIREELRKLQELNSHE---QAEKVQIFQELDRLHQEQ 770
Cdd:pfam12474 80 ----------QEVEKLPKFQRKEAKRQRKEELELEQKHEELeflQAQSEALERELQQLQNEK 131
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
641-1109 |
7.00e-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: 41.31 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 641 EKLESKRKLI---EEMEEKQKSDKAELERMQQEVETRRKETE-----------IVQRQIRKQEESLK-----RRSFHIEN 701
Cdd:pfam01576 47 EQLQAETELCaeaEEMRARLAARKQELEEILHELESRLEEEEersqqlqnekkKMQQHIQDLEEQLDeeeaaRQKLQLEK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 702 -----KLKDLlaekERFEEERLREQQGLEQQRRQEEESLF----RIREELRKLQELNSHEQAEKVQIFQELDRLHQEQNA 772
Cdd:pfam01576 127 vtteaKIKKL----EEDILLLEDQNSKLSKERKLLEERISeftsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 773 QSAKLRLEKRRLEEEEKEQVQ------RVAHLEEQLRKRQDT-APLLCPGE---AQRAQEEK--RELES----IREALLQ 836
Cdd:pfam01576 203 RQELEKAKRKLEGESTDLQEQiaelqaQIAELRAQLAKKEEElQAALARLEeetAQKNNALKkiRELEAqiseLQEDLES 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 837 AKEMRAGGDHTCRDELERaqqyfLEFKRRQLvkLASLEKDLVQQkDLLSKEVQEekvaLEHVKcdaggdpsflatddgni 916
Cdd:pfam01576 283 ERAARNKAEKQRRDLGEE-----LEALKTEL--EDTLDTTAAQQ-ELRSKREQE----VTELK----------------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 917 lggppdldkiKTAETRLQSREHQLQDLLQNHLPAL------LEEKQRVLDALDSGVLGLDT----------TLCQVEKEV 980
Cdd:pfam01576 334 ----------KALEEETRSHEAQLQEMRQKHTQALeelteqLEQAKRNKANLEKAKQALESenaelqaelrTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 981 GE----KEEQIAQYQANASQLQQLRATFE------------FTANVARQEEKVRRKEKEI--LESQ----------EKQQ 1032
Cdd:pfam01576 404 EHkrkkLEGQLQELQARLSESERQRAELAeklsklqselesVSSLLNEAEGKNIKLSKDVssLESQlqdtqellqeETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 1033 REALEQAVAKLEQRRSALQRCSTLDLEIQEQRQKLGSLHTSEWSGWQASLETDG---EALEMDPARLEHEIHQLKQKICE 1109
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAgtlEALEEGKKRLQRELEALTQQLEE 563
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
634-1032 |
7.94e-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: 41.35 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 634 RQQREELEK-LESKRKLIEEMEEKQKSDKAELERMQQ--EVETRR-----KETEIVQRQIR---KQEESLKRRSFHIEN- 701
Cdd:pfam10174 351 RLRLEEKESfLNKKTKQLQDLTEEKSTLAGEIRDLKDmlDVKERKinvlqKKIENLQEQLRdkdKQLAGLKERVKSLQTd 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 702 ---------KLKDLLAEKERFEEERLREQQGLEQQRRQEEESLfriREELRKLQELNSHEQAEKVQIFQELDRL--HQEQ 770
Cdd:pfam10174 431 ssntdtaltTLEEALSEKERIIERLKEQREREDRERLEELESL---KKENKDLKEKVSALQPELTEKESSLIDLkeHASS 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 771 NAQSAKLRLEKRRLEEEEKEQ-VQRVAHLEEQLRKRQDTApllcpgEAQRAQEEKRELESIREALLQAKEMRAGgdhTCR 849
Cdd:pfam10174 508 LASSGLKKDSKLKSLEIAVEQkKEECSKLENQLKKAHNAE------EAVRTNPEINDRIRLLEQEVARYKEESG---KAQ 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 850 DELERaqqyflefkrrqlvkLASLEKDLVQQKDLLSKEVQE-EKVALEHVKCdaggdpsfLATDDGNILGGPPDLDKIKT 928
Cdd:pfam10174 579 AEVER---------------LLGILREVENEKNDKDKKIAElESLTLRQMKE--------QNKKVANIKHGQQEMKKKGA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 929 AETRLQSREHqlQDLLQNHLPALLEEkqrVLDALDSGVLGLDTTlcqvekevgekeeqiaqyQANASQLQQLRATFEFTA 1008
Cdd:pfam10174 636 QLLEEARRRE--DNLADNSQQLQLEE---LMGALEKTRQELDAT------------------KARLSSTQQSLAEKDGHL 692
|
410 420
....*....|....*....|....*
gi 1907135707 1009 NVARQEekvRRKE-KEILESqeKQQ 1032
Cdd:pfam10174 693 TNLRAE---RRKQlEEILEM--KQE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
612-841 |
8.88e-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: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 612 DLSKSCENLSAVMLYNPGLEFERQQ-REELEKLESKrklIEEMEEKQKSDKAELERMQQEVetRRKETEIVQRQIRKQEE 690
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENvKSELKELEAR---IEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907135707 691 SLKR---RSFHIENKLKDLLAEKERFEEERLREQQ---GLEQQRRQEEESLFRIREELRKLQELNSHEQAEKVQIFQELD 764
Cdd:TIGR02169 806 EVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907135707 765 RLHQEqnaqsaklrlekrrleeeekeqvqrVAHLEEQLRKRQDTApllcpGEAQRAQEEKRELESIREALLQAKEMR 841
Cdd:TIGR02169 886 DLKKE-------------------------RDELEAQLRELERKI-----EELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| |
