|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
24-381 |
0e+00 |
|
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: 560.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 24 CCVKVAVNVRPLIGDEVTQGCRECVSVSPVTPQVQMGT-HPFTFDHVYGSNgSPSSLMFEECVAPLVDGLFHGYNATVLA 102
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTdKSFTFDYVFDPS-TEQEEVYNTCVAPLVDGLFEGYNATVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 103 YGQTGSGKTYTMGTGIKDGTKN---GLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEEVLDLLDSSVPfnrlangtp 179
Cdd:cd01372 80 YGQTGSGKTYTMGTAYTAEEDEeqvGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETD--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 180 gkvvlSKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKISSIsv 259
Cdd:cd01372 151 -----KKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPI-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 260 vkDTVDEDMGEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRkeGAHVPYRDSKLTR 339
Cdd:cd01372 224 --APMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKK--GAHVPYRDSKLTR 299
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1063715979 340 LLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQ 381
Cdd:cd01372 300 LLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
26-387 |
2.31e-140 |
|
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: 424.29 E-value: 2.31e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSVSPVTPQV--------QMGTHPFTFDHVYGSNGSPSSlMFEECVAPLVDGLFHGYN 97
Cdd:smart00129 2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTltvrspknRQGEKKFTFDKVFDATASQED-VFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 98 ATVLAYGQTGSGKTYTMGtGIKDGTknGLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEEVLDLLDSSvpfnrlang 177
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMI-GTPDSP--GIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPS--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 178 tpgkvvlsKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKISSI 257
Cdd:smart00129 149 --------SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 258 SVVKdtvdedmgeeycCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRKegaHVPYRDSKL 337
Cdd:smart00129 221 GSGK------------ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR---HIPYRDSKL 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1063715979 338 TRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNKPVAN 387
Cdd:smart00129 286 TRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
32-380 |
4.23e-138 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 418.13 E-value: 4.23e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 32 VRPLIGDEVTQGCRECVSVSPVTPQ--------VQMGTHPFTFDHVYGSNgSPSSLMFEECVAPLVDGLFHGYNATVLAY 103
Cdd:pfam00225 2 VRPLNEREKERGSSVIVSVESVDSEtvesshltNKNRTKTFTFDKVFDPE-ATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 104 GQTGSGKTYTMGtGIKDGTknGLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEEVLDLLDSSVPfnrlangtpgkvv 183
Cdd:pfam00225 81 GQTGSGKTYTME-GSDEQP--GIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNK------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 184 lSKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKissisvvkdt 263
Cdd:pfam00225 145 -NKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNR---------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 264 vDEDMGEEYCCAKLHLVDLAGSERAKRTG-SGGVRLKEGIHINRGLLALGNVISALGDEKRrkegAHVPYRDSKLTRLLQ 342
Cdd:pfam00225 214 -STGGEESVKTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS----KHIPYRDSKLTRLLQ 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 1063715979 343 DSLGGNSKTVMIACISPADINAEETLNTLKYANRARNI 380
Cdd:pfam00225 289 DSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
26-378 |
7.58e-121 |
|
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: 373.13 E-value: 7.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEvTQGCRECVSVSPVT-------PQVQMGTHPFTFDHVYGSNgSPSSLMFEECVAPLVDGLFHGYNA 98
Cdd:cd00106 2 VRVAVRVRPLNGRE-ARSAKSVISVDGGKsvvldppKNRVAPPKTFAFDAVFDST-STQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 99 TVLAYGQTGSGKTYTMGTgiKDGTKNGLIPQVMSALFNKIDS-VKHQMGFQLHVSFIEILKEEVLDLLDSSvpfnrlang 177
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLG--PDPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPV--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 178 tpgkvvlSKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKISSI 257
Cdd:cd00106 149 -------PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 258 SVVKDtvdedmgeeyccAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRkegaHVPYRDSKL 337
Cdd:cd00106 222 ESVTS------------SKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK----HIPYRDSKL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1063715979 338 TRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRAR 378
Cdd:cd00106 286 TRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
26-380 |
1.06e-109 |
|
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: 344.33 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSV-------------------SPVTPQVQMGTHP----FTFDHVYGSNGSPSSLmFE 82
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfdpkdeedgffhGGSNNRDRRKRRNkelkYVFDRVFDETSTQEEV-YE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 83 ECVAPLVDGLFHGYNATVLAYGQTGSGKTYTMgtgikDGTKN--GLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEE 160
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTM-----LGTPQepGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 161 VLDLLDSSvpfnrlangtpgkvvlSKsPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRS 240
Cdd:cd01370 156 IRDLLNPS----------------SG-PLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 241 HAIFTITLEQMRKISSISvvkdtvdedmgEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGD 320
Cdd:cd01370 219 HAVLQITVRQQDKTASIN-----------QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 321 EKRRKegAHVPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNI 380
Cdd:cd01370 288 PGKKN--KHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
26-387 |
2.70e-105 |
|
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: 333.55 E-value: 2.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSVSPVTPQVQMG-------------THPFTFDHVYGSNGSPSS------LMFEECVA 86
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPkqadknnkatrevPKSFSFDYSYWSHDSEDPnyasqeQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 87 PLVDGLFHGYNATVLAYGQTGSGKTYTMgTGIKDGtkNGLIPQVMSALFNKIDSVKHQ-MGFQLHVSFIEILKEEVLDLL 165
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTM-MGTQEQ--PGIIPRLCEDLFSRIADTTNQnMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 166 DSSVPFNrlangtpgkvvlsKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFT 245
Cdd:cd01365 160 NPKPKKN-------------KGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 246 ITLEQmrkissisvvKDTVDEDMGEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRK 325
Cdd:cd01365 227 IVLTQ----------KRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGK 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 326 EGAH---VPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNKPVAN 387
Cdd:cd01365 297 SKKKssfIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
25-380 |
1.10e-103 |
|
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: 328.27 E-value: 1.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 25 CVKVAVNVRPLIGDEVTQGCRECVSVSPVTPQVQMgTHP----------FTFDHVYGSNgSPSSLMFEECVAPLVDGLFH 94
Cdd:cd01371 2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSV-RNPkataneppktFTFDAVFDPN-SKQLDVYDETARPLVDSVLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 95 GYNATVLAYGQTGSGKTYTMGTGIKDGTKNGLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEEVLDLLdssvpfnrl 174
Cdd:cd01371 80 GYNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLL--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 175 angtpGKVVLSKSPVqiRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKI 254
Cdd:cd01371 151 -----GKDQTKRLEL--KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 255 ssisvvkdtvdEDMGEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKrrkeGAHVPYRD 334
Cdd:cd01371 224 -----------EDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGK----STHIPYRD 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1063715979 335 SKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNI 380
Cdd:cd01371 289 SKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
26-389 |
9.14e-99 |
|
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: 315.80 E-value: 9.14e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSVSPV---------TPQVQMGTHPFTFDHVYGSnGSPSSLMFEECVAPLVDGLFHGY 96
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVrkevsvrtgGLADKSSTKTYTFDMVFGP-EAKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 97 NATVLAYGQTGSGKTYTM--------GTGIKDGTKNGLIPQVMSALFNKIDSVKHQmgFQLHVSFIEILKEEVLDLLDSS 168
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMegdrspneEYTWELDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 169 VPFNRlangtpgkvvlsksPVQIRESPNGV--ITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTI 246
Cdd:cd01364 161 SDVSE--------------RLRMFDDPRNKrgVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 247 TLEQmrKISSIsvvkdtvdedMGEE-YCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKrrk 325
Cdd:cd01364 227 TIHI--KETTI----------DGEElVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERA--- 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063715979 326 egAHVPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNKPVANKD 389
Cdd:cd01364 292 --PHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
24-380 |
1.54e-97 |
|
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: 311.57 E-value: 1.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 24 CCVKVAVNVRPLIGDEVTQGCRECVSVSP---VTPQVQMGTHPFTFDHVYGSNGSPSSLmFEECVAPLVDGLFHGYNATV 100
Cdd:cd01369 2 CNIKVVCRFRPLNELEVLQGSKSIVKFDPedtVVIATSETGKTFSFDRVFDPNTTQEDV-YNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 101 LAYGQTGSGKTYTMGTGIKDGTKNGLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEEVLDLLDssvpfnrlangtpg 180
Cdd:cd01369 81 FAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLD-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 181 kvvLSKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQmrkissisvv 260
Cdd:cd01369 147 ---VSKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ---------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 261 KDTVDEDMGEeyccAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRrkegAHVPYRDSKLTRL 340
Cdd:cd01369 214 ENVETEKKKS----GKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK----THIPYRDSKLTRI 285
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1063715979 341 LQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNI 380
Cdd:cd01369 286 LQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
26-380 |
9.37e-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: 309.26 E-value: 9.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSVSPVT-PQVQMGTHPFTFDHVYGSNgSPSSLMFEECVAPLVDGLFHGYNATVLAYG 104
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDTiYLVEPPSTSFTFDHVFGGD-STNREVYELIAKPVVKSALEGYNGTIFAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 105 QTGSGKTYTMgTGikDGTKNGLIPQVMSALFNKIDSVKHQmGFQLHVSFIEILKEEVLDLLDssvpfnrlangtPGKVVL 184
Cdd:cd01374 81 QTSSGKTFTM-SG--DEDEPGIIPLAIRDIFSKIQDTPDR-EFLLRVSYLEIYNEKINDLLS------------PTSQNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 185 skspvQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEqmrkiSSIsvvkdtV 264
Cdd:cd01374 145 -----KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIE-----SSE------R 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 265 DEDMGEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRKegaHVPYRDSKLTRLLQDS 344
Cdd:cd01374 209 GELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG---HIPYRDSKLTRILQPS 285
|
330 340 350
....*....|....*....|....*....|....*.
gi 1063715979 345 LGGNSKTVMIACISPADINAEETLNTLKYANRARNI 380
Cdd:cd01374 286 LGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
32-382 |
1.78e-94 |
|
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: 303.36 E-value: 1.78e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 32 VRPLIGDEVTQGCrECVSVSPVTPQV------QMGTHPFTFDHVYGSNGSpSSLMFEEcVAPLVDGLFHGYNATVLAYGQ 105
Cdd:cd01366 10 VRPLLPSEENEDT-SHITFPDEDGQTieltsiGAKQKEFSFDKVFDPEAS-QEDVFEE-VSPLVQSALDGYNVCIFAYGQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 106 TGSGKTYTMgTGIKDGtkNGLIPQVMSALFNKIDSVKHQMG-FQLHVSFIEILKEEVLDLLdssvpfnrlANGTpgkvvL 184
Cdd:cd01366 87 TGSGKTYTM-EGPPES--PGIIPRALQELFNTIKELKEKGWsYTIKASMLEIYNETIRDLL---------APGN-----A 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 185 SKSPVQIR-ESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRkissisvvkdt 263
Cdd:cd01366 150 PQKKLEIRhDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRN----------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 264 vdeDMGEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALgdekRRKEGaHVPYRDSKLTRLLQD 343
Cdd:cd01366 219 ---LQTGEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL----RQKQS-HIPYRNSKLTYLLQD 290
|
330 340 350
....*....|....*....|....*....|....*....
gi 1063715979 344 SLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQN 382
Cdd:cd01366 291 SLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
26-389 |
3.30e-87 |
|
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: 284.40 E-value: 3.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSVSPVTPQVQMGTHP--FTFDHVYGSNGSPSSLmFEECVAPLVDGLFHGYNATVLAY 103
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKPPktFTFDHVADSNTNQESV-FQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 104 GQTGSGKTYTMGTGIKDGTKN-----GLIPQVMSALFNKIDSVKHQMG----FQLHVSFIEILKEEVLDLLDSSvpfnrl 174
Cdd:cd01373 82 GQTGSGKTYTMWGPSESDNESphglrGVIPRIFEYLFSLIQREKEKAGegksFLCKCSFLEIYNEQIYDLLDPA------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 175 angtpgkvvlsKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKI 254
Cdd:cd01373 156 -----------SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 255 SSISVVKdtvdedmgeeycCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRKEgAHVPYRD 334
Cdd:cd01373 225 ACFVNIR------------TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQ-RHVCYRD 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 335 SKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNKPVANKD 389
Cdd:cd01373 292 SKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
64-519 |
3.40e-85 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 286.64 E-value: 3.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 64 FTFDHVYGSNgSPSSLMFEECVAPLVDGLFHGYNATVLAYGQTGSGKTYTMgTGIKDGTknGLIPQVMSALFNKIDSVKH 143
Cdd:COG5059 58 YAFDKVFGPS-ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM-SGTEEEP--GIIPLSLKELFSKLEDLSM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 144 QMGFQLHVSFIEILKEEVLDLLDSSVPfnrlangtpgkvvlsksPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGS 223
Cdd:COG5059 134 TKDFAVSISYLEIYNEKIYDLLSPNEE-----------------SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 224 LTRATGSTNMNNESSRSHAIFTITLEQmrkissisvvkdtVDEDMGEeYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIH 303
Cdd:COG5059 197 KNRTTASTEINDESSRSHSIFQIELAS-------------KNKVSGT-SETSKLSLVDLAGSERAARTGNRGTRLKEGAS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 304 INRGLLALGNVISALGDEKRRKegaHVPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNK 383
Cdd:COG5059 263 INKSLLTLGNVINALGDKKKSG---HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 384 PVANkdlicSEMQKMRQELQYLQATLCARGATSSEEVqvmREKIMKLESANEELSRELHIYRSKRVTLDyCNIDAQEDGV 463
Cdd:COG5059 340 IQVN-----SSSDSSREIEEIKFDLSEDRSEIEILVF---REQSQLSQSSLSGIFAYMQSLKKETETLK-SRIDLIMKSI 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 464 IF--------SKDDGLKR---------GFESMDSDYEMSEATSD--IGAAEEWEHALRQNsMGKELNELSKRLEE 519
Cdd:COG5059 411 ISgtferkklLKEEGWKYkstlqflriEIDRLLLLREEELSKKKtkIHKLNKLRHDLSSL-LSSIPEETSDRVES 484
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
26-376 |
5.76e-77 |
|
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: 255.68 E-value: 5.76e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDE--------VTQGCRECVSVSPVTPQVQMGT----HPFTFDHVYGSNGSPSSLmFEECVAPLVDGLF 93
Cdd:cd01367 2 IKVCVRKRPLNKKEvakkeidvVSVPSKLTLIVHEPKLKVDLTKyienHTFRFDYVFDESSSNETV-YRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 94 HGYNATVLAYGQTGSGKTYTMGTGIKDGTKNGLIPQVMSA-LFNKIDSVKHQMGFQLHVSFIEILKEEVLDLLDSsvpfn 172
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARdVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLNR----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 173 rlangtpgkvvlsKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLeqmr 252
Cdd:cd01367 156 -------------KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 253 kissisvvKDTVDEDMGeeyccAKLHLVDLAGSER-AKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKrrkegAHVP 331
Cdd:cd01367 219 --------RDRGTNKLH-----GKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK-----AHIP 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1063715979 332 YRDSKLTRLLQDSL-GGNSKTVMIACISPADINAEETLNTLKYANR 376
Cdd:cd01367 281 FRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
26-374 |
1.27e-73 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 247.31 E-value: 1.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVT---QGCRECVSVSPVTPQVQMG-------------THPFTFDHVYGSNGSPSSLmFEECVAPLV 89
Cdd:cd01368 3 VKVYLRVRPLSKDELEsedEGCIEVINSTTVVLHPPKGsaanksernggqkETKFSFSKVFGPNTTQKEF-FQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 90 DGLFHGYNATVLAYGQTGSGKTYTMGTGIKDGtknGLIPQVMSALFNKIDsvkhqmGFQLHVSFIEILKEEVLDLLDSSv 169
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG---GILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 170 pfnrlangtPGKVVLSKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLE 249
Cdd:cd01368 152 ---------PSSPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 250 QMRKISSISVVKDTvdedmgEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRKEGAH 329
Cdd:cd01368 223 QAPGDSDGDVDQDK------DQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKM 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1063715979 330 VPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYA 374
Cdd:cd01368 297 VPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
26-378 |
8.78e-72 |
|
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: 241.25 E-value: 8.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECV------SVSPVTPQVQMGTHPFTFDHVYGSNGSPSSLmFEECVAPLVDGLFHGYNAT 99
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVsgidscSVELADPRNHGETLKYQFDAFYGEESTQEDI-YAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 100 VLAYGQTGSGKTYTMgtgIKDGTKNGLIPQVMSALFNKIDSVKHQMGFQlhVSFIEILKEEVLDLLDSSvpfnrlangtp 179
Cdd:cd01376 81 VFAYGSTGAGKTFTM---LGSPEQPGLMPLTVMDLLQMTRKEAWALSFT--MSYLEIYQEKILDLLEPA----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 180 gkvvlsKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRKISSISV 259
Cdd:cd01376 145 ------SKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 260 VKdtvdedmgeeyccAKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRkegahVPYRDSKLTR 339
Cdd:cd01376 219 RT-------------GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR-----IPYRDSKLTR 280
|
330 340 350
....*....|....*....|....*....|....*....
gi 1063715979 340 LLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRAR 378
Cdd:cd01376 281 LLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
64-378 |
1.21e-68 |
|
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: 233.24 E-value: 1.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 64 FTFDHVYgsNGSPSSLMFEECVAPLVDGLFHGYNATVLAYGQTGSGKTYTMGTGIKDGTKNGLIPQVMSALFNKIDSVKH 143
Cdd:cd01375 50 FKFDGVL--HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 144 QMgFQLHVSFIEILKEEVLDLLDSsvpfnrlangTPgKVVLSKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGS 223
Cdd:cd01375 128 KA-YTVHVSYLEIYNEQLYDLLST----------LP-YVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 224 LTRATGSTNMNNESSRSHAIFTITLE-QMRKISSisvvkdtvdedmgEEYCCAKLHLVDLAGSERAKRTGSGGVRLKEGI 302
Cdd:cd01375 196 TNRIIASHTMNKNSSRSHCIFTIHLEaHSRTLSS-------------EKYITSKLNLVDLAGSERLSKTGVEGQVLKEAT 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063715979 303 HINRGLLALGNVISALGDEKRrkegAHVPYRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRAR 378
Cdd:cd01375 263 YINKSLSFLEQAIIALSDKDR----THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
26-407 |
1.53e-61 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 229.82 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 26 VKVAVNVRPLIGDEVTQGCRECVSVSPVTPQVQMgthpFTFDHVyGSNGSPSSLMFEECVAPLVDGLFHGYNATVLAYGQ 105
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGEMIVQKMSNDSLTINGQT----FTFDSI-ADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 106 TGSGKTYTM---GTGIKD----GTKNGLIPQVMSALFNKI--DSVKH---QMGFQLHVSFIEILKEEVLDLLDSSvpfnr 173
Cdd:PLN03188 175 TGSGKTYTMwgpANGLLEehlsGDQQGLTPRVFERLFARIneEQIKHadrQLKYQCRCSFLEIYNEQITDLLDPS----- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 174 langtpgkvvlsKSPVQIRESPNGVITLSGATEVPIATKEEMASCLEQGSLTRATGSTNMNNESSRSHAIFTITLEQMRK 253
Cdd:PLN03188 250 ------------QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 254 ISS--ISVVKDTvdedmgeeyccaKLHLVDLAGSERAKRTGSGGVRLKEGIHINRGLLALGNVISALGDEKRRKEGAHVP 331
Cdd:PLN03188 318 SVAdgLSSFKTS------------RINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 332 YRDSKLTRLLQDSLGGNSKTVMIACISPADINAEETLNTLKYANRARNIQNKPVANKDL------ICSEMQKMRQELQYL 405
Cdd:PLN03188 386 YRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMqddvnfLREVIRQLRDELQRV 465
|
..
gi 1063715979 406 QA 407
Cdd:PLN03188 466 KA 467
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
65-359 |
3.84e-15 |
|
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: 74.30 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 65 TFDHVYGSNGSPSSlMFEECvAPLVDGLFHGYN-ATVLAYGQTGSGKTYTMgtgikdgtkNGLIPQVMSALFNKIDSVKH 143
Cdd:cd01363 21 VFYRGFRRSESQPH-VFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------KGVIPYLASVAFNGINKGET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 144 QMGFQLHVSFIEiLKEEVLDLLDSSVpfnrlANGtpgkvvlskspvqirespngvitlsgatevpiatkeemascleqgs 223
Cdd:cd01363 90 EGWVYLTEITVT-LEDQILQANPILE-----AFG---------------------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 224 ltraTGSTNMNNESSRSHAIFTItleqmrkissisvvkdtvdedmgeeyccaklhLVDLAGSERakrtgsggvrlkegih 303
Cdd:cd01363 118 ----NAKTTRNENSSRFGKFIEI--------------------------------LLDIAGFEI---------------- 145
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063715979 304 INRGLLALGNVISAlgdekrrkegahvpyrdskltrllqdslggnSKTVMIACISP 359
Cdd:cd01363 146 INESLNTLMNVLRA-------------------------------TRPHFVRCISP 170
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
24-165 |
7.80e-12 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 64.16 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 24 CCVKVAVNVRPLIGDEVtqgCRECVSVSPVTPQVQMGTHPFTFDHVYGSNgSPSSLMFEECVApLVDGLFHGYNATVLAY 103
Cdd:pfam16796 20 GNIRVFARVRPELLSEA---QIDYPDETSSDGKIGSKNKSFSFDRVFPPE-SEQEDVFQEISQ-LVQSCLDGYNVCIFAY 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063715979 104 GQTGSGKTytmgtgikdgtkNGLIPQVMSALFNKIDSVKHQMGFQLHVSFIEILKEEVLDLL 165
Cdd:pfam16796 95 GQTGSGSN------------DGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
515-738 |
1.64e-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: 58.60 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 515 KRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEKRTVQ---------DERDMLLAEVEELAASSDR------QAQVARD 579
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaekarqaemDRQAAIYAEQERMAMERERelerirQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 580 NHAHKLKALETQILNLKKKQENQVEvlkQKQKSEdaakRLKTEIQCIKAQKVQ---LQQKMKQEAEQFRQWKASQE---K 653
Cdd:pfam17380 362 LERIRQEEIAMEISRMRELERLQME---RQQKNE----RVRQELEAARKVKILeeeRQRKIQQQKVEMEQIRAEQEearQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 654 ELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKSSPHDIS--VIANGQPPSRQT--NEKSL 729
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRrkILEKELEERKQAmiEEERK 514
|
....*....
gi 1063715979 730 RKWLDNELE 738
Cdd:pfam17380 515 RKLLEKEME 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
483-762 |
3.29e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 483 EMSEATSDIGAAEEwehalRQNSMGKELNELSKRLEEKESEMrvcgIGTETIRQHFEKKMMELEKEKRTVQDERDMLLAE 562
Cdd:COG1196 296 ELARLEQDIARLEE-----RRRELEERLEELEEELAELEEEL----EELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 563 VEELAASSDRQAQvARDNHAHKLKALETQILNLKKKQEnqvEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAE 642
Cdd:COG1196 367 LLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLE---ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 643 QFRQwkasQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKSSPHDISVIAngqppsr 722
Cdd:COG1196 443 ALEE----AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK------- 511
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063715979 723 qtnEKSLRKWLDNELEVMAKVHQVRFQYEKQIQVRAALAV 762
Cdd:COG1196 512 ---AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
508-722 |
5.65e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEM-----RVCGIGTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQVARDNHA 582
Cdd:COG3206 182 EQLPELRKELEEAEAALeefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 583 H--------KLKALETQILNLKKK-QENQVEVLKQKQKSEDAAKRLKTEIQcikaqkvQLQQKMKQEAEQFRQWKASQEK 653
Cdd:COG3206 262 SpviqqlraQLAELEAELAELSARyTPNHPDVIALRAQIAALRAQLQQEAQ-------RILASLEAELEALQAREASLQA 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063715979 654 ELLQLKKEGRKTEHERLKLEALNRRqkmvLQRKTEEAAMATKRLKELLEARKSSPHDISVIANGQPPSR 722
Cdd:COG3206 335 QLAQLEARLAELPELEAELRRLERE----VEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLK 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
508-772 |
1.03e-06 |
|
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: 53.14 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEmrvcgigTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRqAQVARDNHAHKLKA 587
Cdd:TIGR02168 680 EELEEKIEELEEKIAE-------LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 588 LETQILNLKKKQEnqvEVLKQKQKSEDAAKRLKTEIQcikaqkvQLQQKMKQEAEQFRQWKASQEKEllqlkkegrKTEH 667
Cdd:TIGR02168 752 LSKELTELEAEIE---ELEERLEEAEEELAEAEAEIE-------ELEAQIEQLKEELKALREALDEL---------RAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 668 ERLKLEALNRRQKmvLQRKTEEAAMATKRLKELLEARKSSPHDISvIANGQPPSRQTNEKSLRKWLDNELEVMAKV---- 743
Cdd:TIGR02168 813 TLLNEEAANLRER--LESLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALLNERASLeeal 889
|
250 260
....*....|....*....|....*....
gi 1063715979 744 HQVRFQYEKQIQVRAALAVELTSLRQEME 772
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELE 918
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
393-704 |
1.09e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 393 SEMQKMRQELQYLQATLCARGATSSEEVQVMREKIMKLESANEELSRELHIYRSK--RVTLDYCNIDAQEDGVifskddg 470
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARieELEEDLHKLEEALNDL------- 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 471 lkrgfESMDSDYEMSEATSDIGAAEEwEHA---LRQNSMGKELNELSKRLEEKESEmrvcgigtetiRQHFEKKMMELEK 547
Cdd:TIGR02169 785 -----EARLSHSRIPEIQAELSKLEE-EVSrieARLREIEQKLNRLTLEKEYLEKE-----------IQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 548 EKRTVQDERDMLLAEVEELaassdrQAQVARdnHAHKLKALETQILNLKKKQENQvevlkQKQKSEdaakrLKTEIQCIK 627
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEEL------EEELEE--LEAALRDLESRLGDLKKERDEL-----EAQLRE-----LERKIEELE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 628 AQKVQLQQKMKQEAEQfRQWKASQEKELLQLKKEG----------RKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRL 697
Cdd:TIGR02169 910 AQIEKKRKRLSELKAK-LEALEEELSEIEDPKGEDeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL 988
|
....*..
gi 1063715979 698 KELLEAR 704
Cdd:TIGR02169 989 DELKEKR 995
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
496-705 |
1.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 496 EWEHA-LRQNSMGKELNELSKRLEEKESEMRVCGIGTETIRQHFE-----------------KKMMELEKEKRTVQDERD 557
Cdd:COG1196 233 KLRELeAELEELEAELEELEAELEELEAELAELEAELEELRLELEeleleleeaqaeeyellAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 558 MLLAEVEELAASSDRQAQVARDNHAHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKM 637
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 638 KQEAEQfrqwkASQEKELLQLKK--EGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARK 705
Cdd:COG1196 393 RAAAEL-----AAQLEELEEAEEalLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
512-705 |
1.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 512 ELSKRLEEKESEMRVcgigteTIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQvardnhahklkALETQ 591
Cdd:COG1196 217 ELKEELKELEAELLL------LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-----------ELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 592 ILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLK 671
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190
....*....|....*....|....*....|....
gi 1063715979 672 LEALNRRQKMVLQRKTEEAAMATKRLKELLEARK 705
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
418-901 |
2.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 418 EEVQVMREKIMKLESA-NEELSRELHIYRSKRVTLDYCNIDAQEDgvifSKDDGLKRGFESMDSDyEMSEAtSDIGAAEE 496
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEA----RKADELKKAEEKKKAD-EAKKA-EEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 497 wehALRQNSMGKELNELSKRLEEKESEmrvcgigTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQV 576
Cdd:PTZ00121 1307 ---AKKKAEEAKKADEAKKKAEEAKKK-------ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 577 ARDNHAHKLKALETQILN-LKKKQE---NQVEVLKQKQKSEDAAKRLKTeiqciKAQKVQLQQKMKQEAEQFRQW----- 647
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADeAKKKAEedkKKADELKKAAAAKKKADEAKK-----KAEEKKKADEAKKKAEEAKKAdeakk 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 648 KASQEKELLQLKKEGR-KTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKSSPHdisviANGQPPSRQTNE 726
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-----AKKAEEAKKADE 1526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 727 ksLRKWLD-NELEVMAKVHQVRfqyeKQIQVRAALAVELTSLRQEMEFPSNSHQEKNGQFRFLSPNTRLERiASLESMLD 805
Cdd:PTZ00121 1527 --AKKAEEaKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMK 1599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 806 VSSNALTAMGSQLSEAEErehslhAKPRWNHIQSMTDAKYLLQYVFDSTAEARSKIWE---KDRDIKEKKEQLNDLLCLL 882
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEE------AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEED 1673
|
490
....*....|....*....
gi 1063715979 883 QLTEVQNREILKEKKTREQ 901
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAE 1692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
540-805 |
2.57e-06 |
|
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: 51.60 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 540 KKMMELEKEKRTVQdeRDMLLAEVEELAASSDR------QAQVARDNHAHKLKALETQILNLKKKQ---ENQVEVLKQKQ 610
Cdd:TIGR02168 213 ERYKELKAELRELE--LALLVLRLEELREELEElqeelkEAEEELEELTAELQELEEKLEELRLEVselEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 611 KSEDAAK-RLKTEIQCIKAQKVQLQQKMKQEAEQFRQWK----------ASQEKELLQLKK--EGRKTEHERLKLEALNR 677
Cdd:TIGR02168 291 YALANEIsRLEQQKQILRERLANLERQLEELEAQLEELEskldelaeelAELEEKLEELKEelESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 678 RQKMVLQRK------------TEEAAMATKRLkELLEARKSSphdisvIANGQPPSRQTNEKSLRKWLDNEL-EVMAKVH 744
Cdd:TIGR02168 371 ESRLEELEEqletlrskvaqlELQIASLNNEI-ERLEARLER------LEDRRERLQQEIEELLKKLEEAELkELQAELE 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063715979 745 QVRFQYEKQIQVRAALAVELTSLRQEMEFPSNSHQEKNGQFRFLSpntrlERIASLESMLD 805
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ-----ARLDSLERLQE 499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
467-705 |
3.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 467 KDDGLKRGFESMDSDYEMSEATSDIGAAEEWEHA--LRQNSMGKELNELSKRLEEKES-EMRvcgiGTETIRQHFEKKMM 543
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeAKKAEEAKKADEAKKAEEKKKAdELK----KAEELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 544 ElekEKRTVQDERDMLLAEVEELaassdRQAQVARDNHAHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEI 623
Cdd:PTZ00121 1567 E---EAKKAEEDKNMALRKAEEA-----KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 624 QCIKAQKVQLQQKMKQE-------AEQFRQWKASQEKELLQLKK--EGRKTEHERLKLEALNRRQKMVLQRKTEEAAMAT 694
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAeeenkikAAEEAKKAEEDKKKAEEAKKaeEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
250
....*....|.
gi 1063715979 695 KRLKELLEARK 705
Cdd:PTZ00121 1719 EELKKAEEENK 1729
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
494-735 |
3.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 494 AEEWEHALRQNSMGKELNELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEK----RTVQDERDMLLAEVEELAAS 569
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEE 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 570 SDRQAQVARDNHAHKLKALEtqilnLKKKQEnqvevlKQKQKSEDAAKRLKTEIQciKAQKVQLQQKMKQEAEQFRQWKA 649
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAE-----EAKKAE------EDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEELKKKEA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 650 SQEKELLQLKK--EGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLK--ELLEARKSSPHDISVIANG----QPPS 721
Cdd:PTZ00121 1713 EEKKKAEELKKaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKkeEEKKAEEIRKEKEAVIEEEldeeDEKR 1792
|
250
....*....|....
gi 1063715979 722 RQTNEKSLRKWLDN 735
Cdd:PTZ00121 1793 RMEVDKKIKDIFDN 1806
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
394-717 |
4.42e-06 |
|
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: 50.83 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 394 EMQKMRQELQylqatlcARGATSSEEVQVMREKIMKLESANEELSRELHIYRSKRVTLDycnidaQEDGVIFSKDDGLKR 473
Cdd:TIGR02168 250 EAEEELEELT-------AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE------QQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 474 GFESMDSDYEMSEATSDIGAAEEWEHALRQNSMGKELNELSKRLEEKESEMrvcgigtetirQHFEKKMMELEKEKRTVQ 553
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-----------EELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 554 DERDMLLAEVEELAAssdrqaqvardnhahKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCikAQKVQL 633
Cdd:TIGR02168 386 SKVAQLELQIASLNN---------------EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 634 QQKMKQEAEQFRQWKASQEKELLQLKKEGRKTEHErlkLEALNRRQKMvLQRKTEEAAMATKRLKELLEARKSSPHDISV 713
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERE---LAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
....
gi 1063715979 714 IANG 717
Cdd:TIGR02168 525 LSEL 528
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
508-674 |
5.00e-06 |
|
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: 48.77 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEMRvcgiGTETIRQHFEKKMMELEKEKRTVQDErdmlLAEVEELAASSDRQAQVARDNHAhkLKA 587
Cdd:COG1579 24 HRLKELPAELAELEDELA----ALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNKE--YEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 588 LETQILNLKKKQEnqvevlkqkqKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKKEGRKTEH 667
Cdd:COG1579 94 LQKEIESLKRRIS----------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 1063715979 668 ERLKLEA 674
Cdd:COG1579 164 EREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
483-680 |
7.80e-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: 49.38 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 483 EMSEATSDIGAAEEWEHALRQ--NSMGKELNELSKRLEEKESEMRVcgigTETIRQHFEKKMMELEKEKRTVQDERDMLL 560
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKeeKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 561 AEVEELAA---------------SSDRQAQVARDNHAHK--LKALETQILNLKKKQEnqvEVLKQKQKSEDAAKRLKTEI 623
Cdd:COG4942 104 EELAELLRalyrlgrqpplalllSPEDFLDAVRRLQYLKylAPARREQAEELRADLA---ELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 624 QCIKAQKVQLQQKMKQEAE---QFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQK 680
Cdd:COG4942 181 AELEEERAALEALKAERQKllaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
508-701 |
1.80e-05 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 46.98 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKE---SEMRVcgigtetIRQHFEKK----MMELEKEKRTVQDERDMLLAEVEELAASsdrqaqvardn 580
Cdd:pfam05010 22 LEINELKAKYEELRrenLEMRK-------IVAEFEKTiaqmIEEKQKQKELEHAEIQKVLEEKDQALAD----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 581 hahkLKALETQILNLKKKQENQVEVLKQKQKSEDAAK--------RLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQE 652
Cdd:pfam05010 84 ----LNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKkcaqdylaRIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063715979 653 KELLQLKKEGRKtehERLKLEALNRRqkmvLQRKTEEAAMATKRLKELL 701
Cdd:pfam05010 160 AETAALQASLRK---EQMKVQSLERQ----LEQKTKENEELTKICDELI 201
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
508-707 |
2.06e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEE--KESEMRvcgiGTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEElaASSDRQAQVARDNHAHKl 585
Cdd:PTZ00121 1230 KKAEEAKKDAEEakKAEEER----NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK--AEEKKKADEAKKAEEKK- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 586 KALEtqilnLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEK-ELLQLKKEGRK 664
Cdd:PTZ00121 1303 KADE-----AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKaEAAEKKKEEAK 1377
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063715979 665 TEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKSS 707
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA 1420
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
499-670 |
5.60e-05 |
|
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: 47.25 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 499 HALRQNSMGKELNELSKRLEEKESemrvcgigTETIRQHFEKKMmeleKEKRTVQDERDMLLAEVEELAASSDRQAQVAR 578
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRI----GQQLDAAEELEELLAELEAQLEELEEQAAEAV 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 579 DNHA---HKLKALETQILNLKKKQENQVevlkqkqKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQwkASQEKEL 655
Cdd:COG3096 578 EQRSelrQQLEQLRARIKELAARAPAWL-------AAQDALERLREQSGEALADSQEVTAAMQQLLERERE--ATVERDE 648
|
170
....*....|....*
gi 1063715979 656 LQLKKEGRKTEHERL 670
Cdd:COG3096 649 LAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
508-716 |
9.34e-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: 45.91 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEMRvcgiGTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAassdRQAQVARDNHAHKLKA 587
Cdd:COG4942 34 QEIAELEKELAALKKEEK----ALLKQLAALERRIAALARRIRALEQELAALEAELAELE----KEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 588 LETQILNL-KKKQENQVEVLKQKQKSEDAAKRL----------KTEIQCIKAQKVQLQQK------MKQEAEQFRQWKAS 650
Cdd:COG4942 106 LAELLRALyRLGRQPPLALLLSPEDFLDAVRRLqylkylaparREQAEELRADLAELAALraeleaERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063715979 651 QEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKSSPHDISVIAN 716
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
479-694 |
9.55e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 479 DSDYEMSEATSDIGAAEEWEHALRQ--NSMGKELNELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEKRTVQdER 556
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAelEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 557 DMLLAEVEELAASSDrqaqvardnhahkLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQK 636
Cdd:COG3883 99 GGSVSYLDVLLGSES-------------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063715979 637 MKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMAT 694
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
508-714 |
1.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEMRVCGIGTETIrQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSdrqaqvardnhahkLKA 587
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELGFES--------------VEE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 588 LETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLqQKMKQEAEQFRqwkasqeKELLQLKKEGRKTEH 667
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEELR-------KELEELEKKYSEEEY 661
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 668 ERLKLEALN--------RRQKMVLQRKTEEAAMATKRLKELLEARKSSPHDISVI 714
Cdd:PRK03918 662 EELREEYLElsrelaglRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
508-678 |
2.08e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEMRVcgIGTETIRQHFE-----KKMMELEKEKRTVQDERDMLLAEVEELaassdrqaQVARDNHA 582
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDK--FLTEIKKKEKEleklnNKYNDLKKQKEELENELNLLEKEKLNI--------QKNIDKIK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 583 HKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKKEG 662
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
170
....*....|....*.
gi 1063715979 663 RKTEHERLKLEALNRR 678
Cdd:TIGR04523 274 KELEQNNKKIKELEKQ 289
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
482-706 |
2.56e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 482 YEMSEATSDIGAAEEWEHALRQNSMGKELNELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEK--EKRTVQDERDml 559
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKK-- 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 560 lAEVEELAASSDRQAQVARDNHAHKLKALETQ--ILNLKKKQENQVEVLK-QKQKSEDAAKRLKTEIQCIKAQKVQLQQK 636
Cdd:PTZ00121 1298 -AEEKKKADEAKKKAEEAKKADEAKKKAEEAKkkADAAKKKAEEAKKAAEaAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 637 MKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKS 706
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
389-823 |
3.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 389 DLICSEMQKMRQELQYLQatlcargatssEEVQVMREKIMKLESANEELSRELHIYRSKRVTL--------DYCNIDAQE 460
Cdd:PRK02224 240 DEVLEEHEERREELETLE-----------AEIEDLRETIAETEREREELAEEVRDLRERLEELeeerddllAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 461 DGVIFSKDDGLKRGFESMDSDYEmsEATSDIGAAEEWEHALRQNSmgKELNELSKRLEEKESEMRVCGIGTETIRQHFEK 540
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLE--ECRVAAQAHNEEAESLREDA--DDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 541 KMMELEKEKRTVQDERDMLLAEVEELAASSDrQAQVARDNHAHKLKALETQILNLKKK-QENQ----------------- 602
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERvEEAEalleagkcpecgqpveg 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 603 ---VEVLKQKqksEDAAKRLKTEIQCIKAQKVQLQQKMKQ-----EAEQFRQWKASQEKELLQLKKEGRKT-EHERLKLE 673
Cdd:PRK02224 464 sphVETIEED---RERVEELEAELEDLEEEVEEVEERLERaedlvEAEDRIERLEERREDLEELIAERRETiEEKRERAE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 674 ALNrrqkmvlQRKTE-EAAMATKRlKELLEARKSSPHDISVIAngqppsrQTNEKslRKWLDNELEVMAKVhqvrfqyEK 752
Cdd:PRK02224 541 ELR-------ERAAElEAEAEEKR-EAAAEAEEEAEEAREEVA-------ELNSK--LAELKERIESLERI-------RT 596
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063715979 753 QIQVRAALAVELTSLRQEMEfpsnSHQEKNGQFR-FLSpnTRLERIASLESMLDvsSNALTAMGSQLSEAEE 823
Cdd:PRK02224 597 LLAAIADAEDEIERLREKRE----ALAELNDERReRLA--EKRERKRELEAEFD--EARIEEAREDKERAEE 660
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
471-698 |
4.26e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 471 LKRGFESMDSDYEMSEATSDIGaaEEWehALRQNSMGKELNELSKRLEEKESEMRVCGIGTETIR----QHFEKKMMELE 546
Cdd:pfam02029 76 QKRLQEALERQKEFDPTIADEK--ESV--AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRekeyQENKWSTEVRQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 547 KEKRTVQDERDMLLAEVEELAASSDRQAQVARDNHAHKLKALETQILNLKKKQENQ--------VEVLKQKQK------- 611
Cdd:pfam02029 152 AEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVksqngeeeVTKLKVTTKrrqggls 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 612 -----SEDAAKRLKTEiQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKK---EGRKT-----------EHER-LK 671
Cdd:pfam02029 232 qsqerEEEAEVFLEAE-QKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKkreERRKLleeeeqrrkqeEAERkLR 310
|
250 260
....*....|....*....|....*..
gi 1063715979 672 LEALNRRQKMVLQRKTEEAamATKRLK 698
Cdd:pfam02029 311 EEEEKRRMKEEIERRRAEA--AEKRQK 335
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
547-702 |
4.42e-04 |
|
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: 44.17 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 547 KEKRTVQDERDMLLAEVEELAASSDR-QAQVArdnhahklkalETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQC 625
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRlRAERA-----------EMRRLEVERKRREQEEQRRLQQEQLERAEKMREELEL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 626 --------IKAQKVQL----QQKMKQEAEQFRQWKASQE----------KELLQLKKEGRKTEHERLklEALNRRQKMVL 683
Cdd:pfam15709 381 eqqrrfeeIRLRKQRLeeerQRQEEEERKQRLQLQAAQErarqqqeefrRKLQELQRKKQQEEAERA--EAEKQRQKELE 458
|
170
....*....|....*....
gi 1063715979 684 QRKTEEAamatKRLKELLE 702
Cdd:pfam15709 459 MQLAEEQ----KRLMEMAE 473
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
505-811 |
5.55e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 505 SMGKELNELSKRLEEKESEMRVCGIGTETIRQhfekkmmELEKEKRTVQDERDMLLAEVEELAassdrQAQVARDNHAHK 584
Cdd:pfam12128 573 SVGGELNLYGVKLDLKRIDVPEWAASEEELRE-------RLDKAEEALQSAREKQAAAEEQLV-----QANGELEKASRE 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 585 L----KALETQILNLKKKQENQVEVLKQKQKSEDAAKRLK-TEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLK 659
Cdd:pfam12128 641 EtfarTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAnERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYW 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 660 KE---GRKTEHERLKLEALNRRQkmvlQRKTEEAAMATKRLKElLEARKSSPHDISVIANGqppsRQTNEKSLRKWLDNE 736
Cdd:pfam12128 721 QVvegALDAQLALLKAAIAARRS----GAKAELKALETWYKRD-LASLGVDPDVIAKLKRE----IRTLERKIERIAVRR 791
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 737 LEVmAKVHQvrFQYEKQIQVRAALAVELTSLRQEMEfpsnshqEKNGQFRFLSPNTRLeRIASLESMLDVSSNAL 811
Cdd:pfam12128 792 QEV-LRYFD--WYQETWLQRRPRLATQLSNIERAIS-------ELQQQLARLIADTKL-RRAKLEMERKASEKQQ 855
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
509-662 |
6.74e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 509 ELNELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQVARDNHAHKLKAL 588
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063715979 589 ETQILNLKKKQEnqvevLKQKQKSEDAAKRLKTEIQCIKAQKvqlqQKMKQEAEQFRQWKASQEKELLQLKKEG 662
Cdd:PRK00409 597 QKGGYASVKAHE-----LIEARKRLNKANEKKEKKKKKQKEK----QEELKVGDEVKYLSLGQKGEVLSIPDDK 661
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
508-707 |
6.89e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNEL------SKRLEEKESEMRVCGIGT-ETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQ----- 575
Cdd:pfam07888 41 QERAELlqaqeaANRQREKEKERYKRDREQwERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEekdal 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 576 -VARDNHAHKLKALETQILNL-KKKQENQVEVLKQKQKSEDAAKRLKTEiqciKAQKVQLQQKMKQ----------EAEQ 643
Cdd:pfam07888 121 lAQRAAHEARIRELEEDIKTLtQRVLERETELERMKERAKKAGAQRKEE----EAERKQLQAKLQQteeelrslskEFQE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063715979 644 FRQWKASQEKELLQLKKEGRKTEHerlKLEALNRRQKMVLQ-----RKTEEAAMATKRLKELLEARKSS 707
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTLTQ---KLTTAHRKEAENEAlleelRSLQERLNASERKVEGLGEELSS 262
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
598-705 |
6.91e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 598 KQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQ-QKMKQEAEQFRQWKASQEKELLQLKkegRKTEHER-LKLEAL 675
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaEKAAKQAEQAAKQAEEKQKQAEEAK---AKQAAEAkAKAEAE 139
|
90 100 110
....*....|....*....|....*....|.
gi 1063715979 676 N-RRQKMVLQRKTEEAAMAtkrlKELLEARK 705
Cdd:TIGR02794 140 AeRKAKEEAAKQAEEEAKA----KAAAEAKK 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
492-680 |
8.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 492 GAAEEWEHALRQNSMGKELNELSKRLEEKESEMRVCGIGTETIRQHF-EKKMMELEKEKRTVQDERDMLLAEVEELAASS 570
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFaQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 571 D------RQAQVARDNHAH-KLKALETQILNLKKKQENQVEVLKQKQkseDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQ 643
Cdd:COG4913 319 DalreelDELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1063715979 644 FRQWKASQEKELLQLK--KEGRKTEHERLK--LEALNRRQK 680
Cdd:COG4913 396 LEEELEALEEALAEAEaaLRDLRRELRELEaeIASLERRKS 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
479-758 |
1.21e-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: 43.13 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 479 DSDYEMSEATSDIGAAEEW--EHALRQNSMGK-ELNELSKRLEEKESEMRVCgigtETIRQHFEKKMMELEKEKRTVQDE 555
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLleELNKKIKDLGEeEQLRVKEKIGELEAEIASL----ERSIAEKERELEDAEERLAKLEAE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 556 RDMLLAEVEELAASSDRQA------QVARDNHAHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKR----LKTEIQC 625
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERkrrdklTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKReineLKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 626 IKAQKVQLQQK---MKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKEL-- 700
Cdd:TIGR02169 411 LQEELQRLSEEladLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqr 490
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063715979 701 ----LEARKSSPHDISviangqpPSRQTNEKSLRKWLDNELEVMAKVHQVRFQYEKQIQVRA 758
Cdd:TIGR02169 491 elaeAEAQARASEERV-------RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAA 545
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
536-705 |
1.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 536 QHFEKKMMELEKEKRTVQDERDMLLAEVEELAAssdrqaqvardnhahKLKALETQILNLKKKQ---ENQVEVLKQKqks 612
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEA---------------RLEAAKTELEDLEKEIkrlELEIEEVEAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 613 edaAKRLKTEIQCIKAQKvQLQQKMKQEAEQFRQwKASQEKELLQL--KKEGRKTEHERLK--LEALNRRQKMVLQRKTE 688
Cdd:COG1579 75 ---IKKYEEQLGNVRNNK-EYEALQKEIESLKRR-ISDLEDEILELmeRIEELEEELAELEaeLAELEAELEEKKAELDE 149
|
170
....*....|....*..
gi 1063715979 689 EAAMATKRLKELLEARK 705
Cdd:COG1579 150 ELAELEAELEELEAERE 166
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
501-901 |
1.66e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 501 LRQNSMGKELNELSKRLEEKESEMrvcgigtetirQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQVARDN 580
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKEL-----------KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 581 HAHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTE--IQCIKAQKVQLQQKMKQEAEQFRQWKASQEK--ELL 656
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLedLLKEEKKEELEILEEEEESIELKQGKLTEEKeeLEK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 657 QLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARKS-SPHDISVIANGQPPSRQTNEKSLRKWL-- 733
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKArSGLKVLLALIKDGVGGRIISAHGRLGDlg 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 734 --------DNELEVMAKVHQVRFQYEKQIQVRAALAVELTSLRQEMEFPSNShQEKNGQFRFLSPNTRLERIASLESMLD 805
Cdd:pfam02463 536 vavenykvAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKL-KLPLKSIAVLEIDPILNLAQLDKATLE 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 806 VSSNALTAMGSQLSEAEEREHSLHAKPRWNHIQSMTDAKYLLQYVFDSTAEARSKIWEKDRDIKEKKEQLNDLLCLLQLT 885
Cdd:pfam02463 615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
410
....*....|....*.
gi 1063715979 886 EVQNREILKEKKTREQ 901
Cdd:pfam02463 695 LRRQLEIKKKEQREKE 710
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
539-781 |
1.81e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 539 EKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQVARDNHAHKLKALETQILNLKKKQENQvevlkQKQKSEDAAKR 618
Cdd:pfam15558 43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQ-----RQEKLERARQE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 619 LKTEIQCiKAQKVQLQQKMKQE-AEQFRQwkASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKrl 697
Cdd:pfam15558 118 AEQRKQC-QEQRLKEKEEELQAlREQNSL--QLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAK-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 698 KELLEARKSSPHDISVIANGQPPSRQTNEKSLRKWLDNELEVMAKVHQVRFQYEKQIQVRAALAVELT--SLRQEMEFPS 775
Cdd:pfam15558 193 AEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELAdrKIQQARQVAH 272
|
....*.
gi 1063715979 776 NSHQEK 781
Cdd:pfam15558 273 KTVQDK 278
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
481-714 |
1.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 481 DYEMSEATSDIGAAEEWEHALRQN-----SMGKELNELSKRLEEKESEMRVCGIGTETIRQHFEkKMMELEKEKRTVQDE 555
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKekeleEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 556 RDML---LAEVEELAASSDRQAQVARDNhAHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQ 632
Cdd:PRK03918 254 KRKLeekIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 633 LQQKmKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAmatKRLKELLEARKSSPHDIS 712
Cdd:PRK03918 333 LEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE---KELEELEKAKEEIEEEIS 408
|
..
gi 1063715979 713 VI 714
Cdd:PRK03918 409 KI 410
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
502-646 |
1.92e-03 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 40.36 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 502 RQNSMGKELNELSKRLEEKESEmrvcgigTETIRQHFEKkmmeLEKEKrtvqDERDMLLAEVEELAASSDRQAQVARDNH 581
Cdd:pfam16043 22 ELEKLSETTSELSERLQQRQKH-------LEALYQQIEK----LEKVK----ADKEVVEEELDEKADKEALASKVSRDQF 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 582 AHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQ 646
Cdd:pfam16043 87 DETLEELNQMLQELLDKLEGQEDAWKKALETLSEELDTKLDRLELDPLKELLERRIKALQKLLQE 151
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
483-659 |
2.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 483 EMSEATSDIGAAEEWEHALRQ-----NSMGKELNELSKRLEEKESEMRVCgigtETIRQHFE--KKMMELEKEKRTVQDE 555
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAElqeelEELEEELEELEAELEELREELEKL----EKLLQLLPlyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 556 RDMLLAEVEELAASSDRQAQvARDNHAHKLKALETQILNLKKKQENQVEVLKQK-QKSEDAAKRLKTEIQCIKAQKVQLQ 634
Cdd:COG4717 148 LEELEERLEELRELEEELEE-LEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|....*
gi 1063715979 635 QKMKQEAEQfrQWKASQEKELLQLK 659
Cdd:COG4717 227 EELEQLENE--LEAAALEERLKEAR 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
504-705 |
2.22e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 504 NSMGKELNELSKRLEEKESEMRvcgiGTETIrqhfEKKMMELEKEKRTVQDERDMLLAEVEELAAssdrqaqvardnhah 583
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIK----RTENI----EELIKEKEKELEEVLREINEISSELPELRE--------------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 584 KLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFR-----QWKASQEKELLQL 658
Cdd:PRK03918 222 ELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelKEKAEEYIKLSEF 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063715979 659 KKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELLEARK 705
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
495-660 |
2.79e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 495 EEWEHALRQNS------MGKELNELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEKRTVQDERDmllaEVEELaa 568
Cdd:PRK01156 568 TSWLNALAVISlidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN----EIQEN-- 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 569 ssdrqaQVARDNHAHKLKALETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMK---QEAEQFR 645
Cdd:PRK01156 642 ------KILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEilrTRINELS 715
|
170
....*....|....*
gi 1063715979 646 QWKASQEKELLQLKK 660
Cdd:PRK01156 716 DRINDINETLESMKK 730
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
382-757 |
3.28e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 382 NKPVANKDLICSEMQKMRQELQYLQATLCARGATSSEEVQVMREKIMKLESANEELSRelhIYRSKRVTLDYCNIDAQED 461
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK---FKNNKEVELEELKKILAED 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 462 GVIFSKddglKRGFESMDSDYEMSEatsdigaaeewehalrqnsmgKELNELSKRLEEKESEMRVCGIGTETIRQHFEKK 541
Cdd:pfam05483 418 EKLLDE----KKQFEKIAEELKGKE---------------------QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 542 MMELEKEKRTVQDERDMLLAEVEELAASSDRQAQVARDnhahklkaletQILNLKKKQENQVEVLKQKQksedaakRLKT 621
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD-----------MTLELKKHQEDIINCKKQEE-------RMLK 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 622 EIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVLQRKTEEAAMATKRLKELL 701
Cdd:pfam05483 535 QIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063715979 702 EARKssphdiSVIANGQPPSRQTNEKSLR-KWLDNELE-VMAKVHQVRFQYEKQIQVR 757
Cdd:pfam05483 615 QENK------ALKKKGSAENKQLNAYEIKvNKLELELAsAKQKFEEIIDNYQKEIEDK 666
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
604-705 |
3.29e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 604 EVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMVL 683
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAA 130
|
90 100
....*....|....*....|..
gi 1063715979 684 QRKTEEAAMATKRLKEllEARK 705
Cdd:TIGR02794 131 EAKAKAEAEAERKAKE--EAAK 150
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
512-705 |
3.67e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 512 ELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEKRtvqdERDMLLAEVEELAASSDRQAQVARDNHAHKLKALETQ 591
Cdd:pfam13868 60 EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ----EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 592 ILNLKKKQENQ-----------VEVLKQKQKSEDAAKRlktEIQCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKK 660
Cdd:pfam13868 136 NEEQAEWKELEkeeereederiLEYLKEKAEREEEREA---EREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063715979 661 EGRKTEHERLKLEALNRRQKMVLQ-RKTEEAAMATKRLKELLEARK 705
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQElQQAREEQIELKERRLAEEAER 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
561-690 |
4.35e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.60 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 561 AEVEELAASSDRQAQVARDNHAHKLKALETQILNLKKKQ---ENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQ-LQQK 636
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRaaeQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQaEEAK 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063715979 637 MKQEAEQfrqwKASQEKELLQLKKEG--RKTEHERLKLEALNRRQKMVLQRKTEEA 690
Cdd:TIGR02794 126 AKQAAEA----KAKAEAEAERKAKEEaaKQAEEEAKAKAAAEAKKKAEEAKKKAEA 177
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
508-874 |
4.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKESEMRVCGIGTETIRQhFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAqvardnHAHKLKA 587
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLPLYQELEA------LEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 588 LETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEI----QCIKAQKVQLQQKMKQEAEQFRQWKASQEKELLQLKKEGR 663
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 664 KTEHERLKLEALNRRQKmvLQRKTEEAAMATKRLKELLEARKSSPHDISVIANgqppsrqtnekslrkWLDNELEVMAKV 743
Cdd:COG4717 224 ELEEELEQLENELEAAA--LEERLKEARLLLLIAAALLALLGLGGSLLSLILT---------------IAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 744 HQVRFQYEKQIQVRAALAVELTSLRQEMEFpsnSHQEKNGQFRFLSPNTRLERIASLESMLDVSsnaltAMGSQLSEAEE 823
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLELLDRIE-----ELQELLREAEE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1063715979 824 REHSLHAKPRWNHIQSmtdakyLLQYVFDSTAEARSKIWEKDRDIKEKKEQ 874
Cdd:COG4717 359 LEEELQLEELEQEIAA------LLAEAGVEDEEELRAALEQAEEYQELKEE 403
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
519-903 |
4.71e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 519 EKESEMRVCGIGTETIRQHFEKKMMELEKEKRTVQDErdmllaEVEELAASSDRQAQVARDNHAHKLKALETQILNLKKK 598
Cdd:COG5185 207 IKESETGNLGSESTLLEKAKEIINIEEALKGFQDPES------ELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 599 QENQVEVLKQkqkSEDAAKRLKTEIQCIKAQKVQLQ-QKMKQEAE---QFRQWKASQEKELLQLKKE---GRKTEHERLK 671
Cdd:COG5185 281 NENANNLIKQ---FENTKEKIAEYTKSIDIKKATESlEEQLAAAEaeqELEESKRETETGIQNLTAEieqGQESLTENLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 672 LEALNRRQKMVLQRKTEEAAMATKRLKELLEARKSSPHDISVIANGQPPSRQTNEKSLRKWLDNELEVMAKVHQVRFQYE 751
Cdd:COG5185 358 AIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 752 KQIQVRAALAVELTSLRQEMEFPSNSHQEKNGQFRFLSPNTRLERIASLESMLDVSSNALTAMGSQLSEAEEREHSLHAK 831
Cdd:COG5185 438 EVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRS 517
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 832 PRWNHIQSMTDAK---YLLQYVFDSTAEARSKIWEKdrDIKEKKEQLNDLLCLLQLTEVQNREILKEKKTREQTV 903
Cdd:COG5185 518 KLDQVAESLKDFMrarGYAHILALENLIPASELIQA--SNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPI 590
|
|
| iSH2_PI3K_IA_R |
cd12923 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
540-661 |
4.81e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.
Pssm-ID: 214016 [Multi-domain] Cd Length: 152 Bit Score: 38.74 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 540 KKMMELEKEKRTVQDERDMLLAEVEELAASSD--RQAQVArdnHAHKLKALETQILNLKKKQ-ENQVevlKQKQKSEDAA 616
Cdd:cd12923 8 KKLKEINKEYLDKSREYDELYEKYNKLSQEIQlkRQALEA---FEEAVKMFEEQLRTQEKFQkEAQP---HEKQRLMENN 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063715979 617 KRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWkasqEKELLQLKKE 661
Cdd:cd12923 82 ELLKSRLKELEESKEQLEEDLRKQVAYNREL----EREMNSLKPE 122
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
508-700 |
5.30e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 508 KELNELSKRLEEKesemrvcgigtetiRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQVARDNHaHKLKA 587
Cdd:TIGR00606 691 AELQEFISDLQSK--------------LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-NKLQK 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 588 LETQILNLKKKQENQVEVLKQKQKSEDAAKRLKTEIQCIKAQKVQLQQKMKQEAEQFRQWKASQ-EKELLQLKKEGRKTE 666
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDlDRTVQQVNQEKQEKQ 835
|
170 180 190
....*....|....*....|....*....|....
gi 1063715979 667 HERLKLEALNRRQKMVLQRKTEEAAMATKRLKEL 700
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
558-772 |
5.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 558 MLLAEVEELAASSDRQAQVARDNHAHKLKALETQILNLKKKQENQVEVLKQ-KQKSEDAAKRLKTEIQCIKAQKVQLQQK 636
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 637 MKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKL-------EALNRRQKMV------LQRKTEEAAMATKRLKELLEA 703
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLkylapaRREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063715979 704 RKSSPHDISVIANGQppsrQTNEKSLRKWLDNELEVMAKVHQVRFQYEKQIQVRAALAVELTSLRQEME 772
Cdd:COG4942 169 LEAERAELEALLAEL----EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
576-702 |
5.68e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 576 VARDNHAHKLKALETQILNLKKKQENQVEVLKQKQKSEdaakrLKTEIQcikaqkvQLQQKMKQEAEQFRQWKASQEKEL 655
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLE-----AKEEIH-------KLRNEFEKELRERRNELQKLEKRL 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063715979 656 LQ----LKKEGRKTEHERLKLEA----LNRRQKMVLQRKTEEAAMATKRLKELLE 702
Cdd:PRK12704 92 LQkeenLDRKLELLEKREEELEKkekeLEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
556-772 |
6.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 556 RDMLLAEVEELAASSDRQAQVARDNHAHKLKALETQIlnlkKKQENQVEVLKQKQkseDAAKRLKTEIQCIKAQKVQLQQ 635
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEEL----KEAEEKEEEYAELQ---EELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 636 KMKQEAEQFRQWKASQEKELLQLKKEGRKTEHERLKLEALNRRQKMV-LQRKTEEAAMATKRLKELLEArkssphdisvi 714
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEeLEELEAELAELQEELEELLEQ----------- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063715979 715 angqppSRQTNEKSLRKWLDNELEVMAKVHQVRFQYEKQIQVRAALAVELTSLRQEME 772
Cdd:COG4717 186 ------LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-700 |
7.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 383 KPVANKDLICSE-MQKMRQELQYLQATLcargATSSEEVQVMREKIMKLESANEELsrelhiyrskrvtldycnidaqed 461
Cdd:PRK03918 289 KEKAEEYIKLSEfYEEYLDELREIEKRL----SRLEEEINGIEERIKELEEKEERL------------------------ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 462 GVIFSKDDGLKRGFESMDSDYEM-SEATSDIGAAEEWEHALRQNSMGK---ELNELSKR---LEEKESEMRVCGIGTETI 534
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTGLTPEKlekELEELEKAkeeIEEEISKITARIGELKKE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 535 RQHFEKKMMELEKEKRTV--------QDERDMLLAE-VEELAASSDRQAQVARdnhahKLKALETQILNLKKKQENQVEV 605
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEyTAELKRIEKELKEIEE-----KERKLRKELRELEKVLKKESEL 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 606 LKQKQKSEDaAKRLKTEIQCIKAQKVqlqqkmKQEAEQFRQWKasqeKELLQLKKEGRKTEHERLKLEALNRRQKMV--- 682
Cdd:PRK03918 496 IKLKELAEQ-LKELEEKLKKYNLEEL------EKKAEEYEKLK----EKLIKLKGEIKSLKKELEKLEELKKKLAELekk 564
|
330
....*....|....*...
gi 1063715979 683 LQRKTEEAAMATKRLKEL 700
Cdd:PRK03918 565 LDELEEELAELLKELEEL 582
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
418-661 |
7.86e-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: 40.09 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 418 EEVQVMREKIMKLESANEELSRELhIYRSKRVTldyCNIDAQEDGVIFSKDDGLKRGFESMDSDYEMSEATSDIGAAEEW 497
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEF-IQKGDEVK---CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 498 EHALRQ--NSMGKELNELSKRLEEKESEMRVCGIGTETIRQHFEKKMMELEKEKRTVQDERDMLLAEVEELAASSDRQAQ 575
Cdd:pfam05483 610 IEELHQenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 576 VARD---NHAHKLKAL-------ETQILNLKKKQENQVEVLKQKQKSEDAAK-RLKTEIQCIKAQKVQLQQKMKQEAEQF 644
Cdd:pfam05483 690 LQKEidkRCQHKIAEMvalmekhKHQYDKIIEERDSELGLYKNKEQEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEK 769
|
250
....*....|....*..
gi 1063715979 645 RQWKASQEKELLQLKKE 661
Cdd:pfam05483 770 EKLKMEAKENTAILKDK 786
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
584-689 |
8.30e-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: 37.93 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063715979 584 KLKALETQILNLKKKQENQVEVLKQKQKSE--DAAKRLKTEiqcikaQKVQLQQ----------KMKQEAEQFRQWkasQ 651
Cdd:pfam12474 19 LKKRYEKELEQLERQQKQQIEKLEQRQTQElrRLPKRIRAE------QKKRLKMfreslkqekkELKQEVEKLPKF---Q 89
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1063715979 652 EKELLQLKKEGRKTEH---ERLKLEALNRRQKMVLQRKTEE 689
Cdd:pfam12474 90 RKEAKRQRKEELELEQkheELEFLQAQSEALERELQQLQNE 130
|
|
| |
