|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
1.43e-164 |
|
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: 495.31 E-value: 1.43e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 95 QTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTASR-DIQLREDE 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 173 RGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRLPRPAPGQL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 251 VDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 2217301032 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
9.84e-139 |
|
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: 426.99 E-value: 9.84e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVT-------LGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 88 ATVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLevGTASRD 165
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMiGT-------PDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 166 IQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRlprpapGQLLV 245
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:smart00129 226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304
|
330 340 350
....*....|....*....|....*....|.
gi 2217301032 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
2.99e-134 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 414.66 E-value: 2.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 21 RVRPLLPKELLHGHQSCLQVEPGLGRVTL-------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 94 GQTGSGKTYTMGEasvaslLEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 172 ERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpAPGQLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTG-----GEESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 252 DLAGSERVLKTG-STGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 2217301032 331 SDFDETLNTLNYASRAQNI 349
Cdd:pfam00225 308 SNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
15-347 |
2.98e-124 |
|
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: 387.77 E-value: 2.98e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKELLHGHqSCLQVEPG------LGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 89 TVFAYGQTGSGKTYTMGEASvasllEDEQGIVPRAMAEAFKLIDENDLLD--CLVHVSYLEVYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 167 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpaPGQLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 2217301032 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
16-349 |
8.15e-108 |
|
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: 8.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELLHGHQSCLQV--------EPGLGRVTL--------------GRDRHFGFHVVLAEDAGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 153 FRDLLEvgTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 233 SRLPrpapgQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217301032 313 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
16-356 |
2.67e-103 |
|
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: 332.78 E-value: 2.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKEL---------LHGHQSCLQVEPGLGRVTLGRDRH---FGFHVVL----AED---AGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLID--ENDLLDCLVHVSYLEVYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 155 DLLEVGTASRDIQLREDE---RGNVVLcGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRgRA 231
Cdd:cd01365 157 DLLNPKPKKNKGNLKVREhpvLGPYVE-DLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 232 PSRLPRPAPgqlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQR-----RGSHIPYRDSKI 306
Cdd:cd01365 235 DAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2217301032 307 TRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01365 312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
16-349 |
7.45e-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: 330.58 E-value: 7.45e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTL--GRD------RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 88 ATVFAYGQTGSGKTYTMGEASVAsllEDEQGIVPRAMAEAFKLID-ENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 167 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQrgrapSRLPRPAPGQLLVS 246
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHIRVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01371 234 KLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANI 311
|
330 340
....*....|....*....|...
gi 2217301032 327 SPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01371 312 GPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
16-349 |
2.83e-102 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 328.14 E-value: 2.83e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELLHG--------HQSCLQVEPGLGRvtlgrdrhFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 88 ATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 168 LREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPsrlprPAPGQLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 248 FHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 2217301032 328 PSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01374 300 PAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
16-351 |
7.02e-96 |
|
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: 311.07 E-value: 7.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELlHGHQSCLQVEPGLG-RVTL---GRDRH-FGFHVVLAEDAGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 91 FAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLIDENDLLDCLVH--VSYLEVYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTMEGP------PESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 166 IQLREDErGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLeqRGRAPSRlprpapGQLLV 245
Cdd:cd01366 156 IRHDSEK-GDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 2217301032 326 VSPSSSDFDETLNTLNYASRAQNIRN 351
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
16-358 |
2.54e-94 |
|
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: 307.72 E-value: 2.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTL--------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 88 ATVFAYGQTGSGKTYTM-GEASVASLLEDEQ----GIVPRAMAEAFKLIDENDLlDCLVHVSYLEVYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 162 ASRDIQLREDER--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpa 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 240 pGQLLV--SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGN 317
Cdd:cd01364 237 -GEELVkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217301032 318 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWR 358
Cdd:cd01364 313 TKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
16-349 |
3.81e-93 |
|
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: 303.48 E-value: 3.81e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELLHGHQSCLQVEPGlGRVTLGRD---RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPE-DTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 93 YGQTGSGKTYTMgEASvaslLEDEQ--GIVPRAMAEAFKLIDEND-LLDCLVHVSYLEVYKEEFRDLLEVgtaSRD-IQL 168
Cdd:cd01369 83 YGQTSSGKTYTM-EGK----LGDPEsmGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 169 REDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPsrlprpapGQLLVSKF 248
Cdd:cd01369 155 HEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVET--------EKKKSGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 249 HFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSP 328
Cdd:cd01369 227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSP 304
|
330 340
....*....|....*....|.
gi 2217301032 329 SSSDFDETLNTLNYASRAQNI 349
Cdd:cd01369 305 SSYNESETLSTLRFGQRAKTI 325
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
1.08e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 285.48 E-value: 1.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 55 FGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 135 DLLDCL-VHVSYLEVYKEEFRDLLEVGTASRDIqlREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 214 SSRSHTVFTVTLEQRGRAPSRLPRpapgqllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301032 294 RRGsHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:COG5059 282 KSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
15-356 |
1.23e-83 |
|
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: 277.47 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLG-RDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 94 GQTGSGKTYTM-GEA-SVASLLEDEQGIVPRAMAEAFKLID-----ENDLLDCLVHVSYLEVYKEEFRDLLEvgTASRDI 166
Cdd:cd01373 82 GQTGSGKTYTMwGPSeSDNESPHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 167 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEqrgrapSRLPRPAPGQLLVS 246
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE------SWEKKACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340 350
....*....|....*....|....*....|.
gi 2217301032 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01373 314 VHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
15-347 |
2.02e-79 |
|
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: 265.80 E-value: 2.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKELLHGHQSCLQVE--------------PGLGRVTLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhppkgsaANKSERNGGQKETkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDlldclVHVSYLEVYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 160 GTASRD-----IQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSR 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 235 LPRPAPGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRG--SHIPYRDSKITRILKD 312
Cdd:cd01368 231 DVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSKLTHLFQN 310
|
330 340 350
....*....|....*....|....*....|....*
gi 2217301032 313 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01368 311 YFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
15-345 |
5.52e-79 |
|
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: 263.77 E-value: 5.52e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKEL---------LHGHQSCLQVEPGLgRVTLGR--DRH-FGFHVVLAEDAGQEAVYQACVQPLLEAF 82
Cdd:cd01367 1 KIKVCVRKRPLNKKEVakkeidvvsVPSKLTLIVHEPKL-KVDLTKyiENHtFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 83 FEGFNATVFAYGQTGSGKTYTMGEASvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGT 161
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 162 asrDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLeqrgrapsrlpRPAPG 241
Cdd:cd01367 158 ---RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 242 QLLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSSLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAK 319
Cdd:cd01367 224 NKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSK 300
|
330 340
....*....|....*....|....*.
gi 2217301032 320 TVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01367 301 TCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
15-347 |
1.13e-77 |
|
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: 259.74 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLgRVTLGRDRHFG------FHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 89 TVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDENDLLDClVHVSYLEVYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlGS-------PEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 168 LREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGR-APSRLPRpapgqllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERlAPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 2217301032 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01376 299 APERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
55-345 |
2.97e-72 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 244.80 E-value: 2.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 55 FGFHVVLaEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASlleDEQGIVPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 135 DLLDCLVHVSYLEVYKEEFRDLL----EVGTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHL 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 211 NHLSSRSHTVFTVTLEQRGRAPSRlprpapGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLSS------EKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217301032 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
10-356 |
1.75e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 225.20 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 10 GAEEAPVRVALRVRPLLPKEllhghQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNAT 89
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 90 VFAYGQTGSGKTYTM-GEASVAS---LLEDEQGIVPRAMAEAFKLIDENDL------LDCLVHVSYLEVYKEEFRDLLEv 159
Cdd:PLN03188 169 VFAYGQTGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 160 gTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEqrgrapSRLPRPA 239
Cdd:PLN03188 248 -PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVE------SRCKSVA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 240 PG--QLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLG 315
Cdd:PLN03188 321 DGlsSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLG 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217301032 316 GNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 401 GNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
700-1196 |
1.16e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 779
Cdd:COG1196 254 ELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 RLQEFRRRVAAAQSQVQVLKEK--------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLE 851
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEEleeaeaelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 852 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 931
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 932 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKsgQLRQGSAQSQQQIRGEIDSLRQE 1011
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA--ALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1012 KDSLLKQ----RLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAK 1085
Cdd:COG1196 562 AIEYLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1086 LSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1165
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
490 500 510
....*....|....*....|....*....|.
gi 2217301032 1166 LQQSRDHLGEGLADSRRQYEARIQALEKELG 1196
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
723-1060 |
1.41e-15 |
|
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: 82.41 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 723 GELVRTG---------KAAQALNRQhsQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAGE--RSRLQEFRRRVA 789
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKEleELEEELEqlRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 790 AAQSQVQVLKEKKQaterlvslsaQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHE 869
Cdd:TIGR02168 730 ALRKDLARLEAEVE----------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 870 QQQKILKIKTEEI------AAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILA 942
Cdd:TIGR02168 800 ALREALDELRAELtllneeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 943 KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGsaqsQQQIRGEIDSLRQEKDSLLKQRLEI 1022
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR----LEGLEVRIDNLQERLSEEYSLTLEE 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2217301032 1023 DGKLRQGSLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1060
Cdd:TIGR02168 956 AEALENKIEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
742-1195 |
1.90e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 742 RIRELEQEAEQVRAELSEGQRQLRELEgKELQDAgeRSRLQEFRRRVAAAQSQVqvlkEKKQATERLVslsaqsEKRLQE 821
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELE-AELAEL--EAELEELRLELEELELEL----EEAQAEEYEL------LAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 822 LERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLE 901
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 902 QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK 981
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 982 ELSEKSGQLRQ---------GSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ----------------GSLLSPEE 1036
Cdd:COG1196 454 LEEEEEALLELlaelleeaaLLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaalllaglrglagaVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1037 ERTLFQLDEAIEALDAAIEYKNE--AITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ 1114
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1115 QQIAFSE-----------LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRR 1182
Cdd:COG1196 614 RYYVLGDtllgrtlvaarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490
....*....|...
gi 2217301032 1183 QYEARIQALEKEL 1195
Cdd:COG1196 694 ELEEALLAEEEEE 706
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
67-288 |
1.20e-11 |
|
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: 64.67 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 67 QEAVYqACVQPLLEAFFEGFN-ATVFAYGQTGSGKTYTMgeasvaslledeQGIVPRAMAEAFklidendlldclvhvSY 145
Cdd:cd01363 32 QPHVF-AIADPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAF---------------NG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 146 LEVYKEEFRDLLEvgtasrdiqlredergnvvlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHLNHLSSRSHTVFTVtl 225
Cdd:cd01363 84 INKGETEGWVYLT------------------------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI-- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301032 226 eqrgrapsrlprpapgqllvskfhFVDLAGSERvlktgstgerlkesiqINSSLLALGNVISA 288
Cdd:cd01363 137 ------------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
676-1015 |
5.34e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 676 GSRVGGSKAR---VQARQVPPATASEwRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE------- 745
Cdd:TIGR02168 659 GVITGGSAKTnssILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlar 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 746 LEQEAEQVRAELSEGQRQLRELEGK----ELQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATERLVSLSAQ---SEK 817
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEieelEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAEltlLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 818 RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsv 897
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL------ 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 898 VSLEQQQKIEEQKKWLDQEMEKvlqqRRALEELGEELHKreAILAKKEALMQEKTGLEskRLRSSQALNEDIVrvssrle 977
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSEL----RRELEELREKLAQ--LELRLEGLEVRIDNLQE--RLSEEYSLTLEEA------- 956
|
330 340 350
....*....|....*....|....*....|....*...
gi 2217301032 978 hlekelseksGQLRQGSAQSQQQIRGEIDSLRQEKDSL 1015
Cdd:TIGR02168 957 ----------EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-1024 |
6.65e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 703 QAQQKIRELAINIRMKEELIGE-------LVRTGKAAQALNRQHSQ-----------RIRELEQEAEQVRAELSEGQRQL 764
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNElerqlksLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 765 ----RELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQElernvqlmrqqQGQLQRRL 840
Cdd:TIGR02168 256 eeltAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------QLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 841 REETEQKR-RLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvslEQQQKIEEQKKWLDQEMEK 919
Cdd:TIGR02168 325 LEELESKLdELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----------ELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 920 VLQQRRALEELGEEL----HKREAILAKKEALMQEKTGLESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKSGQLRQGS 994
Cdd:TIGR02168 395 IASLNNEIERLEARLerleDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350
....*....|....*....|....*....|
gi 2217301032 995 aQSQQQIRGEIDSLRQEKDSLLKQRLEIDG 1024
Cdd:TIGR02168 475 -QALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-1037 |
7.24e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 702 AQAQQKIR-----------ELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAEQVRAELSEGQRQLREL 767
Cdd:TIGR02168 207 RQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 768 EGkelqdagersRLQEFRRRVAAAQSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 847
Cdd:TIGR02168 287 QK----------ELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 848 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNgsvvsleQQQKIEEQKKWLDQEMEKVLQQRRAL 927
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-------EIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 928 EELGEElHKREAILAKKEALMQEKTGLESKRLRSSQALNedivRVSSRLEHLEKELSEKSGQLRQGSAQ--SQQQIRGEI 1005
Cdd:TIGR02168 427 LKKLEE-AELKELQAELEELEEELEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
|
330 340 350
....*....|....*....|....*....|...
gi 2217301032 1006 DSLRQEKDSLLKQRLEIDGKL-RQGSLLSPEEE 1037
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILgVLSELISVDEG 534
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
701-1028 |
1.69e-10 |
|
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: 65.43 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 701 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalnrqhSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDagERSR 780
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEEKQ-NEIEK--LKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 781 LQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 860
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 861 VKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAI 940
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 941 LAKK-EALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKsgqlrqgsaqsQQqirgEIDSLRQEKDSLLK 1017
Cdd:TIGR04523 522 LKEKiEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEK-----------NK----EIEELKQTQKSLKK 582
|
330
....*....|.
gi 2217301032 1018 QRLEIDGKLRQ 1028
Cdd:TIGR04523 583 KQEEKQELIDQ 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
738-1128 |
1.95e-10 |
|
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: 65.43 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 738 QHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELqdagersrlqefrrrvaaaQSQVQVLKEKKQATERLVSlsaQSEK 817
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL-------------------KSELKNQEKKLEEIQNQIS---QNNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 818 RLQELERNVQLMRqqqgqlqrrlreetEQKRRLEAEMSKRQhrvKELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSv 897
Cdd:TIGR04523 336 IISQLNEQISQLK--------------KELTNSESENSEKQ---RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 898 vSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELhKREAILAKKE--ALMQEKTGLES-----KRLRSSQ-----A 964
Cdd:TIGR04523 395 -DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEikDLTNQDSVKELiiknlDNTRESLetqlkV 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 965 LNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQsQQQIRGEIDSLRQEKDSLL-------KQRLEIDGKLRQ--GSLLSPE 1035
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKekiekleSEKKEKESKISDleDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1036 EERTLFQLDEAIEALDAAIEYKNEAITcrqrvlrasaSLLSqcemnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQ 1115
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQK----------SLKK-------------KQEEKQELIDQKEKEKKDLIKEIEEK 608
|
410
....*....|...
gi 2217301032 1116 QIAFSELEMQLEE 1128
Cdd:TIGR04523 609 EKKISSLEKELEK 621
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
793-1077 |
2.22e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 793 SQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKR-RLEAEMSKRQHRVKELELKHEQQ 871
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELeELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 872 QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEK 951
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 952 tgLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSL 1031
Cdd:COG1196 360 --LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2217301032 1032 LSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1077
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-1055 |
1.71e-09 |
|
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: 62.78 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 709 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFR 785
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKRELSSL----------QSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 786 RRVAAAQSQVQVLKEKkqaTERLvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 865
Cdd:TIGR02169 702 NRLDELSQELSDASRK---IGEI-------EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 866 LK-HEQQQKILKIK----------TEEIAAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 933
Cdd:TIGR02169 772 EDlHKLEEALNDLEarlshsripeIQAELSKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 934 LHKR-EAILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKSGQLRQ-----GSAQSQQQIRGEIDS 1007
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRElerkiEELEAQIEKKRKRLS 920
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217301032 1008 LRQEKDSLLKQRL-EIDGKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1055
Cdd:TIGR02169 921 ELKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
794-1077 |
1.88e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 794 QVQVLKEKKQATERLVSLSAQSE--------KRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 865
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 866 LKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsleqqqKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKE 945
Cdd:TIGR02168 281 EEIEELQKELYALANEIS---------------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 946 ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIR-----------------GEIDSL 1008
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneierlearlerleDRRERL 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217301032 1009 RQEKDSLLKQRLEIDGKLRQGSLlsPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1077
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
739-1012 |
1.93e-09 |
|
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: 62.39 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 739 HSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERS-----RLQEFRRRV--------AAAQSQVQVLKEKKQAT 805
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLT-EEISELEKRLeeieqLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 806 ERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR-----------LEAEMSKRQHRVKELELKHEQQQKI 874
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteeyaeLKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 875 LKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEElhKREAILAKKEALMQEKTGL 954
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIKKQEWKLEQLAADL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301032 955 ESKRlrssqalnEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEK 1012
Cdd:TIGR02169 465 SKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
789-1034 |
2.88e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 789 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKH 868
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 869 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELHKREAILAKKEA 946
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 947 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKL 1026
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 2217301032 1027 RQGSLLSP 1034
Cdd:COG4942 251 LKGKLPWP 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
698-1196 |
3.02e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 698 EWRLAQAQQKIRELAINIRmkeELIGELvrtgkaaqalnrqhsQRIRELEQEAEQVRAELSEGQRQLRELEGKElqdAGE 777
Cdd:PRK03918 199 EKELEEVLREINEISSELP---ELREEL---------------EKLEKEVKELEELKEEIEELEKELESLEGSK---RKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 778 RSRLQEFRRRVAAAQSQVQVLKEK----------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 847
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKvkelkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 848 RRLEaEMSKR----QHRVKELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQ 922
Cdd:PRK03918 338 ERLE-ELKKKlkelEKRLEELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 923 QRRALEELGEELH---------KREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQL-RQ 992
Cdd:PRK03918 413 RIGELKKEIKELKkaieelkkaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 993 GSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAIT 1062
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1063 CRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALER 1142
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEE 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1143 QRLEMDR-QLTLQQKEHEQNMQLLLQQSRDHLG-----EGLADSRRQYEARIQALEKELG 1196
Cdd:PRK03918 645 LRKELEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
703-1209 |
3.56e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 703 QAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQ--------HSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQD 774
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 775 AGERSRLQEFRRRVAAAQSQVQvlkEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreETEQKRRLEAEM 854
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQH------------------IHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 855 SKRQHRVKELELKHEQQQKIlkikteeiaAFQRKRRSGSNGSVVSLEQQQKIE-EQKKWLDQEMEKVLQ----QRRALEE 929
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATI---------DTRTSAFRDLQGQLAHAKKQQELQqRYAELCAAAITCTAQceklEKIHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 930 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKEL-----SEKSGQLRQGSAQSQQQIRGE 1004
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1005 IDSLRQEKDSLLKQRLEIdgklrqgsllspEEERTLFQLDEAIEAldaaieykneaiTCRQRVlRASASLLSQcEMNLMA 1084
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASL------------KEQMQEIQQSFSILT------------QCDNRS-KEDIPNLQN-ITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1085 KLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLV----YWLEVALERQRlEMDRQLTLQQKEHEQ 1160
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTalhaLQLTLTQERVR-EHALSIRVLPKELLA 676
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2217301032 1161 NMQLLLQ--QSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKL 1209
Cdd:TIGR00618 677 SRQLALQkmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-1050 |
4.26e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 696 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR-QHSQRIRELEQEAEQVRAELSEGQRQLRELE-GKELQ 773
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEA---KKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkADEAK 1516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 774 DAGERSRLQEFRRRVAAAQS-QVQVLKEKKQATE--RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 850
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKAdEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 851 EAEMSKRQHRVKELELKHEQQQKIlkiKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVlqqRRALEEL 930
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKI---KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKI---KAAEEAK 1668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 931 GEELHKREAILAKKEALMQEKTGLESKRlrssqalNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQ 1010
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKK-------EAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAKKEA 1739
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217301032 1011 EKDSLLKQRLEID-GKLRQGSLLSPEEERTLFQLDEAIEAL 1050
Cdd:PTZ00121 1740 EEDKKKAEEAKKDeEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
742-1017 |
7.82e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 742 RIRELEQEAEQVRAELSEGQRQLRELEG------KELQDAGE-RSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQ 814
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREelekleKEVKELEElKEEIEELEKELESLEGSKRKLEEKIRELEERI---EE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 815 SEKRLQELERNVqlmrqqqgQLQRRLREETEQKRRLEAEMSKRQHRVKELElkheqqqKILKIKTEEIAAFQRKrrsgsn 894
Cdd:PRK03918 271 LKKEIEELEEKV--------KELKELKEKAEEYIKLSEFYEEYLDELREIE-------KRLSRLEEEINGIEER------ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 895 gsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRlrssqaLNEDIVRVSS 974
Cdd:PRK03918 330 -----IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK------LEKELEELEK 398
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2217301032 975 RLEHLEKELSEksgqlrqgsaqsqqqIRGEIDSLRQEKDSLLK 1017
Cdd:PRK03918 399 AKEEIEEEISK---------------ITARIGELKKEIKELKK 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
668-1194 |
2.50e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 668 EELDAAIPGSRVGGSKARVQARQVPPA-TASEWRLAQAQQKIREL--AINIRMKEEL-IGELVRTGKAA-QALNRQHSQR 742
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAArkAEEVRKAEELrKAEDARKAEAArKAEEERKAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 743 IRELEQE--------AEQVRAELSEGQRQLRELEGKELQDAgERSRLQEFRRRVAAAQSQ-------VQVLKEKKQATER 807
Cdd:PTZ00121 1217 ARKAEDAkkaeavkkAEEAKKDAEEAKKAEEERNNEEIRKF-EEARMAHFARRQAAIKAEearkadeLKKAEEKKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 808 LVS----------LSAQSEKRLQELERNVQLMRQQQGQLQRRLREET---------EQKRRLEAEMSKRQHRVKELELKH 868
Cdd:PTZ00121 1296 KKAeekkkadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaeaakaeAEAAADEAEAAEEKAEAAEKKKEE 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 869 EQQQ-KILKIKTEEIAAFQRKRRSGSNGSVVSlEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEAl 947
Cdd:PTZ00121 1376 AKKKaDAAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA- 1453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 948 mQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGS--AQSQQQIRGEIDSLRQEKDSLLKQRL-EIDG 1024
Cdd:PTZ00121 1454 -EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAkKAEE 1532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1025 KLRQGSLLSPEEERTLFQLDEAIEALDA----AIEYKNEAITCRQRVLRaSASLLSQCEMNLMAKLSYLSSSETRAllck 1100
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKM---- 1607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1101 yfdKVVTLREEQhQQQIAFSELEMQLEEQQRLvywleVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRdhlgEGLADS 1180
Cdd:PTZ00121 1608 ---KAEEAKKAE-EAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK----KAEEDK 1674
|
570
....*....|....
gi 2217301032 1181 RRQYEARIQALEKE 1194
Cdd:PTZ00121 1675 KKAEEAKKAEEDEK 1688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
698-1195 |
3.46e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 698 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDA 775
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 776 --GERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLE 851
Cdd:TIGR02168 381 leTLRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 852 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 917
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 918 EKVL-------------QQRRALEELGEELHKREAILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 977
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 978 ----------------HLEKELSE-------------KSGQLRQGSAQSQQQI---RGEIDSLRQEK------------- 1012
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPgyrivtldgdlvrPGGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1013 -DSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1091
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1092 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRD 1171
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 2217301032 1172 --HLGEGLADSRRQYEARIQALEKEL 1195
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
742-1208 |
4.75e-08 |
|
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: 57.72 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 742 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQE----FRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEK 817
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 818 RLQELERNVQlmrqqqgqlqrrlrEETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIaafqrkrrSGSNGSV 897
Cdd:TIGR04523 226 QNNQLKDNIE--------------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--------EQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 898 VSLEQQ-QKIEEQKKWLDQEMEKVLqqrraLEELGEELHKREailakkealmQEKTGLESKRLRSSQA---LNEDIVRVS 973
Cdd:TIGR04523 284 KELEKQlNQLKSEISDLNNQKEQDW-----NKELKSELKNQE----------KKLEEIQNQISQNNKIisqLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 974 SRLEHLEKELSEKSGQLRQgsAQSQ-QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQgsllspeEERTLFQLDEAIEALda 1052
Cdd:TIGR04523 349 KELTNSESENSEKQRELEE--KQNEiEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKL-- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1053 aiEYKNEAITCRQRVLRASASLLSQCEMNLmaklsylssSETRALLCKYFDKVVTLREEQhQQQIafSELEMQLEEQQRL 1132
Cdd:TIGR04523 418 --QQEKELLEKEIERLKETIIKNNSEIKDL---------TNQDSVKELIIKNLDNTRESL-ETQL--KVLSRSINKIKQN 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 1133 VYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSrdhlgegladsrRQYEARIQALEKELGRymwINQELKQK 1208
Cdd:TIGR04523 484 LEQKQKELKSKEKELK-KLNEEKKELEEKVKDLTKKI------------SSLKEKIEKLESEKKE---KESKISDL 543
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
796-1097 |
4.89e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 57.67 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 796 QVLKEKKQATERLVSLSAQSEKRL----------QELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 865
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLELeeeyllyldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 866 LKHEQ-QQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELH-KREAILAK 943
Cdd:pfam02463 278 EKEKKlQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 944 KEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgSAQSQQQIRGEIDSLRQEKDSLLKQRLEID 1023
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--EAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217301032 1024 GKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRqrvLRASASLLSQCEMNLMAKLSYLSSSETRAL 1097
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
690-887 |
5.80e-08 |
|
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: 56.70 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 690 QVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEg 769
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 770 KELQDagersRLQEFRRRVAAAQSQVQVLKEK------------------KQATERLVSLSAQSEKRLQELERNVQLMRQ 831
Cdd:COG4942 97 AELEA-----QKEELAELLRALYRLGRQPPLAlllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 832 QQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 887
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
920-1195 |
7.34e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 920 VLQQRRALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQ 999
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1000 ------QIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1073
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1074 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1153
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2217301032 1154 QQKEHEQNMQlLLQQSRDHLGEGLADSRRQY---EARIQALEKEL 1195
Cdd:TIGR02168 902 ELRELESKRS-ELRRELEELREKLAQLELRLeglEVRIDNLQERL 945
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
1.01e-07 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 52.61 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 16 VRVALRVRPLLPKELlhghqsclQVEPGLGRVTLGRDRH----FGFHVVLAEDAGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217301032 92 AYGQTGSGKTYTMgeasvaslledeqgiVPRAMAEAFKLIDENDLLDCL-VHVSYLEVYKEEFRDLL 157
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
696-1027 |
1.06e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 696 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR--QHSQRIRELEQEAEQVRAELSEGQRQLRELEgkELQ 773
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 774 DAGERSRLQEFRR--RVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERnvqlMRQQQGQLQRRLREETEQKRRLE 851
Cdd:PTZ00121 1541 KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEEEKKMKAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 852 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAleelG 931
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKK----A 1690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 932 EELHKREAILAKKEALMQEKTGLESKR---LRSSQALNEDIVRVSSRLEHLEKELSE----------KSGQLRQGSAQSQ 998
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkKIAHLKKEEEKKA 1770
|
330 340 350
....*....|....*....|....*....|.
gi 2217301032 999 QQIRGEIDSLRQE--KDSLLKQRLEIDGKLR 1027
Cdd:PTZ00121 1771 EEIRKEKEAVIEEelDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
701-946 |
1.25e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 701 LAQAQQKIRELAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 779
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 RLQEFRRRVAAAQSQVQVLKEkkQATERLVSLSAQSEK---RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSK 856
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 857 RQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsNGSVVSlEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK 936
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIK-KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
250
....*....|
gi 2217301032 937 REAILAKKEA 946
Cdd:TIGR02169 488 LQRELAEAEA 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
700-988 |
1.86e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAGE 777
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 778 RSRLQEFRRRVAAAQSQVQ----VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 853
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 854 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 932
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 933 ELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG 988
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
683-949 |
2.36e-07 |
|
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: 55.51 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 683 KARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAEQVRA--ELS 758
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 759 EGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQR 838
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 839 RLREETEQKRRlEAEMSKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQ 909
Cdd:pfam17380 465 LRQQEEERKRK-KLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEE 540
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217301032 910 KKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQ 949
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
694-1046 |
2.46e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 694 ATASEWRLAQAQQKIREL---AINIRMKEELIGELVRTGKAAQALNRQHSQRIR--ELEQEAEQVRAELSEGQRQLRELE 768
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 769 GKELQDAGERSRLQEFRRRVAAAQSQVQVLK---EKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE 845
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 846 QKRRLEA-----EMSKRQHRVKELELKHEQQQKilkiKTEEIAAFQRKRRSGS--NGSVVSLEQQQKIEEQ------KKW 912
Cdd:PTZ00121 1526 EAKKAEEakkadEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAEEdkNMALRKAEEAKKAEEArieevmKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 913 LDQEMEKVLQQRRALEEL--GEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVS--SRLEHLEKELSEKSG 988
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAK 1681
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301032 989 QLRQGSAQSQQQIRGEidslRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEA 1046
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKE----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
701-1171 |
2.81e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 701 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAEQVRAELSEGQR----QLRELEGK------ 770
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQlvlans 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 771 ELQDAgeRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRL---------------QEL-ERNVQLMRQQQG 834
Cdd:pfam15921 357 ELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrRELdDRNMEVQRLEAL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 835 QLQRRLREETEQKRRLEAEMSKRQ--HRVKELELKHEQQQKILKIKTEEIAA----FQRKRRSGSNGSVVSLEQQQKIEE 908
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 909 QKKWLDQEMEKV---LQQRRALEELGEELHKREAILAKKEALMQEK--------------TGLESKRLRSSQALNEDIVR 971
Cdd:pfam15921 515 TNAEITKLRSRVdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMQVEKAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 972 VSSRLEHLEKELSE-------KSGQLRQGSAQ--------------SQQQIRGeIDSLRQEKDSLLKQ----RLEIDGKL 1026
Cdd:pfam15921 595 LEKEINDRRLELQEfkilkdkKDAKIRELEARvsdlelekvklvnaGSERLRA-VKDIKQERDQLLNEvktsRNELNSLS 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1027 RQGSLL-------SPEEERTLFQLDEAIEALDAAIEYKNEAITCRQ----RVLRASASLLSQCEMN------LMAKLSYL 1089
Cdd:pfam15921 674 EDYEVLkrnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQITAKrgqidaLQSKIQFL 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1090 SSSETRALLCKYFdkvvtLREEQHQQQIAFS-----------ELEMQLEEQQRL---VYWLEVALERQRLEMDRQLTLQQ 1155
Cdd:pfam15921 754 EEAMTNANKEKHF-----LKEEKNKLSQELStvateknkmagELEVLRSQERRLkekVANMEVALDKASLQFAECQDIIQ 828
|
570
....*....|....*.
gi 2217301032 1156 KEHEQNMQLLLQQSRD 1171
Cdd:pfam15921 829 RQEQESVRLKLQHTLD 844
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
683-1226 |
3.25e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 683 KARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQA-----------LNRQHSQRIReLEQEAE 751
Cdd:TIGR00618 284 ERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqqssieeqrrlLQTLHSQEIH-IRDAHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 752 Q---VRAELSEG----------QRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKR 818
Cdd:TIGR00618 363 VatsIREISCQQhtltqhihtlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 819 LQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE---MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNG 895
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 896 SVVSLEQQQKIEEQKKWLDQEMEKVLQQrraleelGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 975
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 976 LEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQEKDSLLKQrleIDGKLRQGSLLSPEEERTLFQLDEAIEALdAAIE 1055
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLAC--EQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREHAL-SIRV 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1056 YKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQLEEQQRL 1132
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSDLAAREDA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1133 VYWLEVALERQRLEMDRQLTL--QQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRymwINQELKQKLG 1210
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKARTEahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE---IGQEIPSDED 817
|
570
....*....|....*.
gi 2217301032 1211 GVNAVGHSRGGEKRSL 1226
Cdd:TIGR00618 818 ILNLQCETLVQEEEQF 833
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
720-1059 |
3.77e-07 |
|
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: 54.74 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 720 ELIGELVRTGKAAQALN-RQHSQRIRELEQEaeQVRAELSEgqrQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVL 798
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSeRQQQEKFEKMEQE--RLRQEKEE---KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 799 KEKKQATERLvslsaQSEKRLQELERnvqlmrqQQGQLQRRLREETEQKRRLEAEMSKRQHRVK-ELE-------LKHEQ 870
Cdd:pfam17380 344 MERERELERI-----RQEERKRELER-------IRQEEIAMEISRMRELERLQMERQQKNERVRqELEaarkvkiLEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 871 QQKI--LKIKTEEIAAFQRKRRSgsngsvvslEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAILAKKEALM 948
Cdd:pfam17380 412 QRKIqqQKVEMEQIRAEQEEARQ---------REVRRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 949 Q-----EKTGLESKRLRSSQALNED---IVRVSSRLEHLEKELSEksgqlRQGSAQSQQQIRGEIDSLRQEKDslLKQRL 1020
Cdd:pfam17380 480 EkekrdRKRAEEQRRKILEKELEERkqaMIEEERKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQE--MEERR 552
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217301032 1021 EIDGKLRQGSllspEEERTLFQLDEAIEALDAAIEYKNE 1059
Cdd:pfam17380 553 RIQEQMRKAT----EERSRLEAMEREREMMRQIVESEKA 587
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
737-1197 |
7.36e-07 |
|
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: 54.07 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 737 RQHSQRIRELEQEAEQVRAELSEGQRQLRElEGKELQDAgERSRLQEFRRRVAAAQSQVQVLKEKKQATERlvslsAQSE 816
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDD-QWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-----ADIE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 817 KRLQELERNVQLMRQQQGQLQRRLREETEQkRRLEAEMSKRQHRVKE-----LELKHEQQQKI----LKIKTEEIAAFQR 887
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEqnnrdIAGIKDKLAKIrearDRQLAVAEDDLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 888 KR---RSGSNGSVVSLEQQQK-----IEEQKKWLDQ---EMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLES 956
Cdd:pfam12128 420 LEselREQLEAGKLEFNEEEYrlksrLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 957 KRLRSSQALNEDIVRVS---SRLEHLEKELSEKSGQLRqgsAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSlls 1033
Cdd:pfam12128 500 RRDQASEALRQASRRLEerqSALDELELQLFPQAGTLL---HFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGS--- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1034 PEEERTLFQLDEAIEALDAAiEYKNEAITCRQRVLRASASLLSQCEMN---------LMAKLSYLSSSETRALlCKYFDK 1104
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVP-EWAASEEELRERLDKAEEALQSAREKQaaaeeqlvqANGELEKASREETFAR-TALKNA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1105 VVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQR--LEMDRQLTLQQ-----KEHEQNMQLLLQQ-------SR 1170
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqLDKKHQAWLEEqkeqkREARTEKQAYWQVvegaldaQL 731
|
490 500
....*....|....*....|....*..
gi 2217301032 1171 DHLGEGLADSRRQYEARIQALEKELGR 1197
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKR 758
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
700-1189 |
1.06e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAEQVR--AELSEGQRQ--LRELEGKELQDA 775
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKtnGLLHTEDREeeIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 776 GERSRLQEFRRRVAAAQSQVQVLKEK-----------KQATERLV-SLSAQsEKRLQELERNVQLMRQQQGQLQRRLREE 843
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKletltnqnsdcKQHIEVLKeSLTAK-EQRAAILQTEVDALRLRLEEKESFLNKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 844 TEQKRRLEAEMSKRQHRVKELelkheqqQKILKIKTEEIAAFQRKrrsgsngsVVSLEQQQKieEQKKWLDQEMEKV--L 921
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDL-------KDMLDVKERKINVLQKK--------IENLQEQLR--DKDKQLAGLKERVksL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 922 QQRR-----ALEELGEELHKREAILakkEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLR--QGS 994
Cdd:pfam10174 428 QTDSsntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEH 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 995 AQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLrQGSLL----SPEEERTLFQLDEAIEALDAAIE-YKNEAITCRQRVLR 1069
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKL-ENQLKkahnAEEAVRTNPEINDRIRLLEQEVArYKEESGKAQAEVER 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1070 ASAsLLSQCEMNLMAKLSYLSSSETRALLcKYFDKVVTLREEQHQQQIAFSELEMQLEE------------QQRLVYWLE 1137
Cdd:pfam10174 584 LLG-ILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEarrrednladnsQQLQLEELM 661
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2217301032 1138 VALERQRLEMDrqltlQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQ 1189
Cdd:pfam10174 662 GALEKTRQELD-----ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILE 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
735-1199 |
1.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 735 LNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLsaq 814
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 815 sEKRLQELERNVQLMRQQqgqlqrrlreETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQrkrrsgsn 894
Cdd:COG4717 145 -PERLEELEERLEELREL----------EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ-------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 895 gsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGL----ESKRLRSSQALNEDIV 970
Cdd:COG4717 206 ------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 971 RVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKlrqgslLSPEEERTLFQLDEAIEAL 1050
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPD------LSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1051 DAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEmqLEEQQ 1130
Cdd:COG4717 353 LREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEELEELEEQLEELL--GELEE 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 1131 RLVYWLEVALERQRLEMDRQLTLQQKEHEQNM-------QLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYM 1199
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
694-1195 |
1.28e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.82 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 694 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAEQVRAELSEGQRQL------ 764
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknelse 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 765 --RELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLrE 842
Cdd:pfam05557 116 lrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK-S 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 843 ETEQKRRLEAEMSKRQHRVKELelkHEQQQKILKIKtEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQ 922
Cdd:pfam05557 195 ELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRK-----------LEREEKYREEAATLELEKEKLEQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 923 QRRALEELG----------EELHKR-EAILAKKEALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKSG 988
Cdd:pfam05557 260 ELQSWVKLAqdtglnlrspEDLSRRiEQLQQREIVLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHKA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 989 QLRQgsaqSQQQIRgeidSLRQEKDsLLKQRLEidgklRQGSLLSPEEerTLFQLDEAI-EALDAAIEYKNEAITCRQRV 1067
Cdd:pfam05557 340 LVRR----LQRRVL----LLTKERD-GYRAILE-----SYDKELTMSN--YSPQLLERIeEAEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1068 ---LRASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQR 1144
Cdd:pfam05557 404 svaEEELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERRC 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2217301032 1145 LEMDRQLTLQQK-EHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKEL 1195
Cdd:pfam05557 476 LQGDYDPKKTKVlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
701-1028 |
3.16e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.90 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 701 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQE----AEQVRAELSEGQRQLRELEGK---ELQ 773
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKideEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 774 DAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 853
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 854 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEE 929
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 930 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNED---------IVRVSSRLEHLEKELSEKSGQLRQGSA--QSQ 998
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeennkeeeEERNKRLLLAKEELGKVNLMAIEEFEEkeERY 990
|
330 340 350
....*....|....*....|....*....|
gi 2217301032 999 QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ 1028
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
714-1041 |
5.08e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 714 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFRRRVAAAQS 793
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 794 QVQVLKEKKQATerlvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVkeLELKHEQQ-- 871
Cdd:COG1340 72 KVKELKEERDEL----------NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV--LSPEEEKElv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 872 QKILKIKTEeiaafqrkrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK-REAILAKKEALMQE 950
Cdd:COG1340 140 EKIKELEKE-------------------LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIEL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 951 KTGLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRL-EIDGKLRQG 1029
Cdd:COG1340 201 YKEADELR-KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAeEIFEKLKKG 279
|
330
....*....|..
gi 2217301032 1030 SLLSPEEERTLF 1041
Cdd:COG1340 280 EKLTTEELKLLQ 291
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
741-1209 |
5.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 741 QRIRELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFRRRVAAAQSQVQVLKEKKQATERLvslsaqsEKRLQ 820
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEI----------SSELPELREELEKLEKEVKELEELKEEIEEL-------EKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 821 ELERNvqlmrqqqgqlqrrlreeteqKRRLEAEMSKRQHRVKELELKHEQQQKILKiKTEEIAAFQRKRRSGSngsvvsl 900
Cdd:PRK03918 249 SLEGS---------------------KRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLS------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 901 EQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREailAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEH 978
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 979 LEKELSEKsgqlrqgsaqSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKN 1058
Cdd:PRK03918 377 LKKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1059 EAITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEV 1138
Cdd:PRK03918 437 KCPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKEL 501
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217301032 1139 ALERQRLEmdrqltlqQKEHEQNMQLLLQQSRDHlgEGLADSRRQYEARIQALEKELGRYmwinQELKQKL 1209
Cdd:PRK03918 502 AEQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKL----EELKKKL 558
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
709-1146 |
5.38e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 709 RELAINIRMKEELIGELvRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERSRLQEFRRRV 788
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 789 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLEAEMSKRQHRVKELELK 867
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 868 HEQQQKILKIKTEEIAAFQRKRR-------SGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQ---------QRRALEELG 931
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERlkearllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfllLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 932 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIR--------- 1002
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1003 GEIDSLR------QEKDSLLKQRLEIDGKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAIT-CRQRVLRASAs 1073
Cdd:COG4717 382 EDEEELRaaleqaEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEeLREELAELEA- 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 1074 llsqcemnlmaKLSYLSSSETrallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVY---WLEVALERQRLE 1146
Cdd:COG4717 461 -----------ELEQLEEDGE-------------LAELLQELEELKAELRELAEEWAALKLaleLLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1216 |
5.48e-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: 51.21 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 842 EETEQK--------RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSLEQqqKIEEQKKWL 913
Cdd:TIGR02168 175 KETERKlertrenlDRLEDILNELERQLKSLERQAEKAERYKELKAEL----RELELALLVLRLEELRE--ELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 914 DQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKSGQLRQ 992
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISrLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 993 GSAQSQQQIRgEIDSLRQEKDSLLKQRLEIDGKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNeaitcrqrvlrasa 1072
Cdd:TIGR02168 328 LESKLDELAE-ELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLR-------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1073 sllsqcemnlmaklsylsssetrallckyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywlevalERQRLEmDRQLT 1152
Cdd:TIGR02168 386 ------------------------------SKVAQLELQIASLNNEIERLEARLERLED---------RRERLQ-QEIEE 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217301032 1153 LQQKEHEQNMQLLlQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKLGGVNAVG 1216
Cdd:TIGR02168 426 LLKKLEEAELKEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
718-1060 |
1.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 718 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAelSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQsqvqv 797
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----- 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 798 lkeKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAemskrQHRVKELELKHEQQQKILKI 877
Cdd:PTZ00121 1177 ---KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 878 KT-EEIAAFQRKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELHKREAILAKKEAlMQEKTGLES 956
Cdd:PTZ00121 1249 RNnEEIRKFEEARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 957 KRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQiRGEIDSLRQE----KDSLLKQRLEIDGKLRQGSLL 1032
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKK 1399
|
330 340
....*....|....*....|....*...
gi 2217301032 1033 SPEEERTLFQLDEAIEALDAAIEYKNEA 1060
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
698-1159 |
1.19e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 698 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGE 777
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 778 RSRLQEFRRRVAAAQSQvQVLKEKKQATERLVSLSA---QSEKRLQELERNVQL-------MRQQQGQLQRRLREETEQK 847
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLE-ELREERDELREREAELEAtlrTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 848 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsVVSLEQQQKIEEQKkwLDQEMEKVLQQRRAL 927
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDR----------------IERLEERREDLEEL--IAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 928 EELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK--ELSEKSGQLRQ--GSAQSQQQIRG 1003
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDeiERLREKREALA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1004 EIDSLRQEKDSLLKQRL-EIDGKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCE--- 1079
Cdd:PRK02224 620 ELNDERRERLAEKRERKrELEAEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelr 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1080 ---MNLMAKLSYLSS--SETRALLCKYFDkvvtLREEQHQQQIafSELEMQLEEQQRLVYWLEvALERQRLEMDRQLTLQ 1154
Cdd:PRK02224 698 errEALENRVEALEAlyDEAEELESMYGD----LRAELRQRNV--ETLERMLNETFDLVYQND-AYSHIELDGEYELTVY 770
|
....*
gi 2217301032 1155 QKEHE 1159
Cdd:PRK02224 771 QKDGE 775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
694-1077 |
1.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 694 ATASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQ 773
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 774 DAGERSRLQEFRRRVAAAQSQVQVLKEK---------KQATERLVSLS---AQSEKRLQELERNVQLMRQQQGQLQRRLR 841
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlslateeelQDLAEELEELQqrlAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 842 EETEQKRRLEAEMSKR--------------------------------------QHRVKELELKHEQQQKILKIKTEEIA 883
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 884 AFQRKRRSGSNGsvvsLEQQQKIEEQKKWLDQeMEKVLQQRRALEELGEELhKREAILAKKEALMQEKTGLESKRLRSSQ 963
Cdd:COG4717 318 EEELEELLAALG----LPPDLSPEELLELLDR-IEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 964 ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQ--------QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQgsllsPE 1035
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREELAELEAELEQ-----LE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2217301032 1036 EERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1077
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
691-1022 |
1.77e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 691 VPPATASEWRLAQAQQKIRELainIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEG- 769
Cdd:pfam07888 26 VPRAELLQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 770 -KELQDAGERsrlqefrrrvaaaqsqvqvLKEKKQAterLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKR 848
Cdd:pfam07888 103 yKELSASSEE-------------------LSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 849 RLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 928
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 929 ELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKSGQLRQGSAQSQQQIRGEID 1006
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQ 311
|
330
....*....|....*.
gi 2217301032 1007 SLRQEKDSLLKQRLEI 1022
Cdd:pfam07888 312 SAEADKDRIEKLSAEL 327
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
694-1062 |
1.84e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 694 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAEQVRAELSEG-QRQLREL 767
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlTRRMQRG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 768 E--GKELQDAGE--RSRLQEFRRRVAAAQSQVQVLKEKKQA-TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLRE 842
Cdd:TIGR00618 534 EqtYAQLETSEEdvYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 843 ETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQKIEEQK 910
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQSEKEQLT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 911 KWLD----------QEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQALNEDIVRVSSR---- 975
Cdd:TIGR00618 694 YWKEmlaqcqtllrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKeLMHQARTVLKARTEAHFNNNEEvtaa 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 976 ------LEHLE-------KELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQ 1042
Cdd:TIGR00618 774 lqtgaeLSHLAaeiqffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
410 420
....*....|....*....|
gi 2217301032 1043 LDEAIEALDAAIEYKNEAIT 1062
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQ 873
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
694-937 |
1.90e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 694 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQ 773
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-SELE 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 774 DAGERS-----RLQEFRRRVAAAQSQVQVL----KEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET 844
Cdd:TIGR02168 877 ALLNERasleeALALLRSELEELSEELRELeskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 845 EQK-RRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFqrkrrsgsnGSV--VSLEQQQKIEEQKKWLDQEMEKVL 921
Cdd:TIGR02168 957 EALeNKIEDDEEEARRRLKRLE--------------NKIKEL---------GPVnlAAIEEYEELKERYDFLTAQKEDLT 1013
|
250
....*....|....*.
gi 2217301032 922 QQRRALEELGEELHKR 937
Cdd:TIGR02168 1014 EAKETLEEAIEEIDRE 1029
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
737-1195 |
2.26e-05 |
|
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: 49.27 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 737 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAG---ERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSA 813
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 814 --------------QSEKRLQELERNVQLMRQQQgqlqrrlreETEQKRrLEAEMSKRQHRVKELELKHEQQQKILKIKT 879
Cdd:TIGR00606 674 denqsccpvcqrvfQTEAELQEFISDLQSKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 880 EEIAAFQRKRRSGSNGSVvslEQQQKIEEQKKWL-----DQEMEKVLQQR-RALEELGEELHKREAILAKKEALMQEKTG 953
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 954 leskrLRSSQALNEdivRVSSRLEHLEKELSEksGQLRQGSAQSQQQirgEIDSLRQEKDSLLKQRLEIDGKLRQGSLLS 1033
Cdd:TIGR00606 821 -----DRTVQQVNQ---EKQEKQHELDTVVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1034 PEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTL 1108
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDG 967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1109 REEQ-HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQ----------LTLQQKEHEqnMQLLLQQSRDHLGEGL 1177
Cdd:TIGR00606 968 KDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQkiqerwlqdnLTLRKRENE--LKEVEEELKQHLKEMG 1045
|
490
....*....|....*...
gi 2217301032 1178 ADSRRQYEARIQALEKEL 1195
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENI 1063
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
737-1019 |
2.32e-05 |
|
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: 48.80 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 737 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERSRLQEFRRRVAAAQSQVQVLKEkkqaterlvslsaqSE 816
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAEAEQELEESKRE--------------TE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 817 KRLQELERNVQLMRQQQGQLQRRLREETEQ------KRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 890
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 891 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK--REAILAKKEALMQEKTGLESKRLRSSQALNED 968
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKvmREADEESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217301032 969 IVRVSSRL----EHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQR 1019
Cdd:COG5185 487 LTQIESRVstlkATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
725-857 |
3.42e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 725 LVRTGKAAQALNRQHSQ----------RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQ 794
Cdd:PRK09510 54 MVDPGAVVEQYNRQQQQqksakraeeqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301032 795 VQvlKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 857
Cdd:PRK09510 134 AE--EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1195 |
4.06e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 847 KRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQRR 925
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrELSSLQSELRRIENRLDELSQELSDA-----------SRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 926 ALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEksgqlrqgsaQSQQQIRGEI 1005
Cdd:TIGR02169 738 RLEELEEDL---SSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDLEARLSH----------SRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1006 DSLRQEKDSLLKQRLEIDGKLRQgslLSPEEErtlfQLDEAIEALDAAIEYKNEAITCRQRVLRasasllsqcemNLMAK 1085
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNR---LTLEKE----YLEKEIQELQEQRIDLKEQIKSIEKEIE-----------NLNGK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1086 LsylssSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1165
Cdd:TIGR02169 863 K-----EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
330 340 350
....*....|....*....|....*....|
gi 2217301032 1166 LQQSRDHLGEGLADSRRQYEARIQALEKEL 1195
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
738-1074 |
5.40e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 738 QHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSR---LQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSA 813
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 814 QSE----------KRLQELERNVQLMRQQQGQLQRrlreetEQKRRLEAEMSKrqhrvkeLELKHEQQQKILKIKTEEIA 883
Cdd:PRK11281 157 QPEraqaalyansQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 884 AFQrKRRSGSNgsvvslEQQQKIEEQKkwldQEMEKVLQQRRAleELGEElHKREAILAKKEALMQE----KTGLE---- 955
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQL----QLLQEAINSKRL--TLSEK-TVQEAQSQDEAARIQAnplvAQELEinlq 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 956 -SKRL-RSSQALNE---DIVRVSSRLEHL---EKELSEKSGQLrQGS------AQSQQQ-----------------IRGE 1004
Cdd:PRK11281 290 lSQRLlKATEKLNTltqQNLRVKNWLDRLtqsERNIKEQISVL-KGSlllsriLYQQQQalpsadliegladriadLRLE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1005 IDSLRQEKDSLLKQRLEIDgKL--RQGSLLSPEEERTLFQ--------LDEAIEALDAAIeykNEAITC---RQRVLRAS 1071
Cdd:PRK11281 369 QFEINQQRDALFQPDAYID-KLeaGHKSEVTDEVRDALLQllderrelLDQLNKQLNNQL---NLAINLqlnQQQLLSVS 444
|
...
gi 2217301032 1072 ASL 1074
Cdd:PRK11281 445 DSL 447
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
700-826 |
7.87e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALnrqhsQRIRELEQEAEQVRAELSEG-------QRQLRELEgKEL 772
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR-----AQLAELEAELAELSARYTPNhpdvialRAQIAALR-AQL 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217301032 773 QDAGERSrLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 826
Cdd:COG3206 308 QQEAQRI-LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
842-1060 |
8.49e-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: 46.68 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 842 EETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEkvl 921
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 922 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALN-------EDIVRVSSRLEHLEKELSEKSGQLRQGS 994
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 995 AQSQQQiRGEIDSLRQEKDSLLKQrLEIDGKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEA 1060
Cdd:COG4942 181 AELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
961-1195 |
1.02e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 961 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRqgsllspEEERTL 1040
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1041 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1119
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301032 1120 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNMQLLLQQSRDHLGE--GLADSRRQYEARIQALEKEL 1195
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
915-1055 |
1.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 915 QEMEKVLQQRRALE---ELGEELHKREAILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 979
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 980 EKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1055
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
700-985 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQAL---------NRQHSQRIRELEQEaeqvRAELSEGQRQLRELEgK 770
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAE----LERLDASSDDLAALE-E 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 771 ELQDAgeRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 850
Cdd:COG4913 693 QLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 851 EAEMSKRQHRVKelELKHEQQQKILKIkteeIAAFQRKRRSGSNGSVVSLEqqqkieeqkkwldqEMEKVLQQRRALEEL 930
Cdd:COG4913 768 RENLEERIDALR--ARLNRAEEELERA----MRAFNREWPAETADLDADLE--------------SLPEYLALLDRLEED 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2217301032 931 GEELHKREAILAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 985
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
741-929 |
1.35e-04 |
|
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: 44.92 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 741 QRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAgeRSRLQEFRRRVAAAQSQVQVLKEK-KQATERLvsLSAQSEKRL 819
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALE-ARLEAA--KTELEDLEKEIKRLELEIEEVEARiKKYEEQL--GNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 820 QELERnvqlmrqqqgqlqrrlrEETEQKRRLeaemSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 899
Cdd:COG1579 92 EALQK-----------------EIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|
gi 2217301032 900 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE 929
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
780-1028 |
1.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslsAQSEKRLQELERnvQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 859
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERY----AAARERLAELEY--LRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 860 RVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHkrea 939
Cdd:COG4913 310 ELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLEALLAALG---- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 940 ilakkEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQGsaqsqqqiRGEIDSLRQEKDSLLKQR 1019
Cdd:COG4913 373 -----LPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDL--------RRELRELEAEIASLERRK 435
|
....*....
gi 2217301032 1020 LEIDGKLRQ 1028
Cdd:COG4913 436 SNIPARLLA 444
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
742-1193 |
1.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 742 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQ-----------EFRRRVAAAQSQVQVL-KEKKQATERLV 809
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 810 SLSAQ------SEKRLQELeRNVQLMRQQQGQLQRRLREETEQ-----KRRLEAEMSKRQHRVKELELKHEQQQKILKIK 878
Cdd:pfam01576 163 EFTSNlaeeeeKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 879 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE----ELGEELH------------------- 935
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEkqrrDLGEELEalkteledtldttaaqqel 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 936 --KREAILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKSgqlRQGSAQSQQQIRGEID 1006
Cdd:pfam01576 322 rsKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1007 SLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKL 1086
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1087 SYLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNMQLL- 1165
Cdd:pfam01576 475 ELL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLe 541
|
490 500
....*....|....*....|....*....
gi 2217301032 1166 -LQQSRDHLGEGLADSRRQYEARIQALEK 1193
Cdd:pfam01576 542 aLEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
718-1022 |
1.91e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 718 KEELIGELVRTGKAAQALNRQHS---QRIRELEQEAEQVRAELSEgqrqLRELEGK------ELQDAGERSRLQEFRRRV 788
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEE----LKKAKGKcpvcgrELTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 789 AAAQSQVQVLKEK-KQATERLVS----LSAQSE--------KRLQELERNVQLMRQQQGQLQRRLREETEQK-RRLEAEM 854
Cdd:PRK03918 462 KRIEKELKEIEEKeRKLRKELRElekvLKKESEliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEI 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 855 S---KRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQ-QKIEE-QKKWL---DQEMEKVLQQRRa 926
Cdd:PRK03918 542 KslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPfYNEYLelkDAEKELEREEKE- 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 927 LEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQalnEDIVRVSSRLEHLEKELSEKSGQLrQGSAQSQQQIRGEI 1005
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKeLEELEKKYSE---EEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTL 696
|
330
....*....|....*..
gi 2217301032 1006 DSLRQEKDSLLKQRLEI 1022
Cdd:PRK03918 697 EKLKEELEEREKAKKEL 713
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
747-1159 |
2.39e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 747 EQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEfrrrvaAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 826
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 827 qlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 906
Cdd:pfam01576 85 --------------EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 907 EEQKKWLDQEMEKVLQQRRALEELGEEL----HKREAI-------LAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 975
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLsklkNKHEAMisdleerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 976 LEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDsLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1055
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1056 YKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFSELEMQLEEQQRLVYW 1135
Cdd:pfam01576 310 DTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALEELTEQLEQAKRNKAN 374
|
410 420
....*....|....*....|....*...
gi 2217301032 1136 LE---VALERQRLEMDRQL-TLQQKEHE 1159
Cdd:pfam01576 375 LEkakQALESENAELQAELrTLQQAKQD 402
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
801-1151 |
3.15e-04 |
|
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: 45.35 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 801 KKQATERLVSLSAQSEKRLQELERNVQL--MRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIK 878
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 879 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKR 958
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE--ELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 959 LRSS------QALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRgEIDSLRQEKDSLLKQRLEIDGKLRQGSLL 1032
Cdd:pfam02463 307 RRKVddeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1033 SPEEERTLFQLDEAIEALDAAIEYKNEAitcRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQ 1112
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLEL---ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217301032 1113 HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL 1151
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
792-1060 |
3.27e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 792 QSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 871
Cdd:COG1340 7 SSSLEELEEKI---EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 872 QKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQEMEKVLQQRraLEELGEELHKREAILAKKEA 946
Cdd:COG1340 84 NEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPEEEKELVEK--IKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 947 LMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKSGQLRqgsaQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKL 1026
Cdd:COG1340 162 LKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----EEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270
....*....|....*....|....*....|....
gi 2217301032 1027 RQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1060
Cdd:COG1340 226 DE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
683-875 |
3.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 683 KARVQARQVPPATASEW---RLAQAQQKIRELAINI---RMKEELIgelvrtgkAAQALNRQHSQRIRELEQEAEQVRAE 756
Cdd:COG3206 163 EQNLELRREEARKALEFleeQLPELRKELEEAEAALeefRQKNGLV--------DLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 757 LSEGQRQLRELEGK------ELQDAGERSRLQEFRRRVAAAQSQVQVLKEK--------KQATERLVSLSAQSEKRLQEL 822
Cdd:COG3206 235 LAEAEARLAALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217301032 823 ERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKIL 875
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
843-985 |
3.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 843 ETEQKRRLEAEMSKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 921
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217301032 922 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 985
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
783-1128 |
4.59e-04 |
|
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: 44.67 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 783 EFRRRVAAAqsqvqvLKEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrRLREETE-------QKRRLEAEMS 855
Cdd:TIGR02169 167 EFDRKKEKA------LEELEEVEENIERLDLIIDEKRQQLER--------------LRREREKaeryqalLKEKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 856 KRQHRVKELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVSLEQQQKiEEQKKWLDQEMEKVLQQRRALEELGEELH 935
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTE-EISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 936 KREAILAKKEALMQEktgLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQ----------SQQQIRGEI 1005
Cdd:TIGR02169 305 SLERSIAEKERELED---AEERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1006 DSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEER---TLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNL 1082
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2217301032 1083 MaklsylsssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1128
Cdd:TIGR02169 458 E---------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
782-1027 |
5.07e-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: 44.83 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 782 QEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 860
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 861 VKELELKHEQQQKILKIKTEeiAAFQRKRRSGSNGSVVSLEQQQKIEEQKK----WLDQEMEKVLQQRRA---------- 926
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQ--AWLEEQKEQKREARTEKQAYWQVVEGALDaqlaLLKAAIAARRSGAKAelkaletwyk 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 927 --LEELG---EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV----RVSSRLEHLEKELSEKSGQLrqgsAQS 997
Cdd:pfam12128 758 rdLASLGvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQL----ARL 833
|
250 260 270
....*....|....*....|....*....|
gi 2217301032 998 QQQIRGEIDSLRQEKDSLLKQRLEIDGKLR 1027
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
932-1195 |
5.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 932 EELHKREAILAKKEALMQEKTGLeSKRLRSSQALNEDIVRVSSRLEHLEKELseksgqlrQGSAQSQQQIRGEIDSLRQE 1011
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1012 KDSLLKQRLEiDGKLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSS 1091
Cdd:PRK11281 110 NDEETRETLS-TLSLRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1092 SETRAllckyfdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQL--LLQQS 1169
Cdd:PRK11281 168 NSQRL------------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQ 228
|
250 260
....*....|....*....|....*.
gi 2217301032 1170 RDHLgegladsrrqyEARIQALEKEL 1195
Cdd:PRK11281 229 RDYL-----------TARIQRLEHQL 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
700-1049 |
8.20e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELsEGQRQLRELEGKELQDAGErs 779
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGE-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 rlqefrrrvaaaqsQVQVLKEKKQATerLVSLSAQSEKRLQElernvqlmrqqqgqlqrrLREETEQKRRLEAEMSKRQH 859
Cdd:pfam01576 300 --------------ELEALKTELEDT--LDTTAAQQELRSKR------------------EQEVTELKKALEEETRSHEA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 860 RVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKVLQQRRALEElgeelHKRE 938
Cdd:pfam01576 346 QLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RTLQQAKQDSE-----HKRK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 939 ailaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQ-----GSAQSQQQirgEIDSLRQEKD 1013
Cdd:pfam01576 409 ----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvSSLESQLQ---DTQELLQEET 481
|
330 340 350
....*....|....*....|....*....|....*...
gi 2217301032 1014 sllKQRLEIDGKLRQgsllsPEEERT--LFQLDEAIEA 1049
Cdd:pfam01576 482 ---RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
692-958 |
9.92e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 692 PPATASEWRLAQAQ----QKIRELAINIRMKEELIGELVRTGKAAQALnrqhSQRIRELEQEAEQVRAElsEGQRQLREL 767
Cdd:COG4913 220 EPDTFEAADALVEHfddlERAHEALEDAREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLW--FAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 768 EGKELQDAGERSRLQEfrrRVAAAQSQVQVLKEKKQATERlvSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreeteQK 847
Cdd:COG4913 294 EAELEELRAELARLEA---ELERLEARLDALREELDELEA--QIRGNGGDRLEQLER---------------------EI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 848 RRLEAEMSKRQHRVKELelkhEQQQKILKIKT-EEIAAFQRKRRsgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRA 926
Cdd:COG4913 348 ERLERELEERERRRARL----EALLAALGLPLpASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270
....*....|....*....|....*....|..
gi 2217301032 927 LEElgeelhkreailaKKEALMQEKTGLESKR 958
Cdd:COG4913 417 LRR-------------ELRELEAEIASLERRK 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
742-932 |
1.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 742 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQ 820
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 821 ELERNVQLMRQQQGQLQRRLREET-----EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsng 895
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK------ 710
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217301032 896 svvslEQQQKIEEQKKWLDQEMEKV-----LQQRRALEELGE 932
Cdd:PRK03918 711 -----KELEKLEKALERVEELREKVkkykaLLKERALSKVGE 747
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
900-1194 |
1.86e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 900 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILakkealmqEKTGLESKRLRS-----SQALNEDIVR--- 971
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL--------EAAEEEVDSLKSqladyQQALDVQQTRaiq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 972 ---VSSRLEHLEK-----ELSEKSGQLRQGSAQSQQQirgEIDSLRQEkdslLKQRLEIDGKLRQgsllspeeertlfQL 1043
Cdd:COG3096 415 yqqAVQALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1044 DEAIEAL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT-- 1107
Cdd:COG3096 475 EKAYELVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaa 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1108 --LREEQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NMQLLLQQSRDHLGEGLA 1178
Cdd:COG3096 553 eeLEELLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALA 623
|
330
....*....|....*.
gi 2217301032 1179 DSRRQYEARIQALEKE 1194
Cdd:COG3096 624 DSQEVTAAMQQLLERE 639
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
696-949 |
1.87e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 696 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDA 775
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 776 GERSRLqefrrrVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE----QKRRLE 851
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 852 AEMSKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 924
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 2217301032 925 RALEELGEELHKREAILAKKEALMQ 949
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
700-1204 |
2.90e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQdagers 779
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE-EDLQ------ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 rlqefrrrvAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 859
Cdd:pfam05483 321 ---------IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 860 RVKEL-ELKHEQQQKILKIKT----EEIAAFQRKrrsgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRaleelgEEL 934
Cdd:pfam05483 392 ELEEMtKFKNNKEVELEELKKilaeDEKLLDEKK-------------QFEKIAEELKGKEQELIFLLQARE------KEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 935 HKRE----AILAKKEALMQE----KTGLESKRLRSSQAL---------NEDIVRVSSRL-----EHLEKELSEKSGQLR- 991
Cdd:pfam05483 453 HDLEiqltAIKTSEEHYLKEvedlKTELEKEKLKNIELTahcdkllleNKELTQEASDMtlelkKHQEDIINCKKQEERm 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 992 ----QGSAQSQQQIRGEIDSLRQEkdsLLKQRLEIDGKL-------RQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1060
Cdd:pfam05483 533 lkqiENLEEKEMNLRDELESVREE---FIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1061 ITCRQRVLRAsasllsqcemnlmakLSYLSSSETRALLCkYFDKVVTLREEQHQQQIAFSEL----EMQLEEQQRLVYWL 1136
Cdd:pfam05483 610 IEELHQENKA---------------LKKKGSAENKQLNA-YEIKVNKLELELASAKQKFEEIidnyQKEIEDKKISEEKL 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301032 1137 EVALERQRLEMDRQLTLQQKeheqnMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQE 1204
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
691-896 |
2.91e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 691 VPPATASEWRLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAEQVRAELSEGQRQLREL 767
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 768 E---GKELQDAGERSR-------------LQEFRRRVAA----AQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQ 827
Cdd:COG3883 85 ReelGERARALYRSGGsvsyldvllgsesFSDFLDRLSAlskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217301032 828 LMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGS 896
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
733-1018 |
3.22e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 733 QALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAA----QSQVQVLK-EKKQATER 807
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSglkkDSKLKSLEiAVEQKKEE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 808 LVSLSAQSEK----------------RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 871
Cdd:pfam10174 533 CSKLENQLKKahnaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 872 QKILKIKTEEIAAFQRKRRSGSngsvvsleqQQKIEEQKKWLDQEMEKVLQQR-----RALEELGEELHKREAILAKKEA 946
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKG---------AQLLEEARRREDNLADNSQQLQleelmGALEKTRQELDATKARLSSTQQ 683
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217301032 947 LMQEKTG-LESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQ--LRQGSAQSQQQIRGEIDSLRQEKDSLLKQ 1018
Cdd:pfam10174 684 SLAEKDGhLTNLRAERRKQLEE---ILEMKQEALLAAISEKDANiaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
740-1194 |
3.36e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 740 SQRIRELEQEAEQVRAELSEGQRQLRELEgkelqdagersrlqefrrrvAAAQSQVQVLKEKKQatERLVSLSAQSEKRL 819
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALK--------------------SESQNKIELLLQQHQ--DRIEQLISEHEVEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 820 QELERNVQLMRQQQGQLQRRLREETEQKRRLEA----EMSKRQHRVKELELKHEQQQKILKIKTEEIaafqRKRRSGSNG 895
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEEL----EKQLVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 896 SVVSLE-QQQKIEEQKKWLDQEMEKVLQqrraleelgeELHKREailaKKEALMQEktglESKRLRSSQALNedivrvSS 974
Cdd:pfam15921 357 ELTEARtERDQFSQESGNLDDQLQKLLA----------DLHKRE----KELSLEKE----QNKRLWDRDTGN------SI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 975 RLEHLEKELSEKSGQLRQGSA-----------QSQQQ---IRGEIDSLrqEKDSLLKQRLE--------IDGKLRQGSLL 1032
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEAllkamksecqgQMERQmaaIQGKNESL--EKVSSLTAQLEstkemlrkVVEELTAKKMT 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1033 SPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrVLRASASLLSQCEMNLMAKLSYLSSSETRA----LLCKYFDKVVtl 1108
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEIT----KLRSRVDLKLQELQHLKNEGDHLRNVQTECealkLQMAEKDKVI-- 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1109 reEQHQQQIafsELEMQLEEQQ-RLVYWLEValERQRLEM---DRQLTLQQKEheqnmqlLLQQSRDhlgeglaDSRRQY 1184
Cdd:pfam15921 565 --EILRQQI---ENMTQLVGQHgRTAGAMQV--EKAQLEKeinDRRLELQEFK-------ILKDKKD-------AKIREL 623
|
490
....*....|
gi 2217301032 1185 EARIQALEKE 1194
Cdd:pfam15921 624 EARVSDLELE 633
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
746-963 |
3.94e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 746 LEQEAEQVRAELSEGQRQLRElegkelqdagERSRLQ-EFRRRVAAAQSQVQVLKEKKQAT-ERLVSLSAQSEKRLQELE 823
Cdd:pfam07111 468 PPPPAPPVDADLSLELEQLRE----------ERNRLDaELQLSAHLIQQEVGRAREQGEAErQQLSEVAQQLEQELQRAQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 824 RNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH--------RVKELELKHEQQQKILKIKTEEIAAFQRKrrsgsng 895
Cdd:pfam07111 538 ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqeKVAEVETRLREQLSDTKRRLNEARREQAK------- 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217301032 896 SVVSLEQQQKIEEQKKWLDQEMEKVlqQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQ 963
Cdd:pfam07111 611 AVVSLRQIQHRATQEKERNQELRRL--QDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQ 676
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
702-821 |
4.40e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 702 AQAQQKIRELAINIrmkEELIGELvrtgkaaQALNRQHSQRIRELE---QEAEQVRAELSEGQRQLRELEGKELQDAger 778
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASL-------EELERELEQKAEEAEallKEAEKLKEELEEKKEKLQEEEDKLLEEA--- 571
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2217301032 779 srLQEFRRRVAAAQSQV-QVLKEKKQatERLVSLSAQSEKRLQE 821
Cdd:PRK00409 572 --EKEAQQAIKEAKKEAdEIIKELRQ--LQKGGYASVKAHELIE 611
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
700-822 |
4.96e-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: 40.90 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 779
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2217301032 780 RLQefrRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQEL 822
Cdd:COG4942 189 ALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
700-1199 |
5.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAEQVRAELSEGQRQLRELEGKElqDAGERS 779
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 859
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 860 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 920
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 921 L---------------QQRRALEE--LGEELHKREAILAKKEALMQE------------KTGLESKRLRSSQALNEDIVR 971
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPRldpdslagkldfKPHPFRAWLEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 972 VSS--RLEHLEKELSeKSGQLRQGSAQSQQQIRGEIDSLR------QEKDSLLKQRLEidgklrqgsllspEEERTLFQL 1043
Cdd:COG4913 564 VDSpeELRRHPRAIT-RAGQVKGNGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELA-------------ELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1044 DEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQI 1117
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1118 AFSELEMQLE-----------EQQRLVYWLEVALER-QRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYE 1185
Cdd:COG4913 700 ELEELEEELDelkgeigrlekELEQAEEELDELQDRlEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
570
....*....|....
gi 2217301032 1186 ARIQALEKELGRYM 1199
Cdd:COG4913 780 ARLNRAEEELERAM 793
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
788-920 |
5.72e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 788 VAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrLREETEQ-KRRLEAEMSKRQHRVKELE 865
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217301032 866 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV 920
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKK 623
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
780-1055 |
6.88e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 780 RLQEFRRRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------KRLQELErnvqlmrqqqgqlqRRLREETEQKRRLE 851
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 852 AEMSKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 928
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 929 ELGEElhkREAILAkkealmqeKTGLESKrlrssqalneDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSL 1008
Cdd:PRK02224 290 ELEEE---RDDLLA--------EAGLDDA----------DAEAVEARREELEDRDEELRDRLEE-CRVAAQAHNEEAESL 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1009 RQEKDSLlkqRLEIDGKLRQGSLLSPEEERTLFQLD---EAIEALDAAIE 1055
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIE 394
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
737-1021 |
7.08e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 737 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS-------RLQEFRRRVAAAQSQVQVLKEK-KQA---- 804
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKsqnslqeKLAQEKSRVADAEEKILELQQKlEHAhkvc 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 805 -TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRL------REETEQKRR--------LEAEMSKRQHRVKELELKHE 869
Cdd:pfam15742 145 lTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRklldqnVNELQQQVRslqdkeaqLEMTNSQQQLRIQQQEAQLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 870 QQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELHKReailakKEALM 948
Cdd:pfam15742 225 QLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEKHH 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217301032 949 QEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQsQQQIRGEIDSLRQEKDSLLKQRLE 1021
Cdd:pfam15742 281 HHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-967 |
8.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 700 RLAQAQQKIRELAINIRMKEELIGELVRTGKaaqalNRQHSQRIRELEQEAEQVRAE-LSEGQRQLRELEGKELQDAGER 778
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 779 SRLQEFRRRVAAAQSQVQVLKEKKQATE--------RLVSLSAQS----EKRLQELE---------RNVQLMRQQQGQLQ 837
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEeelaellkELEELGFESveelEERLKELEpfyneylelKDAEKELEREEKEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 838 RRLREETEQKRrleAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEM 917
Cdd:PRK03918 622 KKLEEELDKAF---EELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217301032 918 EKVLQQRRALEELGEELHKREAILAKKEALmQEKTgLESKRLRSSQALNE 967
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEEL-REKV-KKYKALLKERALSK 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
708-969 |
8.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 708 IRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQE---- 783
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEeles 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 784 -------FRRRVAAAQSQVQVLKEKKQATE----RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEA 852
Cdd:COG4372 106 lqeeaeeLQEELEELQKERQDLEQQRKQLEaqiaELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 853 EMSKRQHR---VKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEE 929
Cdd:COG4372 186 DELLKEANrnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217301032 930 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDI 969
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
856-1018 |
9.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 856 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 934
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 935 HKREAILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKSGQLrQGSAQSQQQIRGEIDSLRQE-- 1011
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEea 155
|
....*..
gi 2217301032 1012 KDSLLKQ 1018
Cdd:PRK12704 156 KEILLEK 162
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
740-1079 |
9.33e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 740 SQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRL----QEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQS 815
Cdd:PRK10929 101 NMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLpqqqTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 816 EK-----RLQELErnvqlmrqqqgqLQRRLREETEQKRRLEAEMSKRQHrvKELELKHEQQQKILKikteeiaaFQRKRR 890
Cdd:PRK10929 181 ESaalkaLVDELE------------LAQLSANNRQELARLRSELAKKRS--QQLDAYLQALRNQLN--------SQRQRE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 891 SGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEAL-----MQEKTGLESKR-----LR 960
Cdd:PRK10929 239 AER-----ALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQaasqtLQVRQALNTLReqsqwLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 961 SSQALNEDIVRVSSRLEHLEKelseksgqlrqgsaqsQQQIRGEIDSLRQEK----DSLLKQRLEIDGKLRQGSLLSPEE 1036
Cdd:PRK10929 314 VSNALGEALRAQVARLPEMPK----------------PQQLDTEMAQLRVQRlryeDLLNKQPQLRQIRQADGQPLTAEQ 377
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2217301032 1037 ERTlfqldeaieaLDAAIEYKNEAITcrqrvlrasaSLLSQCE 1079
Cdd:PRK10929 378 NRI----------LDAQLRTQRELLN----------SLLSGGD 400
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
779-1198 |
9.44e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 779 SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQ 858
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 859 HRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKRE 938
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 939 AILAKKEALMQEKTGLESKR------LRSSQALNEDIVRVSSRLEHLEKELSEKSG----------QLRQGSAQSQQQIR 1002
Cdd:PRK01156 343 KKKSRYDDLNNQILELEGYEmdynsyLKSIESLKKKIEEYSKNIERMSAFISEILKiqeidpdaikKELNEINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1003 GEIDSLRQEKDSLLKQRLEIDgklRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNE---AITCRQRVLRASASLLSQCE 1079
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELS---RNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEkksRLEEKIREIEIEVKDIDEKI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217301032 1080 MNLMAKLSYLSSSET-------------RALLCKYFDKVVTLREEQHQQQIAFSELE-MQLEE-QQRLVYWLEVALERQR 1144
Cdd:PRK01156 500 VDLKKRKEYLESEEInksineynkiesaRADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDlDSKRTSWLNALAVISL 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2217301032 1145 LEMDrqlTLQQKEHEQNMQLLLQQSRDHLGE-GLADSRRQYEARIQALEKELGRY 1198
Cdd:PRK01156 580 IDIE---TNRSRSNEIKKQLNDLESRLQEIEiGFPDDKSYIDKSIREIENEANNL 631
|
|
| |
