|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
1.49e-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: 1.49e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 95 QTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTASR-DIQLREDE 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 173 RGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRLPRPAPGQL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 251 VDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 203096856 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
9.66e-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: 9.66e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVT-------LGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 88 ATVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLevGTASRD 165
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMiGT-------PDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 166 IQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRlprpapGQLLV 245
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:smart00129 226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304
|
330 340 350
....*....|....*....|....*....|.
gi 203096856 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
2.78e-134 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 414.66 E-value: 2.78e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 21 RVRPLLPKELLHGHQSCLQVEPGLGRVTL-------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 94 GQTGSGKTYTMGEasvaslLEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 172 ERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpAPGQLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTG-----GEESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 252 DLAGSERVLKTG-STGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 203096856 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 |
2.95e-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: 388.15 E-value: 2.95e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKELLHGHqSCLQVEPG------LGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 89 TVFAYGQTGSGKTYTMGEASvasllEDEQGIVPRAMAEAFKLIDENDLLD--CLVHVSYLEVYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 167 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpaPGQLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 203096856 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 |
7.91e-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: 7.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELLHGHQSCLQV--------EPGLGRVTL--------------GRDRHFGFHVVLAEDAGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 153 FRDLLEvgTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 233 SRLPrpapgQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 203096856 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 |
2.69e-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: 2.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKEL---------LHGHQSCLQVEPGLGRVTLGRDRH---FGFHVVL----AED---AGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLID--ENDLLDCLVHVSYLEVYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 155 DLLEVGTASRDIQLREDE---RGNVVLcGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRgRA 231
Cdd:cd01365 157 DLLNPKPKKNKGNLKVREhpvLGPYVE-DLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 232 PSRLPRPAPgqlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQR-----RGSHIPYRDSKI 306
Cdd:cd01365 235 DAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 203096856 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 |
7.59e-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: 7.59e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTL--GRD------RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 88 ATVFAYGQTGSGKTYTMGEASVAsllEDEQGIVPRAMAEAFKLID-ENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 167 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQrgrapSRLPRPAPGQLLVS 246
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHIRVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01371 234 KLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANI 311
|
330 340
....*....|....*....|...
gi 203096856 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 |
2.88e-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: 2.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELLHG--------HQSCLQVEPGLGRvtlgrdrhFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 88 ATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 168 LREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPsrlprPAPGQLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 248 FHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 203096856 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 |
6.78e-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: 6.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELlHGHQSCLQVEPGLG-RVTL---GRDRH-FGFHVVLAEDAGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 91 FAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLIDENDLLDCLVH--VSYLEVYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTMEGP------PESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 166 IQLREDErGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLeqRGRAPSRlprpapGQLLV 245
Cdd:cd01366 156 IRHDSEK-GDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 203096856 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 |
2.53e-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: 2.53e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTL--------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 88 ATVFAYGQTGSGKTYTM-GEASVASLLEDEQ----GIVPRAMAEAFKLIDENDLlDCLVHVSYLEVYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 162 ASRDIQLREDER--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpa 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 240 pGQLLV--SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGN 317
Cdd:cd01364 237 -GEELVkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 203096856 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 |
3.86e-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: 3.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELLHGHQSCLQVEPGlGRVTLGRD---RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPE-DTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 93 YGQTGSGKTYTMgEASvaslLEDEQ--GIVPRAMAEAFKLIDEND-LLDCLVHVSYLEVYKEEFRDLLEVgtaSRD-IQL 168
Cdd:cd01369 83 YGQTSSGKTYTM-EGK----LGDPEsmGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 169 REDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPsrlprpapGQLLVSKF 248
Cdd:cd01369 155 HEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVET--------EKKKSGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 249 HFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSP 328
Cdd:cd01369 227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSP 304
|
330 340
....*....|....*....|.
gi 203096856 329 SSSDFDETLNTLNYASRAQNI 349
Cdd:cd01369 305 SSYNESETLSTLRFGQRAKTI 325
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
9.80e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 285.86 E-value: 9.80e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 55 FGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 135 DLLDCL-VHVSYLEVYKEEFRDLLEVGTASRDIqlREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 214 SSRSHTVFTVTLEQRGRAPSRLPRpapgqllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 203096856 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 |
1.20e-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: 277.85 E-value: 1.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLG-RDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 94 GQTGSGKTYTM-GEA-SVASLLEDEQGIVPRAMAEAFKLID-----ENDLLDCLVHVSYLEVYKEEFRDLLEvgTASRDI 166
Cdd:cd01373 82 GQTGSGKTYTMwGPSeSDNESPHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 167 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEqrgrapSRLPRPAPGQLLVS 246
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE------SWEKKACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340 350
....*....|....*....|....*....|.
gi 203096856 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 |
2.01e-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: 2.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKELLHGHQSCLQVE--------------PGLGRVTLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhppkgsaANKSERNGGQKETkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDlldclVHVSYLEVYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 160 GTASRD-----IQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSR 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 235 LPRPAPGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRG--SHIPYRDSKITRILKD 312
Cdd:cd01368 231 DVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSKLTHLFQN 310
|
330 340 350
....*....|....*....|....*....|....*
gi 203096856 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 |
5.29e-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: 5.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKEL---------LHGHQSCLQVEPGLgRVTLGR--DRH-FGFHVVLAEDAGQEAVYQACVQPLLEAF 82
Cdd:cd01367 1 KIKVCVRKRPLNKKEVakkeidvvsVPSKLTLIVHEPKL-KVDLTKyiENHtFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 83 FEGFNATVFAYGQTGSGKTYTMGEASvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGT 161
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 162 asrDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLeqrgrapsrlpRPAPG 241
Cdd:cd01367 158 ---RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 242 QLLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSSLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAK 319
Cdd:cd01367 224 NKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSK 300
|
330 340
....*....|....*....|....*.
gi 203096856 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 |
1.07e-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: 1.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLgRVTLGRDRHFG------FHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 89 TVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDENDLLDClVHVSYLEVYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlGS-------PEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 168 LREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGR-APSRLPRpapgqllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERlAPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 203096856 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 |
3.04e-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: 3.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 55 FGFHVVLaEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASlleDEQGIVPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 135 DLLDCLVHVSYLEVYKEEFRDLL----EVGTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHL 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 211 NHLSSRSHTVFTVTLEQRGRAPSRlprpapGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLSS------EKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 203096856 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
10-356 |
1.68e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 225.20 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 10 GAEEAPVRVALRVRPLLPKEllhghQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNAT 89
Cdd:PLN03188 94 GVSDSGVKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 90 VFAYGQTGSGKTYTM-GEASVAS---LLEDEQGIVPRAMAEAFKLIDENDL------LDCLVHVSYLEVYKEEFRDLLEv 159
Cdd:PLN03188 169 VFAYGQTGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 160 gTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEqrgrapSRLPRPA 239
Cdd:PLN03188 248 -PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVE------SRCKSVA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 240 PG--QLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLG 315
Cdd:PLN03188 321 DGlsSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLG 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 203096856 316 GNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 401 GNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-1198 |
1.14e-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: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 781
Cdd:COG1196 254 ELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 RLQEFRRRVAAAQSQVQVLKEK--------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLE 853
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEEleeaeaelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 854 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 933
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 934 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKsgQLRQGSAQSQQQIRGEIDSLRQE 1013
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA--ALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1014 KDSLLKQ----RLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAK 1087
Cdd:COG1196 562 AIEYLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1088 LSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1167
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
490 500 510
....*....|....*....|....*....|.
gi 203096856 1168 LQQSRDHLGEGLADSRRQYEARIQALEKELG 1198
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1062 |
1.51e-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: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 725 GELVRTG---------KAAQALNRQhsQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAGE--RSRLQEFRRRVA 791
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKEleELEEELEqlRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 792 AAQSQVQVLKEKKQaterlvslsaQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHE 871
Cdd:TIGR02168 730 ALRKDLARLEAEVE----------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 872 QQQKILKIKTEEI------AAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILA 944
Cdd:TIGR02168 800 ALREALDELRAELtllneeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 945 KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGsaqsQQQIRGEIDSLRQEKDSLLKQRLEI 1024
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR----LEGLEVRIDNLQERLSEEYSLTLEE 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 203096856 1025 DGKLRQGSLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1062
Cdd:TIGR02168 956 AEALENKIEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
744-1197 |
1.98e-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: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 744 RIRELEQEAEQVRAELSEGQRQLRELEgKELQDAgeRSRLQEFRRRVAAAQSQVqvlkEKKQATERLVslsaqsEKRLQE 823
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELE-AELAEL--EAELEELRLELEELELEL----EEAQAEEYEL------LAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 824 LERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLE 903
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 904 QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK 983
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 984 ELSEKSGQLRQ---------GSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ----------------GSLLSPEE 1038
Cdd:COG1196 454 LEEEEEALLELlaelleeaaLLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaalllaglrglagaVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1039 ERTLFQLDEAIEALDAAIEYKNE--AITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ 1116
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1117 QQIAFSE-----------LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRR 1184
Cdd:COG1196 614 RYYVLGDtllgrtlvaarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490
....*....|...
gi 203096856 1185 QYEARIQALEKEL 1197
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 203096856 67 QEAVYqACVQPLLEAFFEGFN-ATVFAYGQTGSGKTYTMgeasvaslledeQGIVPRAMAEAFklidendlldclvhvSY 145
Cdd:cd01363 32 QPHVF-AIADPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAF---------------NG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 146 LEVYKEEFRDLLEvgtasrdiqlredergnvvlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHLNHLSSRSHTVFTVtl 225
Cdd:cd01363 84 INKGETEGWVYLT------------------------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI-- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 203096856 226 eqrgrapsrlprpapgqllvskfhFVDLAGSERvlktgstgerlkesiqINSSLLALGNVISA 288
Cdd:cd01363 137 ------------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-1026 |
6.72e-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: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 705 QAQQKIRELAINIRMKEELIGE-------LVRTGKAAQALNRQHSQ-----------RIRELEQEAEQVRAELSEGQRQL 766
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNElerqlksLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 767 ----RELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQElernvqlmrqqQGQLQRRL 842
Cdd:TIGR02168 256 eeltAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------QLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 843 REETEQKR-RLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvslEQQQKIEEQKKWLDQEMEK 921
Cdd:TIGR02168 325 LEELESKLdELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----------ELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 922 VLQQRRALEELGEEL----HKREAILAKKEALMQEKTGLESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKSGQLRQGS 996
Cdd:TIGR02168 395 IASLNNEIERLEARLerleDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350
....*....|....*....|....*....|
gi 203096856 997 aQSQQQIRGEIDSLRQEKDSLLKQRLEIDG 1026
Cdd:TIGR02168 475 -QALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-1039 |
7.38e-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: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 704 AQAQQKIR-----------ELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAEQVRAELSEGQRQLREL 769
Cdd:TIGR02168 207 RQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 770 EGkelqdagersRLQEFRRRVAAAQSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 849
Cdd:TIGR02168 287 QK----------ELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 850 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNgsvvsleQQQKIEEQKKWLDQEMEKVLQQRRAL 929
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-------EIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 930 EELGEElHKREAILAKKEALMQEKTGLESKRLRSSQALNedivRVSSRLEHLEKELSEKSGQLRQGSAQ--SQQQIRGEI 1007
Cdd:TIGR02168 427 LKKLEE-AELKELQAELEELEEELEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
|
330 340 350
....*....|....*....|....*....|...
gi 203096856 1008 DSLRQEKDSLLKQRLEIDGKL-RQGSLLSPEEE 1039
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILgVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
702-1017 |
9.04e-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: 66.62 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE-------LEQEAEQVRAELSEGQRQLRELEGK-- 772
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTELEAEie 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 773 --ELQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATERLVSLSAQ---SEKRLQELERNVQLMRQQQGQLQRRLREET 846
Cdd:TIGR02168 765 elEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 847 EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKvlqqR 926
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL------LRSELEELSEELRELESKRSEL----R 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 927 RALEELGEELHKreAILAKKEALMQEKTGLEskRLRSSQALNEDIVrvssrlehlekelseksGQLRQGSAQSQQQIRGE 1006
Cdd:TIGR02168 915 RELEELREKLAQ--LELRLEGLEVRIDNLQE--RLSEEYSLTLEEA-----------------EALENKIEDDEEEARRR 973
|
330
....*....|.
gi 203096856 1007 IDSLRQEKDSL 1017
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
703-1030 |
1.72e-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: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 703 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalnrqhSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDagERSR 782
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEEKQ-NEIEK--LKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 783 LQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 862
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 863 VKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAI 942
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 943 LAKK-EALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKsgqlrqgsaqsQQqirgEIDSLRQEKDSLLK 1019
Cdd:TIGR04523 522 LKEKiEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEK-----------NK----EIEELKQTQKSLKK 582
|
330
....*....|.
gi 203096856 1020 QRLEIDGKLRQ 1030
Cdd:TIGR04523 583 KQEEKQELIDQ 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
740-1130 |
1.97e-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: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 740 QHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELqdagersrlqefrrrvaaaQSQVQVLKEKKQATERLVSlsaQSEK 819
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL-------------------KSELKNQEKKLEEIQNQIS---QNNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 820 RLQELERNVQLMRqqqgqlqrrlreetEQKRRLEAEMSKRQhrvKELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSv 899
Cdd:TIGR04523 336 IISQLNEQISQLK--------------KELTNSESENSEKQ---RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 900 vSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELhKREAILAKKE--ALMQEKTGLES-----KRLRSSQ-----A 966
Cdd:TIGR04523 395 -DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEikDLTNQDSVKELiiknlDNTRESLetqlkV 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 967 LNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQsQQQIRGEIDSLRQEKDSLL-------KQRLEIDGKLRQ--GSLLSPE 1037
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKekiekleSEKKEKESKISDleDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1038 EERTLFQLDEAIEALDAAIEYKNEAITcrqrvlrasaSLLSqcemnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQ 1117
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQK----------SLKK-------------KQEEKQELIDQKEKEKKDLIKEIEEK 608
|
410
....*....|...
gi 203096856 1118 QIAFSELEMQLEE 1130
Cdd:TIGR04523 609 EKKISSLEKELEK 621
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
795-1079 |
2.36e-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: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 795 SQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKR-RLEAEMSKRQHRVKELELKHEQQ 873
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELeELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 874 QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEK 953
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 954 tgLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSL 1033
Cdd:COG1196 360 --LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 203096856 1034 LSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1079
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
711-1057 |
1.76e-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: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 711 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFR 787
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKRELSSL----------QSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 788 RRVAAAQSQVQVLKEKkqaTERLvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 867
Cdd:TIGR02169 702 NRLDELSQELSDASRK---IGEI-------EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 868 LK-HEQQQKILKIK----------TEEIAAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 935
Cdd:TIGR02169 772 EDlHKLEEALNDLEarlshsripeIQAELSKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 936 LHKR-EAILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKSGQLRQ-----GSAQSQQQIRGEIDS 1009
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRElerkiEELEAQIEKKRKRLS 920
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 203096856 1010 LRQEKDSLLKQRL-EIDGKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:TIGR02169 921 ELKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
796-1079 |
1.92e-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: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 796 QVQVLKEKKQATERLVSLSAQSE--------KRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 867
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 868 LKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsleqqqKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKE 947
Cdd:TIGR02168 281 EEIEELQKELYALANEIS---------------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 948 ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIR-----------------GEIDSL 1010
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneierlearlerleDRRERL 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 203096856 1011 RQEKDSLLKQRLEIDGKLRQGSLlsPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1079
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
741-1014 |
1.95e-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: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 741 HSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERS-----RLQEFRRRV--------AAAQSQVQVLKEKKQAT 807
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLT-EEISELEKRLeeieqLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 808 ERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR-----------LEAEMSKRQHRVKELELKHEQQQKI 876
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteeyaeLKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 877 LKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEElhKREAILAKKEALMQEKTGL 956
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIKKQEWKLEQLAADL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 203096856 957 ESKRlrssqalnEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEK 1014
Cdd:TIGR02169 465 SKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-1198 |
2.97e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 700 EWRLAQAQQKIRELAINIRmkeELIGELvrtgkaaqalnrqhsQRIRELEQEAEQVRAELSEGQRQLRELEGKElqdAGE 779
Cdd:PRK03918 199 EKELEEVLREINEISSELP---ELREEL---------------EKLEKEVKELEELKEEIEELEKELESLEGSK---RKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 780 RSRLQEFRRRVAAAQSQVQVLKEK----------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 849
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKvkelkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 850 RRLEaEMSKR----QHRVKELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQ 924
Cdd:PRK03918 338 ERLE-ELKKKlkelEKRLEELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 925 QRRALEELGEELH---------KREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQL-RQ 994
Cdd:PRK03918 413 RIGELKKEIKELKkaieelkkaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 995 GSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAIT 1064
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1065 CRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALER 1144
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEE 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1145 QRLEMDR-QLTLQQKEHEQNMQLLLQQSRDHLG-----EGLADSRRQYEARIQALEKELG 1198
Cdd:PRK03918 645 LRKELEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1036 |
3.10e-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: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 791 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKH 870
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 871 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELHKREAILAKKEA 948
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 949 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKL 1028
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 203096856 1029 RQGSLLSP 1036
Cdd:COG4942 251 LKGKLPWP 258
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
705-1211 |
4.02e-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: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 705 QAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQ--------HSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQD 776
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 777 AGERSRLQEFRRRVAAAQSQVQvlkEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreETEQKRRLEAEM 856
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQH------------------IHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 857 SKRQHRVKELELKHEQQQKIlkikteeiaAFQRKRRSGSNGSVVSLEQQQKIE-EQKKWLDQEMEKVLQ----QRRALEE 931
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATI---------DTRTSAFRDLQGQLAHAKKQQELQqRYAELCAAAITCTAQceklEKIHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 932 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKEL-----SEKSGQLRQGSAQSQQQIRGE 1006
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1007 IDSLRQEKDSLLKQRLEIdgklrqgsllspEEERTLFQLDEAIEAldaaieykneaiTCRQRVlRASASLLSQcEMNLMA 1086
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASL------------KEQMQEIQQSFSILT------------QCDNRS-KEDIPNLQN-ITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1087 KLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLV----YWLEVALERQRlEMDRQLTLQQKEHEQ 1162
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTalhaLQLTLTQERVR-EHALSIRVLPKELLA 676
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 203096856 1163 NMQLLLQ--QSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKL 1211
Cdd:TIGR00618 677 SRQLALQkmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
698-1052 |
4.23e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 698 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR-QHSQRIRELEQEAEQVRAELSEGQRQLRELE-GKELQ 775
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEA---KKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkADEAK 1516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 776 DAGERSRLQEFRRRVAAAQS-QVQVLKEKKQATE--RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 852
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKAdEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 853 EAEMSKRQHRVKELELKHEQQQKIlkiKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVlqqRRALEEL 932
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKI---KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKI---KAAEEAK 1668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 933 GEELHKREAILAKKEALMQEKTGLESKRlrssqalNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQ 1012
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKK-------EAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAKKEA 1739
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 203096856 1013 EKDSLLKQRLEID-GKLRQGSLLSPEEERTLFQLDEAIEAL 1052
Cdd:PTZ00121 1740 EEDKKKAEEAKKDeEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
744-1019 |
7.19e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 744 RIRELEQEAEQVRAELSEGQRQLRELEG------KELQDAGE-RSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQ 816
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREelekleKEVKELEElKEEIEELEKELESLEGSKRKLEEKIRELEERI---EE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 817 SEKRLQELERNVqlmrqqqgQLQRRLREETEQKRRLEAEMSKRQHRVKELElkheqqqKILKIKTEEIAAFQRKrrsgsn 896
Cdd:PRK03918 271 LKKEIEELEEKV--------KELKELKEKAEEYIKLSEFYEEYLDELREIE-------KRLSRLEEEINGIEER------ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 897 gsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRlrssqaLNEDIVRVSS 976
Cdd:PRK03918 330 -----IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK------LEKELEELEK 398
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 203096856 977 RLEHLEKELSEksgqlrqgsaqsqqqIRGEIDSLRQEKDSLLK 1019
Cdd:PRK03918 399 AKEEIEEEISK---------------ITARIGELKKEIKELKK 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
643-1196 |
2.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 643 RISNCSQRAGARPGSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPA-TASEWRLAQAQQKIREL--AINIRM 719
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAArkAEEVRK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 720 KEEL-IGELVRTGKAA-QALNRQHSQRIRELEQE--------AEQVRAELSEGQRQLRELEGKELQDAgERSRLQEFRRR 789
Cdd:PTZ00121 1190 AEELrKAEDARKAEAArKAEEERKAEEARKAEDAkkaeavkkAEEAKKDAEEAKKAEEERNNEEIRKF-EEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 790 VAAAQSQ-------VQVLKEKKQATERLVS----------LSAQSEKRLQELERNVQLMRQQQGQLQRRLREET------ 846
Cdd:PTZ00121 1269 QAAIKAEearkadeLKKAEEKKKADEAKKAeekkkadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaeaa 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 847 ---EQKRRLEAEMSKRQHRVKELELKHEQQQ-KILKIKTEEIAAFQRKRRSGSNGSVVSlEQQQKIEEQKKWLDQEMEKV 922
Cdd:PTZ00121 1349 kaeAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKA 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 923 LQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGS--AQSQ 1000
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1001 QQIRGEIDSLRQEKDSLLKQRL-EIDGKLRQGSLLSPEEERTLFQLDEAIEALDA----AIEYKNEAITCRQRVLRaSAS 1075
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALR-KAE 1584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1076 LLSQCEMNLMAKLSYLSSSETRAllckyfdKVVTLREEQhQQQIAFSELEMQLEEQQRLvywleVALERQRLEMDRQLTL 1155
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKM-------KAEEAKKAE-EAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEE 1651
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 203096856 1156 QQKEHEQNMQLLLQQSRdhlgEGLADSRRQYEARIQALEKE 1196
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAK----KAEEDKKKAEEAKKAEEDEK 1688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-1197 |
3.64e-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: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 700 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDA 777
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 778 --GERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLE 853
Cdd:TIGR02168 381 leTLRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 854 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 919
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 920 EKVL-------------QQRRALEELGEELHKREAILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 979
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 980 ----------------HLEKELSE-------------KSGQLRQGSAQSQQQI---RGEIDSLRQEK------------- 1014
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPgyrivtldgdlvrPGGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1015 -DSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1093
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1094 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRD 1173
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 203096856 1174 --HLGEGLADSRRQYEARIQALEKEL 1197
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
744-1210 |
4.92e-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: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 744 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQE----FRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEK 819
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 820 RLQELERNVQlmrqqqgqlqrrlrEETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIaafqrkrrSGSNGSV 899
Cdd:TIGR04523 226 QNNQLKDNIE--------------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--------EQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 900 VSLEQQ-QKIEEQKKWLDQEMEKVLqqrraLEELGEELHKREailakkealmQEKTGLESKRLRSSQA---LNEDIVRVS 975
Cdd:TIGR04523 284 KELEKQlNQLKSEISDLNNQKEQDW-----NKELKSELKNQE----------KKLEEIQNQISQNNKIisqLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 976 SRLEHLEKELSEKSGQLRQgsAQSQ-QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQgsllspeEERTLFQLDEAIEALda 1054
Cdd:TIGR04523 349 KELTNSESENSEKQRELEE--KQNEiEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKL-- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1055 aiEYKNEAITCRQRVLRASASLLSQCEMNLmaklsylssSETRALLCKYFDKVVTLREEQhQQQIafSELEMQLEEQQRL 1134
Cdd:TIGR04523 418 --QQEKELLEKEIERLKETIIKNNSEIKDL---------TNQDSVKELIIKNLDNTRESL-ETQL--KVLSRSINKIKQN 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 1135 VYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSrdhlgegladsrRQYEARIQALEKELGRymwINQELKQK 1210
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 ... |
798-1099 |
4.94e-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: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 798 QVLKEKKQATERLVSLSAQSEKRL----------QELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 867
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLELeeeyllyldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 868 LKHEQ-QQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELH-KREAILAK 945
Cdd:pfam02463 278 EKEKKlQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 946 KEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgSAQSQQQIRGEIDSLRQEKDSLLKQRLEID 1025
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--EAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 203096856 1026 GKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRqrvLRASASLLSQCEMNLMAKLSYLSSSETRAL 1099
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
692-889 |
5.86e-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: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 692 QVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEg 771
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 772 KELQDagersRLQEFRRRVAAAQSQVQVLKEK------------------KQATERLVSLSAQSEKRLQELERNVQLMRQ 833
Cdd:COG4942 97 AELEA-----QKEELAELLRALYRLGRQPPLAlllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 834 QQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 889
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
922-1197 |
7.41e-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: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 922 VLQQRRALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQ 1001
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1002 ------QIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1075
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1076 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1155
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 203096856 1156 QQKEHEQNMQlLLQQSRDHLGEGLADSRRQY---EARIQALEKEL 1197
Cdd:TIGR02168 902 ELRELESKRS-ELRRELEELREKLAQLELRLeglEVRIDNLQERL 945
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
1.00e-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: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 16 VRVALRVRPLLPKELlhghqsclQVEPGLGRVTLGRDRH----FGFHVVLAEDAGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 203096856 92 AYGQTGSGKTYTMgeasvaslledeqgiVPRAMAEAFKLIDENDLLDCL-VHVSYLEVYKEEFRDLL 157
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
698-1029 |
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 203096856 698 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR--QHSQRIRELEQEAEQVRAELSEGQRQLRELEgkELQ 775
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 776 DAGERSRLQEFRR--RVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERnvqlMRQQQGQLQRRLREETEQKRRLE 853
Cdd:PTZ00121 1541 KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEEEKKMKAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 854 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAleelG 933
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKK----A 1690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 934 EELHKREAILAKKEALMQEKTGLESKR---LRSSQALNEDIVRVSSRLEHLEKELSE----------KSGQLRQGSAQSQ 1000
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkKIAHLKKEEEKKA 1770
|
330 340 350
....*....|....*....|....*....|.
gi 203096856 1001 QQIRGEIDSLRQE--KDSLLKQRLEIDGKLR 1029
Cdd:PTZ00121 1771 EEIRKEKEAVIEEelDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-948 |
1.27e-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: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 703 LAQAQQKIRELAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 781
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 RLQEFRRRVAAAQSQVQVLKEkkQATERLVSLSAQSEK---RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSK 858
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 859 RQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsNGSVVSlEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK 938
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIK-KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
250
....*....|
gi 203096856 939 REAILAKKEA 948
Cdd:TIGR02169 488 LQRELAEAEA 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
702-990 |
1.83e-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: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAGE 779
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 780 RSRLQEFRRRVAAAQSQVQ----VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 855
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 856 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 934
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 935 ELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG 990
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
669-1048 |
2.36e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 669 EELDAAIPGSRAVGGSKARVQARQVPPATASEWRLAQAQQKIREL---AINIRMKEELIGELVRTGKAAQALNRQHSQRI 745
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 746 R--ELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLK---EKKQATERLVSLSAQSEKR 820
Cdd:PTZ00121 1419 KadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 821 LQELERNVQLMRQQQGQLQRRLREETEQKRRLEA-----EMSKRQHRVKELELKHEQQQKilkiKTEEIAAFQRKRRSGS 895
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEakkadEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAEE 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 896 --NGSVVSLEQQQKIEEQ------KKWLDQEMEKVLQQRRALEEL--GEELHKREAILAKKEALMQEKTGLESKRLRSSQ 965
Cdd:PTZ00121 1575 dkNMALRKAEEAKKAEEArieevmKLYEEEKKMKAEEAKKAEEAKikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 966 ALNEDIVRVS--SRLEHLEKELSEKSGQLRQGSAQSQQQIRGEidslRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLF 1043
Cdd:PTZ00121 1655 AEEENKIKAAeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
....*
gi 203096856 1044 QLDEA 1048
Cdd:PTZ00121 1731 KAEEA 1735
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
685-951 |
2.39e-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: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 685 KARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAEQVRA--ELS 760
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 761 EGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQR 840
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 841 RLREETEQKRRlEAEMSKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQ 911
Cdd:pfam17380 465 LRQQEEERKRK-KLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEE 540
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 203096856 912 KKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQ 951
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
500-1030 |
2.55e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 500 EEENRDFLAALEDAMEQYKLQSDRLREQQEEMV----ELRLRLELVRPGWGGPRLLNGLPPGSFVPRPHTAPLGGAHAHV 575
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkesKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 576 LGMVPPACLPGDEVGSEQRGEQVTNGREAGAELLTEVNRLGSGSSAASEEEEEEEEPPRRTLHLRRNRISNCSQRAGARP 655
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 656 GSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVppaTASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQ 735
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV---KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 736 ALNRQHSQRIRELEQE----AEQVRAELSEGQRQLRELEGK---ELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATE 808
Cdd:pfam02463 704 KEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKideEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 809 RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQ 888
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 889 RKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSS 964
Cdd:pfam02463 864 TKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 203096856 965 QALNED---------IVRVSSRLEHLEKELSEKSGQLRQGSA--QSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ 1030
Cdd:pfam02463 944 EADEKEkeennkeeeEERNKRLLLAKEELGKVNLMAIEEFEEkeERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
703-1173 |
2.86e-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: 55.12 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 703 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAEQVRAELSEGQR----QLRELEGK------ 772
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQlvlans 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 773 ELQDAgeRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRL---------------QEL-ERNVQLMRQQQG 836
Cdd:pfam15921 357 ELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrRELdDRNMEVQRLEAL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 837 QLQRRLREETEQKRRLEAEMSKRQ--HRVKELELKHEQQQKILKIKTEEIAA----FQRKRRSGSNGSVVSLEQQQKIEE 910
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 911 QKKWLDQEMEKV---LQQRRALEELGEELHKREAILAKKEALMQEK--------------TGLESKRLRSSQALNEDIVR 973
Cdd:pfam15921 515 TNAEITKLRSRVdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMQVEKAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 974 VSSRLEHLEKELSE-------KSGQLRQGSAQ--------------SQQQIRGeIDSLRQEKDSLLKQ----RLEIDGKL 1028
Cdd:pfam15921 595 LEKEINDRRLELQEfkilkdkKDAKIRELEARvsdlelekvklvnaGSERLRA-VKDIKQERDQLLNEvktsRNELNSLS 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1029 RQGSLL-------SPEEERTLFQLDEAIEALDAAIEYKNEAITCRQ----RVLRASASLLSQCEMN------LMAKLSYL 1091
Cdd:pfam15921 674 EDYEVLkrnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQITAKrgqidaLQSKIQFL 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1092 SSSETRALLCKYFdkvvtLREEQHQQQIAFS-----------ELEMQLEEQQRL---VYWLEVALERQRLEMDRQLTLQQ 1157
Cdd:pfam15921 754 EEAMTNANKEKHF-----LKEEKNKLSQELStvateknkmagELEVLRSQERRLkekVANMEVALDKASLQFAECQDIIQ 828
|
570
....*....|....*.
gi 203096856 1158 KEHEQNMQLLLQQSRD 1173
Cdd:pfam15921 829 RQEQESVRLKLQHTLD 844
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
685-1228 |
3.73e-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: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 685 KARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQA-----------LNRQHSQRIReLEQEAE 753
Cdd:TIGR00618 284 ERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqqssieeqrrlLQTLHSQEIH-IRDAHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 754 Q---VRAELSEG----------QRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKR 820
Cdd:TIGR00618 363 VatsIREISCQQhtltqhihtlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 821 LQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE---MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNG 897
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 898 SVVSLEQQQKIEEQKKWLDQEMEKVLQQrraleelGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 977
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 978 LEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQEKDSLLKQrleIDGKLRQGSLLSPEEERTLFQLDEAIEALdAAIE 1057
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLAC--EQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREHAL-SIRV 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1058 YKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQLEEQQRL 1134
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSDLAAREDA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1135 VYWLEVALERQRLEMDRQLTL--QQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRymwINQELKQKLG 1212
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKARTEahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE---IGQEIPSDED 817
|
570
....*....|....*.
gi 203096856 1213 GVNAVGHSRGGEKRSL 1228
Cdd:TIGR00618 818 ILNLQCETLVQEEEQF 833
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
722-1061 |
3.91e-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: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 722 ELIGELVRTGKAAQALN-RQHSQRIRELEQEaeQVRAELSEgqrQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVL 800
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSeRQQQEKFEKMEQE--RLRQEKEE---KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 801 KEKKQATERLvslsaQSEKRLQELERnvqlmrqQQGQLQRRLREETEQKRRLEAEMSKRQHRVK-ELE-------LKHEQ 872
Cdd:pfam17380 344 MERERELERI-----RQEERKRELER-------IRQEEIAMEISRMRELERLQMERQQKNERVRqELEaarkvkiLEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 873 QQKI--LKIKTEEIAAFQRKRRSgsngsvvslEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAILAKKEALM 950
Cdd:pfam17380 412 QRKIqqQKVEMEQIRAEQEEARQ---------REVRRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 951 Q-----EKTGLESKRLRSSQALNED---IVRVSSRLEHLEKELSEksgqlRQGSAQSQQQIRGEIDSLRQEKDslLKQRL 1022
Cdd:pfam17380 480 EkekrdRKRAEEQRRKILEKELEERkqaMIEEERKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQE--MEERR 552
|
330 340 350
....*....|....*....|....*....|....*....
gi 203096856 1023 EIDGKLRQGSllspEEERTLFQLDEAIEALDAAIEYKNE 1061
Cdd:pfam17380 553 RIQEQMRKAT----EERSRLEAMEREREMMRQIVESEKA 587
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
739-1199 |
7.82e-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: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 739 RQHSQRIRELEQEAEQVRAELSEGQRQLRElEGKELQDAgERSRLQEFRRRVAAAQSQVQVLKEKKQATERlvslsAQSE 818
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDD-QWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-----ADIE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 819 KRLQELERNVQLMRQQQGQLQRRLREETEQkRRLEAEMSKRQHRVKE-----LELKHEQQQKI----LKIKTEEIAAFQR 889
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEqnnrdIAGIKDKLAKIrearDRQLAVAEDDLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 890 KR---RSGSNGSVVSLEQQQK-----IEEQKKWLDQ---EMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLES 958
Cdd:pfam12128 420 LEselREQLEAGKLEFNEEEYrlksrLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 959 KRLRSSQALNEDIVRVS---SRLEHLEKELSEKSGQLRqgsAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSlls 1035
Cdd:pfam12128 500 RRDQASEALRQASRRLEerqSALDELELQLFPQAGTLL---HFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGS--- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1036 PEEERTLFQLDEAIEALDAAiEYKNEAITCRQRVLRASASLLSQCEMN---------LMAKLSYLSSSETRALlCKYFDK 1106
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVP-EWAASEEELRERLDKAEEALQSAREKQaaaeeqlvqANGELEKASREETFAR-TALKNA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1107 VVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQR--LEMDRQLTLQQ-----KEHEQNMQLLLQQ-------SR 1172
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqLDKKHQAWLEEqkeqkREARTEKQAYWQVvegaldaQL 731
|
490 500
....*....|....*....|....*..
gi 203096856 1173 DHLGEGLADSRRQYEARIQALEKELGR 1199
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKR 758
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
702-1191 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAEQVR--AELSEGQRQ--LRELEGKELQDA 777
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKtnGLLHTEDREeeIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 778 GERSRLQEFRRRVAAAQSQVQVLKEK-----------KQATERLV-SLSAQsEKRLQELERNVQLMRQQQGQLQRRLREE 845
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKletltnqnsdcKQHIEVLKeSLTAK-EQRAAILQTEVDALRLRLEEKESFLNKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 846 TEQKRRLEAEMSKRQHRVKELelkheqqQKILKIKTEEIAAFQRKrrsgsngsVVSLEQQQKieEQKKWLDQEMEKV--L 923
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDL-------KDMLDVKERKINVLQKK--------IENLQEQLR--DKDKQLAGLKERVksL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 924 QQRR-----ALEELGEELHKREAILakkEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLR--QGS 996
Cdd:pfam10174 428 QTDSsntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEH 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 997 AQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLrQGSLL----SPEEERTLFQLDEAIEALDAAIE-YKNEAITCRQRVLR 1071
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKL-ENQLKkahnAEEAVRTNPEINDRIRLLEQEVArYKEESGKAQAEVER 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1072 ASAsLLSQCEMNLMAKLSYLSSSETRALLcKYFDKVVTLREEQHQQQIAFSELEMQLEE------------QQRLVYWLE 1139
Cdd:pfam10174 584 LLG-ILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEarrrednladnsQQLQLEELM 661
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 203096856 1140 VALERQRLEMDrqltlQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQ 1191
Cdd:pfam10174 662 GALEKTRQELD-----ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILE 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
737-1201 |
1.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 737 LNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLsaq 816
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 817 sEKRLQELERNVQLMRQQqgqlqrrlreETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQrkrrsgsn 896
Cdd:COG4717 145 -PERLEELEERLEELREL----------EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ-------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 897 gsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGL----ESKRLRSSQALNEDIV 972
Cdd:COG4717 206 ------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 973 RVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKlrqgslLSPEEERTLFQLDEAIEAL 1052
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPD------LSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1053 DAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEmqLEEQQ 1132
Cdd:COG4717 353 LREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEELEELEEQLEELL--GELEE 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 1133 RLVYWLEVALERQRLEMDRQLTLQQKEHEQNM-------QLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYM 1201
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
696-1197 |
1.30e-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: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 696 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAEQVRAELSEGQRQL------ 766
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknelse 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 767 --RELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLrE 844
Cdd:pfam05557 116 lrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK-S 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 845 ETEQKRRLEAEMSKRQHRVKELelkHEQQQKILKIKtEEIAAFQRK--RRSGSNGSVVSLE-----QQQKIEEQKKwLDQ 917
Cdd:pfam05557 195 ELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRKleREEKYREEAATLElekekLEQELQSWVK-LAQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 918 EMEKVLQQRRALEELGEELHKREAilakkeALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKSGQLRQ 994
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREI------VLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 995 gsaqSQQQIRgeidSLRQEKDsLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASA 1074
Cdd:pfam05557 344 ----LQRRVL----LLTKERD-GYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1075 SLLSQCEMNLMAKLSYLSSSETRALLckyfDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLT 1154
Cdd:pfam05557 415 QQAQTLERELQALRQQESLADPSYSK----EEVDSLRRK-------LETLELERQRLREQKNELEMELERRCLQGDYDPK 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 203096856 1155 LQQK-EHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKEL 1197
Cdd:pfam05557 484 KTKVlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
743-1211 |
4.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 743 QRIRELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFRRRVAAAQSQVQVLKEKKQATERLvslsaqsEKRLQ 822
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEI----------SSELPELREELEKLEKEVKELEELKEEIEEL-------EKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 823 ELERNvqlmrqqqgqlqrrlreeteqKRRLEAEMSKRQHRVKELELKHEQQQKILKiKTEEIAAFQRKRRSGSngsvvsl 902
Cdd:PRK03918 249 SLEGS---------------------KRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLS------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 903 EQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREailAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEH 980
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 981 LEKELSEKsgqlrqgsaqSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKN 1060
Cdd:PRK03918 377 LKKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1061 EAITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEV 1140
Cdd:PRK03918 437 KCPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKEL 501
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 203096856 1141 ALERQRLEmdrqltlqQKEHEQNMQLLLQQSRDHlgEGLADSRRQYEARIQALEKELGRYmwinQELKQKL 1211
Cdd:PRK03918 502 AEQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKL----EELKKKL 558
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
716-1043 |
5.05e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 716 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFRRRVAAAQS 795
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 796 QVQVLKEKKQATerlvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVkeLELKHEQQ-- 873
Cdd:COG1340 72 KVKELKEERDEL----------NEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV--LSPEEEKElv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 874 QKILKIKTEeiaafqrkrrsgsngsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK-REAILAKKEALMQE 952
Cdd:COG1340 140 EKIKELEKE-------------------LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIEL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 953 KTGLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRL-EIDGKLRQG 1031
Cdd:COG1340 201 YKEADELR-KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAeEIFEKLKKG 279
|
330
....*....|..
gi 203096856 1032 SLLSPEEERTLF 1043
Cdd:COG1340 280 EKLTTEELKLLQ 291
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1218 |
5.82e-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: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 844 EETEQK--------RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSLEQqqKIEEQKKWL 915
Cdd:TIGR02168 175 KETERKlertrenlDRLEDILNELERQLKSLERQAEKAERYKELKAEL----RELELALLVLRLEELRE--ELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 916 DQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKSGQLRQ 994
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISrLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 995 GSAQSQQQIRgEIDSLRQEKDSLLKQRLEIDGKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNeaitcrqrvlrasa 1074
Cdd:TIGR02168 328 LESKLDELAE-ELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLR-------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1075 sllsqcemnlmaklsylsssetrallckyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywlevalERQRLEmDRQLT 1154
Cdd:TIGR02168 386 ------------------------------SKVAQLELQIASLNNEIERLEARLERLED---------RRERLQ-QEIEE 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 203096856 1155 LQQKEHEQNMQLLlQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKLGGVNAVG 1218
Cdd:TIGR02168 426 LLKKLEEAELKEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
711-1148 |
5.96e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 711 RELAINIRMKEELIGELvRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERSRLQEFRRRV 790
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 791 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLEAEMSKRQHRVKELELK 869
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 870 HEQQQKILKIKTEEIAAFQRKRR-------SGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQ---------QRRALEELG 933
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERlkearllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfllLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 934 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIR--------- 1004
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1005 GEIDSLR------QEKDSLLKQRLEIDGKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAIT-CRQRVLRASAs 1075
Cdd:COG4717 382 EDEEELRaaleqaEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEeLREELAELEA- 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 1076 llsqcemnlmaKLSYLSSSETrallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVY---WLEVALERQRLE 1148
Cdd:COG4717 461 -----------ELEQLEEDGE-------------LAELLQELEELKAELRELAEEWAALKLaleLLEEAREEYREE 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
720-1062 |
1.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 720 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAelSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQsqvqv 799
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----- 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 800 lkeKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAemskrQHRVKELELKHEQQQKILKI 879
Cdd:PTZ00121 1177 ---KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 880 KT-EEIAAFQRKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELHKREAILAKKEAlMQEKTGLES 958
Cdd:PTZ00121 1249 RNnEEIRKFEEARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 959 KRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQiRGEIDSLRQE----KDSLLKQRLEIDGKLRQGSLL 1034
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKK 1399
|
330 340
....*....|....*....|....*...
gi 203096856 1035 SPEEERTLFQLDEAIEALDAAIEYKNEA 1062
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
700-1161 |
1.21e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 700 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGE 779
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 780 RSRLQEFRRRVAAAQSQvQVLKEKKQATERLVSLSA---QSEKRLQELERNVQL-------MRQQQGQLQRRLREETEQK 849
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLE-ELREERDELREREAELEAtlrTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 850 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsVVSLEQQQKIEEQKkwLDQEMEKVLQQRRAL 929
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDR----------------IERLEERREDLEEL--IAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 930 EELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK--ELSEKSGQLRQ--GSAQSQQQIRG 1005
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDeiERLREKREALA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1006 EIDSLRQEKDSLLKQRL-EIDGKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCE--- 1081
Cdd:PRK02224 620 ELNDERRERLAEKRERKrELEAEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelr 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1082 ---MNLMAKLSYLSS--SETRALLCKYFDkvvtLREEQHQQQIafSELEMQLEEQQRLVYWLEvALERQRLEMDRQLTLQ 1156
Cdd:PRK02224 698 errEALENRVEALEAlyDEAEELESMYGD----LRAELRQRNV--ETLERMLNETFDLVYQND-AYSHIELDGEYELTVY 770
|
....*
gi 203096856 1157 QKEHE 1161
Cdd:PRK02224 771 QKDGE 775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
696-1079 |
1.38e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 696 ATASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQ 775
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 776 DAGERSRLQEFRRRVAAAQSQVQVLKEK---------KQATERLVSLS---AQSEKRLQELERNVQLMRQQQGQLQRRLR 843
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlslateeelQDLAEELEELQqrlAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 844 EETEQKRRLEAEMSKR--------------------------------------QHRVKELELKHEQQQKILKIKTEEIA 885
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 886 AFQRKRRSGSNGsvvsLEQQQKIEEQKKWLDQeMEKVLQQRRALEELGEELhKREAILAKKEALMQEKTGLESKRLRSSQ 965
Cdd:COG4717 318 EEELEELLAALG----LPPDLSPEELLELLDR-IEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 966 ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQ--------QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQgsllsPE 1037
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREELAELEAELEQ-----LE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 203096856 1038 EERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1079
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
660-939 |
1.63e-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: 49.67 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 660 ERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNR 739
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 740 QHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERS-----RLQEFRRRVAAAQSQVQVL----KEKKQATERL 810
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNERasleeALALLRSELEELSEELRELeskrSELRRELEEL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 811 VSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK-RRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFqr 889
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLE--------------NKIKEL-- 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 203096856 890 krrsgsnGSV--VSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKR 939
Cdd:TIGR02168 985 -------GPVnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
693-1024 |
1.87e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 693 VPPATASEWRLAQAQQKIRELainIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEG- 771
Cdd:pfam07888 26 VPRAELLQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 772 -KELQDAGERsrlqefrrrvaaaqsqvqvLKEKKQAterLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKR 850
Cdd:pfam07888 103 yKELSASSEE-------------------LSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 851 RLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 930
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 931 ELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKSGQLRQGSAQSQQQIRGEID 1008
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQ 311
|
330
....*....|....*.
gi 203096856 1009 SLRQEKDSLLKQRLEI 1024
Cdd:pfam07888 312 SAEADKDRIEKLSAEL 327
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
696-1064 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 696 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAEQVRAELSEG-QRQLREL 769
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlTRRMQRG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 770 E--GKELQDAGE--RSRLQEFRRRVAAAQSQVQVLKEKKQA-TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLRE 844
Cdd:TIGR00618 534 EqtYAQLETSEEdvYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 845 ETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQKIEEQK 912
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQSEKEQLT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 913 KWLD----------QEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQALNEDIVRVSSR---- 977
Cdd:TIGR00618 694 YWKEmlaqcqtllrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKeLMHQARTVLKARTEAHFNNNEEvtaa 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 978 ------LEHLE-------KELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQ 1044
Cdd:TIGR00618 774 lqtgaeLSHLAaeiqffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
410 420
....*....|....*....|
gi 203096856 1045 LDEAIEALDAAIEYKNEAIT 1064
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQ 873
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
739-1021 |
2.39e-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: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 739 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERSRLQEFRRRVAAAQSQVQVLKEkkqaterlvslsaqSE 818
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAEAEQELEESKRE--------------TE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 819 KRLQELERNVQLMRQQQGQLQRRLREETEQ------KRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 892
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 893 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK--REAILAKKEALMQEKTGLESKRLRSSQALNED 970
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKvmREADEESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 203096856 971 IVRVSSRL----EHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQR 1021
Cdd:COG5185 487 LTQIESRVstlkATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
739-1197 |
2.44e-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: 48.89 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 739 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAG---ERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSA 815
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 816 --------------QSEKRLQELERNVQLMRQQQgqlqrrlreETEQKRrLEAEMSKRQHRVKELELKHEQQQKILKIKT 881
Cdd:TIGR00606 674 denqsccpvcqrvfQTEAELQEFISDLQSKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 882 EEIAAFQRKRRSGSNGSVvslEQQQKIEEQKKWL-----DQEMEKVLQQR-RALEELGEELHKREAILAKKEALMQEKTG 955
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 956 leskrLRSSQALNEdivRVSSRLEHLEKELSEksGQLRQGSAQSQQQirgEIDSLRQEKDSLLKQRLEIDGKLRQGSLLS 1035
Cdd:TIGR00606 821 -----DRTVQQVNQ---EKQEKQHELDTVVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1036 PEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTL 1110
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDG 967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1111 REEQ-HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQ----------LTLQQKEHEqnMQLLLQQSRDHLGEGL 1179
Cdd:TIGR00606 968 KDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQkiqerwlqdnLTLRKRENE--LKEVEEELKQHLKEMG 1045
|
490
....*....|....*...
gi 203096856 1180 ADSRRQYEARIQALEKEL 1197
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENI 1063
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
727-859 |
3.61e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 727 LVRTGKAAQALNRQHSQ----------RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQ 796
Cdd:PRK09510 54 MVDPGAVVEQYNRQQQQqksakraeeqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 203096856 797 VQvlKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 859
Cdd:PRK09510 134 AE--EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1197 |
4.20e-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: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 849 KRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQRR 927
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrELSSLQSELRRIENRLDELSQELSDA-----------SRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 928 ALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEksgqlrqgsaQSQQQIRGEI 1007
Cdd:TIGR02169 738 RLEELEEDL---SSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDLEARLSH----------SRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1008 DSLRQEKDSLLKQRLEIDGKLRQgslLSPEEErtlfQLDEAIEALDAAIEYKNEAITCRQRVLRasasllsqcemNLMAK 1087
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNR---LTLEKE----YLEKEIQELQEQRIDLKEQIKSIEKEIE-----------NLNGK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1088 LsylssSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1167
Cdd:TIGR02169 863 K-----EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
330 340 350
....*....|....*....|....*....|
gi 203096856 1168 LQQSRDHLGEGLADSRRQYEARIQALEKEL 1197
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
740-1021 |
5.74e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 740 QHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSR---LQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSA 815
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 816 QSE----------KRLQELERNVQLMRQQQGQLQRrlreetEQKRRLEAEMSKrqhrvkeLELKHEQQQKILKIKTEEIA 885
Cdd:PRK11281 157 QPEraqaalyansQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 886 AFQrKRRSGSNgsvvslEQQQKIEEQKkwldQEMEKVLQQRRAleELGEElHKREAILAKKEALMQEKTgLESKRLRSSQ 965
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQL----QLLQEAINSKRL--TLSEK-TVQEAQSQDEAARIQANP-LVAQELEINL 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 203096856 966 ALNEDIVRVSSRLehleKELSEKSGQLRQ---GSAQSQQQIRGEIDSLrqeKDSLLKQR 1021
Cdd:PRK11281 289 QLSQRLLKATEKL----NTLTQQNLRVKNwldRLTQSERNIKEQISVL---KGSLLLSR 340
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
702-828 |
8.29e-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: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALnrqhsQRIRELEQEAEQVRAELSEG-------QRQLRELEgKEL 774
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR-----AQLAELEAELAELSARYTPNhpdvialRAQIAALR-AQL 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 203096856 775 QDAGERSrLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 828
Cdd:COG3206 308 QQEAQRI-LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
844-1062 |
9.12e-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: 46.30 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 844 EETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEkvl 923
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 924 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALN-------EDIVRVSSRLEHLEKELSEKSGQLRQGS 996
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 997 AQSQQQiRGEIDSLRQEKDSLLKQrLEIDGKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEA 1062
Cdd:COG4942 181 AELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
963-1197 |
1.13e-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: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 963 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRqgsllspEEERTL 1042
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1043 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1121
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 203096856 1122 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNMQLLLQQSRDHLGE--GLADSRRQYEARIQALEKEL 1197
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
917-1057 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 917 QEMEKVLQQRRALE---ELGEELHKREAILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 981
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 982 EKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-987 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQAL---------NRQHSQRIRELEQEaeqvRAELSEGQRQLRELEgK 772
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAE----LERLDASSDDLAALE-E 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 773 ELQDAgeRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 852
Cdd:COG4913 693 QLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 853 EAEMSKRQHRVKelELKHEQQQKILKIkteeIAAFQRKRRSGSNGSVVSLEqqqkieeqkkwldqEMEKVLQQRRALEEL 932
Cdd:COG4913 768 RENLEERIDALR--ARLNRAEEELERA----MRAFNREWPAETADLDADLE--------------SLPEYLALLDRLEED 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 203096856 933 GEELHKREAILAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 987
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
743-931 |
1.40e-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: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 743 QRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAgeRSRLQEFRRRVAAAQSQVQVLKEK-KQATERLvsLSAQSEKRL 821
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALE-ARLEAA--KTELEDLEKEIKRLELEIEEVEARiKKYEEQL--GNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 822 QELERnvqlmrqqqgqlqrrlrEETEQKRRLeaemSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 901
Cdd:COG1579 92 EALQK-----------------EIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|
gi 203096856 902 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE 931
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
782-1030 |
1.53e-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: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslsAQSEKRLQELERnvQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 861
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERY----AAARERLAELEY--LRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 862 RVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHkrea 941
Cdd:COG4913 310 ELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLEALLAALG---- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 942 ilakkEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQGsaqsqqqiRGEIDSLRQEKDSLLKQR 1021
Cdd:COG4913 373 -----LPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDL--------RRELRELEAEIASLERRK 435
|
....*....
gi 203096856 1022 LEIDGKLRQ 1030
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 ... |
744-1195 |
1.73e-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: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 744 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQ-----------EFRRRVAAAQSQVQVL-KEKKQATERLV 811
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 812 SLSAQ------SEKRLQELeRNVQLMRQQQGQLQRRLREETEQ-----KRRLEAEMSKRQHRVKELELKHEQQQKILKIK 880
Cdd:pfam01576 163 EFTSNlaeeeeKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 881 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE----ELGEELH------------------- 937
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEkqrrDLGEELEalkteledtldttaaqqel 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 938 --KREAILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKSgqlRQGSAQSQQQIRGEID 1008
Cdd:pfam01576 322 rsKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1009 SLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKL 1088
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1089 SYLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNMQLL- 1167
Cdd:pfam01576 475 ELL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLe 541
|
490 500
....*....|....*....|....*....
gi 203096856 1168 -LQQSRDHLGEGLADSRRQYEARIQALEK 1195
Cdd:pfam01576 542 aLEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
720-1024 |
1.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 720 KEELIGELVRTGKAAQALNRQHS---QRIRELEQEAEQVRAELSEgqrqLRELEGK------ELQDAGERSRLQEFRRRV 790
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEE----LKKAKGKcpvcgrELTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 791 AAAQSQVQVLKEK-KQATERLVS----LSAQSE--------KRLQELERNVQLMRQQQGQLQRRLREETEQK-RRLEAEM 856
Cdd:PRK03918 462 KRIEKELKEIEEKeRKLRKELRElekvLKKESEliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEI 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 857 S---KRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQ-QKIEE-QKKWL---DQEMEKVLQQRRa 928
Cdd:PRK03918 542 KslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPfYNEYLelkDAEKELEREEKE- 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 929 LEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQalnEDIVRVSSRLEHLEKELSEKSGQLrQGSAQSQQQIRGEI 1007
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKeLEELEKKYSE---EEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTL 696
|
330
....*....|....*..
gi 203096856 1008 DSLRQEKDSLLKQRLEI 1024
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 ... |
749-1161 |
2.33e-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: 45.94 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 749 EQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEfrrrvaAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 828
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 829 qlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 908
Cdd:pfam01576 85 --------------EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 909 EEQKKWLDQEMEKVLQQRRALEELGEEL----HKREAI-------LAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 977
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLsklkNKHEAMisdleerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 978 LEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDsLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1058 YKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFSELEMQLEEQQRLVYW 1137
Cdd:pfam01576 310 DTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALEELTEQLEQAKRNKAN 374
|
410 420
....*....|....*....|....*...
gi 203096856 1138 LE---VALERQRLEMDRQL-TLQQKEHE 1161
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 ... |
803-1153 |
3.23e-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: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 803 KKQATERLVSLSAQSEKRLQELERNVQL--MRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIK 880
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 881 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKR 960
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE--ELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 961 LRSS------QALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRgEIDSLRQEKDSLLKQRLEIDGKLRQGSLL 1034
Cdd:pfam02463 307 RRKVddeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1035 SPEEERTLFQLDEAIEALDAAIEYKNEAitcRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQ 1114
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLEL---ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 203096856 1115 HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL 1153
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
794-1062 |
3.28e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 794 QSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 873
Cdd:COG1340 7 SSSLEELEEKI---EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 874 QKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQEMEKVLQQRraLEELGEELHKREAILAKKEA 948
Cdd:COG1340 84 NEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPEEEKELVEK--IKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 949 LMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKSGQLRqgsaQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKL 1028
Cdd:COG1340 162 LKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----EEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270
....*....|....*....|....*....|....
gi 203096856 1029 RQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1062
Cdd:COG1340 226 DE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
685-877 |
3.58e-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: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 685 KARVQARQVPPATASEW---RLAQAQQKIRELAINI---RMKEELIgelvrtgkAAQALNRQHSQRIRELEQEAEQVRAE 758
Cdd:COG3206 163 EQNLELRREEARKALEFleeQLPELRKELEEAEAALeefRQKNGLV--------DLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 759 LSEGQRQLRELEGK------ELQDAGERSRLQEFRRRVAAAQSQVQVLKEK--------KQATERLVSLSAQSEKRLQEL 824
Cdd:COG3206 235 LAEAEARLAALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 203096856 825 ERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKIL 877
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
845-987 |
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 203096856 845 ETEQKRRLEAEMSKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 923
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 203096856 924 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 987
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
785-1130 |
4.80e-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: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 785 EFRRRVAAAqsqvqvLKEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrRLREETE-------QKRRLEAEMS 857
Cdd:TIGR02169 167 EFDRKKEKA------LEELEEVEENIERLDLIIDEKRQQLER--------------LRREREKaeryqalLKEKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 858 KRQHRVKELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVSLEQQQKiEEQKKWLDQEMEKVLQQRRALEELGEELH 937
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTE-EISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 938 KREAILAKKEALMQEktgLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQ----------SQQQIRGEI 1007
Cdd:TIGR02169 305 SLERSIAEKERELED---AEERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1008 DSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEER---TLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNL 1084
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 203096856 1085 MaklsylsssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1130
Cdd:TIGR02169 458 E---------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
784-1029 |
5.34e-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: 44.44 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 784 QEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 862
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 863 VKELELKHEQQQKILKIKTEeiAAFQRKRRSGSNGSVVSLEQQQKIEEQKK----WLDQEMEKVLQQRRA---------- 928
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQ--AWLEEQKEQKREARTEKQAYWQVVEGALDaqlaLLKAAIAARRSGAKAelkaletwyk 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 929 --LEELG---EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV----RVSSRLEHLEKELSEKSGQLrqgsAQS 999
Cdd:pfam12128 758 rdLASLGvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQL----ARL 833
|
250 260 270
....*....|....*....|....*....|
gi 203096856 1000 QQQIRGEIDSLRQEKDSLLKQRLEIDGKLR 1029
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
934-1197 |
5.82e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 934 EELHKREAILAKKEALMQEKTGLeSKRLRSSQALNEDIVRVSSRLEHLEKELseksgqlrQGSAQSQQQIRGEIDSLRQE 1013
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1014 KDSLLKQRLEiDGKLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSS 1093
Cdd:PRK11281 110 NDEETRETLS-TLSLRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1094 SETRAllckyfdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQL--LLQQS 1171
Cdd:PRK11281 168 NSQRL------------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQ 228
|
250 260
....*....|....*....|....*.
gi 203096856 1172 RDHLgegladsrrqyEARIQALEKEL 1197
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 ... |
702-1051 |
9.02e-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: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELsEGQRQLRELEGKELQDAGErs 781
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGE-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 rlqefrrrvaaaqsQVQVLKEKKQATerLVSLSAQSEKRLQElernvqlmrqqqgqlqrrLREETEQKRRLEAEMSKRQH 861
Cdd:pfam01576 300 --------------ELEALKTELEDT--LDTTAAQQELRSKR------------------EQEVTELKKALEEETRSHEA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 862 RVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKVLQQRRALEElgeelHKRE 940
Cdd:pfam01576 346 QLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RTLQQAKQDSE-----HKRK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 941 ailaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQ-----GSAQSQQQirgEIDSLRQEKD 1015
Cdd:pfam01576 409 ----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvSSLESQLQ---DTQELLQEET 481
|
330 340 350
....*....|....*....|....*....|....*...
gi 203096856 1016 sllKQRLEIDGKLRQgsllsPEEERT--LFQLDEAIEA 1051
Cdd:pfam01576 482 ---RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
694-960 |
1.03e-03 |
|
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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 694 PPATASEWRLAQAQ----QKIRELAINIRMKEELIGELVRTGKAAQALnrqhSQRIRELEQEAEQVRAElsEGQRQLREL 769
Cdd:COG4913 220 EPDTFEAADALVEHfddlERAHEALEDAREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLW--FAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 770 EGKELQDAGERSRLQEfrrRVAAAQSQVQVLKEKKQATERlvSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreeteQK 849
Cdd:COG4913 294 EAELEELRAELARLEA---ELERLEARLDALREELDELEA--QIRGNGGDRLEQLER---------------------EI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 850 RRLEAEMSKRQHRVKELelkhEQQQKILKIKT-EEIAAFQRKRRsgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRA 928
Cdd:COG4913 348 ERLERELEERERRRARL----EALLAALGLPLpASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270
....*....|....*....|....*....|..
gi 203096856 929 LEElgeelhkreailaKKEALMQEKTGLESKR 960
Cdd:COG4913 417 LRR-------------ELRELEAEIASLERRK 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
744-934 |
1.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 744 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQ 822
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 823 ELERNVQLMRQQQGQLQRRLREET-----EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsng 897
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK------ 710
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 203096856 898 svvslEQQQKIEEQKKWLDQEMEKV-----LQQRRALEELGE 934
Cdd:PRK03918 711 -----KELEKLEKALERVEELREKVkkykaLLKERALSKVGE 747
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
698-951 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 698 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDA 777
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 778 GERSRLqefrrrVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE----QKRRLE 853
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 854 AEMSKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 926
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 203096856 927 RALEELGEELHKREAILAKKEALMQ 951
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
902-1196 |
2.13e-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: 42.63 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 902 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILakkealmqEKTGLESKRLRS-----SQALNEDIVR--- 973
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL--------EAAEEEVDSLKSqladyQQALDVQQTRaiq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 974 ---VSSRLEHLEK-----ELSEKSGQLRQGSAQSQQQirgEIDSLRQEkdslLKQRLEIDGKLRQgsllspeeertlfQL 1045
Cdd:COG3096 415 yqqAVQALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1046 DEAIEAL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT-- 1109
Cdd:COG3096 475 EKAYELVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaa 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1110 --LREEQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NMQLLLQQSRDHLGEGLA 1180
Cdd:COG3096 553 eeLEELLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALA 623
|
330
....*....|....*.
gi 203096856 1181 DSRRQYEARIQALEKE 1196
Cdd:COG3096 624 DSQEVTAAMQQLLERE 639
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
702-1206 |
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 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQdagers 781
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE-EDLQ------ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 rlqefrrrvAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 861
Cdd:pfam05483 321 ---------IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 862 RVKEL-ELKHEQQQKILKIKT----EEIAAFQRKrrsgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRaleelgEEL 936
Cdd:pfam05483 392 ELEEMtKFKNNKEVELEELKKilaeDEKLLDEKK-------------QFEKIAEELKGKEQELIFLLQARE------KEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 937 HKRE----AILAKKEALMQE----KTGLESKRLRSSQAL---------NEDIVRVSSRL-----EHLEKELSEKSGQLR- 993
Cdd:pfam05483 453 HDLEiqltAIKTSEEHYLKEvedlKTELEKEKLKNIELTahcdkllleNKELTQEASDMtlelkKHQEDIINCKKQEERm 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 994 ----QGSAQSQQQIRGEIDSLRQEkdsLLKQRLEIDGKL-------RQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1062
Cdd:pfam05483 533 lkqiENLEEKEMNLRDELESVREE---FIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1063 ITCRQRVLRAsasllsqcemnlmakLSYLSSSETRALLCkYFDKVVTLREEQHQQQIAFSEL----EMQLEEQQRLVYWL 1138
Cdd:pfam05483 610 IEELHQENKA---------------LKKKGSAENKQLNA-YEIKVNKLELELASAKQKFEEIidnyQKEIEDKKISEEKL 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 203096856 1139 EVALERQRLEMDRQLTLQQKeheqnMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQE 1206
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
735-1020 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 735 QALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAA----QSQVQVLK-EKKQATER 809
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSglkkDSKLKSLEiAVEQKKEE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 810 LVSLSAQSEK----------------RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 873
Cdd:pfam10174 533 CSKLENQLKKahnaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 874 QKILKIKTEEIAAFQRKRRSGSngsvvsleqQQKIEEQKKWLDQEMEKVLQQR-----RALEELGEELHKREAILAKKEA 948
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKG---------AQLLEEARRREDNLADNSQQLQleelmGALEKTRQELDATKARLSSTQQ 683
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 203096856 949 LMQEKTG-LESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQ--LRQGSAQSQQQIRGEIDSLRQEKDSLLKQ 1020
Cdd:pfam10174 684 SLAEKDGhLTNLRAERRKQLEE---ILEMKQEALLAAISEKDANiaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
693-898 |
3.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 693 VPPATASEWRLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAEQVRAELSEGQRQLREL 769
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 770 E---GKELQDAGERSR-------------LQEFRRRVAA----AQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQ 829
Cdd:COG3883 85 ReelGERARALYRSGGsvsyldvllgsesFSDFLDRLSAlskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 203096856 830 LMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGS 898
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
742-1196 |
3.51e-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: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 742 SQRIRELEQEAEQVRAELSEGQRQLRELEgkelqdagersrlqefrrrvAAAQSQVQVLKEKKQatERLVSLSAQSEKRL 821
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALK--------------------SESQNKIELLLQQHQ--DRIEQLISEHEVEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 822 QELERNVQLMRQQQGQLQRRLREETEQKRRLEA----EMSKRQHRVKELELKHEQQQKILKIKTEEIaafqRKRRSGSNG 897
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEEL----EKQLVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 898 SVVSLE-QQQKIEEQKKWLDQEMEKVLQqrraleelgeELHKREailaKKEALMQEktglESKRLRSSQALNedivrvSS 976
Cdd:pfam15921 357 ELTEARtERDQFSQESGNLDDQLQKLLA----------DLHKRE----KELSLEKE----QNKRLWDRDTGN------SI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 977 RLEHLEKELSEKSGQLRQGSA-----------QSQQQ---IRGEIDSLrqEKDSLLKQRLE--------IDGKLRQGSLL 1034
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEAllkamksecqgQMERQmaaIQGKNESL--EKVSSLTAQLEstkemlrkVVEELTAKKMT 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1035 SPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrVLRASASLLSQCEMNLMAKLSYLSSSETRA----LLCKYFDKVVtl 1110
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEIT----KLRSRVDLKLQELQHLKNEGDHLRNVQTECealkLQMAEKDKVI-- 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1111 reEQHQQQIafsELEMQLEEQQ-RLVYWLEValERQRLEM---DRQLTLQQKEheqnmqlLLQQSRDhlgeglaDSRRQY 1186
Cdd:pfam15921 565 --EILRQQI---ENMTQLVGQHgRTAGAMQV--EKAQLEKeinDRRLELQEFK-------ILKDKKD-------AKIREL 623
|
490
....*....|
gi 203096856 1187 EARIQALEKE 1196
Cdd:pfam15921 624 EARVSDLELE 633
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
704-1061 |
3.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 704 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAE--LSEGQRQLRELEGKELQDAGE-- 779
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagLDDADAEAVEARREELEDRDEel 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 780 RSRLQEFRRRVAAAQSQVQVLKEKkqaTERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 859
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRED---ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 860 QHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSN-----------GSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRA 928
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleaGKCPECGQPVEGSPHVETIEEDRERVEELEAE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 929 LEELGEELHKREAILAKKEALMQEKTGLES---KRLRSSQALNEDIVRVSSRLEHLEkELSEKSGQLR---QGSAQSQQQ 1002
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERleeRREDLEELIAERRETIEEKRERAE-ELRERAAELEaeaEEKREAAAE 562
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 203096856 1003 IRGEIDSLRQEKDSLLKQRLEIDGKLrqgsllspEEERTLFQLDEAIEALDAAIEYKNE 1061
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERI--------ESLERIRTLLAAIADAEDEIERLRE 613
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
748-965 |
3.91e-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: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 748 LEQEAEQVRAELSEGQRQLRElegkelqdagERSRLQ-EFRRRVAAAQSQVQVLKEKKQAT-ERLVSLSAQSEKRLQELE 825
Cdd:pfam07111 468 PPPPAPPVDADLSLELEQLRE----------ERNRLDaELQLSAHLIQQEVGRAREQGEAErQQLSEVAQQLEQELQRAQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 826 RNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH--------RVKELELKHEQQQKILKIKTEEIAAFQRKrrsgsng 897
Cdd:pfam07111 538 ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqeKVAEVETRLREQLSDTKRRLNEARREQAK------- 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 203096856 898 SVVSLEQQQKIEEQKKWLDQEMEKVlqQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQ 965
Cdd:pfam07111 611 AVVSLRQIQHRATQEKERNQELRRL--QDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQ 676
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
702-1076 |
4.28e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINI-RMKEELigelvrTGKAAQALNrqhSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAG 778
Cdd:PRK11281 88 QLAQAPAKLRQAQAELeALKDDN------DEETRETLS---TLSLRQLESRLAQTLDQLQNAQNDLAEYNSQlvSLQTQP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 779 ERS---------RLQEFRRRVAAAQ-SQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMrqqqgqlqrrlreETE 847
Cdd:PRK11281 159 ERAqaalyansqRLQQIRNLLKGGKvGGKALRPSQRVLLQaEQALLNAQNDLQRKSLEGNTQLQ-------------DLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 848 QKRRleAEMSKRQHRVkelelkhEQQQKILKikteeiAAFQRKRRSGSNGSVVSLEQQQKIEE--QKKWLDQEMEKVLQQ 925
Cdd:PRK11281 226 QKQR--DYLTARIQRL-------EHQLQLLQ------EAINSKRLTLSEKTVQEAQSQDEAARiqANPLVAQELEINLQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 926 RRALEELGEELHkreailakkeALMQE----KTGLESKrLRSSQALNEDI-----VRVSSRLEHLEKElSEKSGQLRQGS 996
Cdd:PRK11281 291 SQRLLKATEKLN----------TLTQQnlrvKNWLDRL-TQSERNIKEQIsvlkgSLLLSRILYQQQQ-ALPSADLIEGL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 997 AQSQQQIRGEIDSLRQEKDSLLKQRLEIDgKL--RQGSLLSPEEERTLFQ--------LDEAIEALDAAIeykNEAITC- 1065
Cdd:PRK11281 359 ADRIADLRLEQFEINQQRDALFQPDAYID-KLeaGHKSEVTDEVRDALLQllderrelLDQLNKQLNNQL---NLAINLq 434
|
410
....*....|...
gi 203096856 1066 --RQRVLRASASL 1076
Cdd:PRK11281 435 lnQQQLLSVSDSL 447
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
704-823 |
4.45e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 704 AQAQQKIRELAINIrmkEELIGELvrtgkaaQALNRQHSQRIRELE---QEAEQVRAELSEGQRQLRELEGKELQDAger 780
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASL-------EELERELEQKAEEAEallKEAEKLKEELEEKKEKLQEEEDKLLEEA--- 571
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 203096856 781 srLQEFRRRVAAAQSQV-QVLKEKKQatERLVSLSAQSEKRLQE 823
Cdd:PRK00409 572 --EKEAQQAIKEAKKEAdEIIKELRQ--LQKGGYASVKAHELIE 611
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
702-824 |
4.92e-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: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 781
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 203096856 782 RLQefrRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQEL 824
Cdd:COG4942 189 ALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-1201 |
5.48e-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: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAEQVRAELSEGQRQLRELEGKElqDAGERS 781
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 861
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 862 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 922
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 923 L---------------QQRRALEE--LGEELHKREAILAKKEALMQE------------KTGLESKRLRSSQALNEDIVR 973
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPRldpdslagkldfKPHPFRAWLEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 974 VSS--RLEHLEKELSeKSGQLRQGSAQSQQQIRGEIDSLR------QEKDSLLKQRLEidgklrqgsllspEEERTLFQL 1045
Cdd:COG4913 564 VDSpeELRRHPRAIT-RAGQVKGNGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELA-------------ELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1046 DEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQI 1119
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1120 AFSELEMQLE-----------EQQRLVYWLEVALER-QRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYE 1187
Cdd:COG4913 700 ELEELEEELDelkgeigrlekELEQAEEELDELQDRlEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
570
....*....|....
gi 203096856 1188 ARIQALEKELGRYM 1201
Cdd:COG4913 780 ARLNRAEEELERAM 793
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
790-922 |
5.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 790 VAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrLREETEQ-KRRLEAEMSKRQHRVKELE 867
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 203096856 868 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV 922
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKK 623
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
782-1057 |
6.90e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 782 RLQEFRRRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------KRLQELErnvqlmrqqqgqlqRRLREETEQKRRLE 853
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 854 AEMSKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 930
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 931 ELGEElhkREAILAkkealmqeKTGLESKrlrssqalneDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSL 1010
Cdd:PRK02224 290 ELEEE---RDDLLA--------EAGLDDA----------DAEAVEARREELEDRDEELRDRLEE-CRVAAQAHNEEAESL 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 203096856 1011 RQEKDSLlkqRLEIDGKLRQGSLLSPEEERTLFQLD---EAIEALDAAIE 1057
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIE 394
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
739-1023 |
7.67e-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: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 739 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS-------RLQEFRRRVAAAQSQVQVLKEK-KQA---- 806
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKsqnslqeKLAQEKSRVADAEEKILELQQKlEHAhkvc 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 807 -TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRL------REETEQKRR--------LEAEMSKRQHRVKELELKHE 871
Cdd:pfam15742 145 lTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRklldqnVNELQQQVRslqdkeaqLEMTNSQQQLRIQQQEAQLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 872 QQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELHKReailakKEALM 950
Cdd:pfam15742 225 QLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEKHH 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 203096856 951 QEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQsQQQIRGEIDSLRQEKDSLLKQRLE 1023
Cdd:pfam15742 281 HHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-969 |
8.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKaaqalNRQHSQRIRELEQEAEQVRAE-LSEGQRQLRELEGKELQDAGER 780
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 781 SRLQEFRRRVAAAQSQVQVLKEKKQATE--------RLVSLSAQS----EKRLQELE---------RNVQLMRQQQGQLQ 839
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEeelaellkELEELGFESveelEERLKELEpfyneylelKDAEKELEREEKEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 840 RRLREETEQKRrleAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEM 919
Cdd:PRK03918 622 KKLEEELDKAF---EELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 203096856 920 EKVLQQRRALEELGEELHKREAILAKKEALmQEKTgLESKRLRSSQALNE 969
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEEL-REKV-KKYKALLKERALSK 744
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
858-1020 |
9.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 858 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 936
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 937 HKREAILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKSGQLrQGSAQSQQQIRGEIDSLRQE-- 1013
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEea 155
|
....*..
gi 203096856 1014 KDSLLKQ 1020
Cdd:PRK12704 156 KEILLEK 162
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
742-1081 |
9.26e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 742 SQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRL----QEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQS 817
Cdd:PRK10929 101 NMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLpqqqTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 818 EK-----RLQELErnvqlmrqqqgqLQRRLREETEQKRRLEAEMSKRQHrvKELELKHEQQQKILKikteeiaaFQRKRR 892
Cdd:PRK10929 181 ESaalkaLVDELE------------LAQLSANNRQELARLRSELAKKRS--QQLDAYLQALRNQLN--------SQRQRE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 893 SGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEAL-----MQEKTGLESKR-----LR 962
Cdd:PRK10929 239 AER-----ALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQaasqtLQVRQALNTLReqsqwLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 963 SSQALNEDIVRVSSRLEHLEKelseksgqlrqgsaqsQQQIRGEIDSLRQEK----DSLLKQRLEIDGKLRQGSLLSPEE 1038
Cdd:PRK10929 314 VSNALGEALRAQVARLPEMPK----------------PQQLDTEMAQLRVQRlryeDLLNKQPQLRQIRQADGQPLTAEQ 377
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 203096856 1039 ERTlfqldeaieaLDAAIEYKNEAITcrqrvlrasaSLLSQCE 1081
Cdd:PRK10929 378 NRI----------LDAQLRTQRELLN----------SLLSGGD 400
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
781-1200 |
9.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 781 SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQ 860
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 861 HRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKRE 940
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 941 AILAKKEALMQEKTGLESKR------LRSSQALNEDIVRVSSRLEHLEKELSEKSG----------QLRQGSAQSQQQIR 1004
Cdd:PRK01156 343 KKKSRYDDLNNQILELEGYEmdynsyLKSIESLKKKIEEYSKNIERMSAFISEILKiqeidpdaikKELNEINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1005 GEIDSLRQEKDSLLKQRLEIDgklRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNE---AITCRQRVLRASASLLSQCE 1081
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELS---RNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEkksRLEEKIREIEIEVKDIDEKI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 1082 MNLMAKLSYLSSSET-------------RALLCKYFDKVVTLREEQHQQQIAFSELE-MQLEE-QQRLVYWLEVALERQR 1146
Cdd:PRK01156 500 VDLKKRKEYLESEEInksineynkiesaRADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDlDSKRTSWLNALAVISL 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 203096856 1147 LEMDrqlTLQQKEHEQNMQLLLQQSRDHLGE-GLADSRRQYEARIQALEKELGRY 1200
Cdd:PRK01156 580 IDIE---TNRSRSNEIKKQLNDLESRLQEIEiGFPDDKSYIDKSIREIENEANNL 631
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
710-971 |
9.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 710 IRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQE---- 785
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEeles 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 786 -------FRRRVAAAQSQVQVLKEKKQATE----RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEA 854
Cdd:COG4372 106 lqeeaeeLQEELEELQKERQDLEQQRKQLEaqiaELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096856 855 EMSKRQHR---VKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEE 931
Cdd:COG4372 186 DELLKEANrnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 203096856 932 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDI 971
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| |
