|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
56-391 |
2.38e-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: 495.70 E-value: 2.38e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYG 135
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 136 QTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTASR-DIQLREDE 213
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 214 RGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRLPRPAPGQL--LVSKFHF 291
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 292 VDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 371
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 767984051 372 SDFDETLNTLNYASRAQNIR 391
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
56-397 |
1.04e-138 |
|
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: 427.76 E-value: 1.04e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVT-------LGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 128
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 129 ATVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLevGTASRD 206
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMiGT-------PDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 207 IQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRlprpapGQLLV 286
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 287 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIAC 366
Cdd:smart00129 226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304
|
330 340 350
....*....|....*....|....*....|.
gi 767984051 367 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 397
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
62-390 |
2.99e-134 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 415.43 E-value: 2.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 62 RVRPLLPKELLHGHQSCLQVEPGLGRVTL-------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 134
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 135 GQTGSGKTYTMGEasvaslLEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLEVGTAS-RDIQLRED 212
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 213 ERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpAPGQLLVSKFHFV 292
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTG-----GEESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 293 DLAGSERVLKTG-STGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 371
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 767984051 372 SDFDETLNTLNYASRAQNI 390
Cdd:pfam00225 308 SNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
56-388 |
2.76e-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: 388.92 E-value: 2.76e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKELLHGHqSCLQVEPG------LGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 129
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 130 TVFAYGQTGSGKTYTMGEASvasllEDEQGIVPRAMAEAFKLIDENDLLD--CLVHVSYLEVYKEEFRDLLEvGTASRDI 207
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 208 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpaPGQLLVS 287
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 288 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 367
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 767984051 368 SPSSSDFDETLNTLNYASRAQ 388
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
57-390 |
6.23e-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: 345.10 E-value: 6.23e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELLHGHQSCLQV--------EPGLGRVTL--------------GRDRHFGFHVVLAEDAGQEAVYQA 114
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 115 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEE 193
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 194 FRDLLEvgTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAP 273
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 274 SRLPrpapgQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 353
Cdd:cd01370 234 SINQ-----QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 767984051 354 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNI 390
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
57-397 |
2.55e-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: 333.17 E-value: 2.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKEL---------LHGHQSCLQVEPGLGRVTLGRDRH---FGFHVVL----AED---AGQEAVYQACVQ 117
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 118 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLID--ENDLLDCLVHVSYLEVYKEEFR 195
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 196 DLLEVGTASRDIQLREDE---RGNVVLcGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRgRA 272
Cdd:cd01365 157 DLLNPKPKKNKGNLKVREhpvLGPYVE-DLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 273 PSRLPRPAPgqlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQR-----RGSHIPYRDSKI 347
Cdd:cd01365 235 DAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 767984051 348 TRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 397
Cdd:cd01365 312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
57-390 |
1.10e-102 |
|
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: 1.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTL--GRD------RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 128
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 129 ATVFAYGQTGSGKTYTMGEASVAsllEDEQGIVPRAMAEAFKLID-ENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRdI 207
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 208 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQrgrapSRLPRPAPGQLLVS 287
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHIRVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 288 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMIACV 367
Cdd:cd01371 234 KLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANI 311
|
330 340
....*....|....*....|...
gi 767984051 368 SPSSSDFDETLNTLNYASRAQNI 390
Cdd:cd01371 312 GPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
57-390 |
4.14e-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: 4.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELLHG--------HQSCLQVEPGLGRvtlgrdrhFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 128
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 129 ATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGtaSRDIQ 208
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 209 LREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPsrlprPAPGQLLVSK 288
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 289 FHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 368
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 767984051 369 PSSSDFDETLNTLNYASRAQNI 390
Cdd:cd01374 300 PAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
57-392 |
6.43e-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: 311.45 E-value: 6.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELlHGHQSCLQVEPGLG-RVTL---GRDRH-FGFHVVLAEDAGQEAVYQAcVQPLLEAFFEGFNATV 131
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 132 FAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLIDENDLLDCLVH--VSYLEVYKEEFRDLLEVGTASR---D 206
Cdd:cd01366 82 FAYGQTGSGKTYTMEGP------PESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 207 IQLREDErGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLeqRGRAPSRlprpapGQLLV 286
Cdd:cd01366 156 IRHDSEK-GDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 287 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 366
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 767984051 367 VSPSSSDFDETLNTLNYASRAQNIRN 392
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
57-399 |
1.56e-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: 308.49 E-value: 1.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTL--------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 128
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 129 ATVFAYGQTGSGKTYTM-GEASVASLLEDEQ----GIVPRAMAEAFKLIDENDLlDCLVHVSYLEVYKEEFRDLLEV-GT 202
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 203 ASRDIQLREDER--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSrlprpa 280
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID------ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 281 pGQLLV--SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGN 358
Cdd:cd01364 237 -GEELVkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767984051 359 AKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWR 399
Cdd:cd01364 313 TKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
57-390 |
5.04e-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: 5.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELLHGHQSCLQVEPGlGRVTLGRD---RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFA 133
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPE-DTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 134 YGQTGSGKTYTMgEASvaslLEDEQ--GIVPRAMAEAFKLIDEND-LLDCLVHVSYLEVYKEEFRDLLEVgtaSRD-IQL 209
Cdd:cd01369 83 YGQTSSGKTYTM-EGK----LGDPEsmGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 210 REDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPsrlprpapGQLLVSKF 289
Cdd:cd01369 155 HEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVET--------EKKKSGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 290 HFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSP 369
Cdd:cd01369 227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSP 304
|
330 340
....*....|....*....|.
gi 767984051 370 SSSDFDETLNTLNYASRAQNI 390
Cdd:cd01369 305 SSYNESETLSTLRFGQRAKTI 325
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
96-397 |
2.87e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 287.41 E-value: 2.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 96 FGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDEN 175
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 176 DLLDCL-VHVSYLEVYKEEFRDLLEVGTASRDIqlREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHL 254
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 255 SSRSHTVFTVTLEQRGRAPSRLPRpapgqllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQ 334
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984051 335 RRGsHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 397
Cdd:COG5059 282 KSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
56-397 |
9.53e-84 |
|
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: 278.24 E-value: 9.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLG-RDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 134
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 135 GQTGSGKTYTM-GEA-SVASLLEDEQGIVPRAMAEAFKLID-----ENDLLDCLVHVSYLEVYKEEFRDLLEvgTASRDI 207
Cdd:cd01373 82 GQTGSGKTYTMwGPSeSDNESPHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 208 QLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEqrgrapSRLPRPAPGQLLVS 287
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE------SWEKKACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 288 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 366
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340 350
....*....|....*....|....*....|.
gi 767984051 367 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 397
Cdd:cd01373 314 VHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
56-388 |
1.67e-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: 266.18 E-value: 1.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKELLHGHQSCLQVE--------------PGLGRVTLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLL 120
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhppkgsaANKSERNGGQKETkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 121 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDlldclVHVSYLEVYKEEFRDLLEV 200
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 201 GTASRD-----IQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSR 275
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 276 LPRPAPGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRG--SHIPYRDSKITRILKD 353
Cdd:cd01368 231 DVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSKLTHLFQN 310
|
330 340 350
....*....|....*....|....*....|....*
gi 767984051 354 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQ 388
Cdd:cd01368 311 YFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
56-386 |
3.09e-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: 264.54 E-value: 3.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKEL---------LHGHQSCLQVEPGLgRVTLGR--DRH-FGFHVVLAEDAGQEAVYQACVQPLLEAF 123
Cdd:cd01367 1 KIKVCVRKRPLNKKEVakkeidvvsVPSKLTLIVHEPKL-KVDLTKyiENHtFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 124 FEGFNATVFAYGQTGSGKTYTMGEASvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGT 202
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 203 asrDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLeqrgrapsrlpRPAPG 282
Cdd:cd01367 158 ---RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 283 QLLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSSLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAK 360
Cdd:cd01367 224 NKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSK 300
|
330 340
....*....|....*....|....*.
gi 767984051 361 TVMIACVSPSSSDFDETLNTLNYASR 386
Cdd:cd01367 301 TCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
56-388 |
1.01e-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: 260.13 E-value: 1.01e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 56 PVRVALRVRPLLPKELLHGHQSCLQVEPGLgRVTLGRDRHFG------FHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 129
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 130 TVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDENDLLDClVHVSYLEVYKEEFRDLLEVgtASRDIQ 208
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlGS-------PEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 209 LREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGR-APSRLPRpapgqllvS 287
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERlAPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 288 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 367
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 767984051 368 SPSSSDFDETLNTLNYASRAQ 388
Cdd:cd01376 299 APERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
96-386 |
2.76e-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: 245.18 E-value: 2.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 96 FGFHVVLaEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASlleDEQGIVPRAMAEAFKLIDEN 175
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 176 DLLDCLVHVSYLEVYKEEFRDLL----EVGTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHL 251
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 252 NHLSSRSHTVFTVTLEQRGRAPSRlprpapGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALG 331
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLSS------EKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767984051 332 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 386
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
35-397 |
8.44e-60 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 226.35 E-value: 8.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 35 PEQSSLGMGLEAQRLP--GAEEAPVRVALRVRPLLPKEllhghQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVY 112
Cdd:PLN03188 76 PSSNPLKRKLSAETAPenGVSDSGVKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 113 QACVQPLLEAFFEGFNATVFAYGQTGSGKTYTM-GEASVAS---LLEDEQGIVPRAMAEAFKLIDENDL------LDCLV 182
Cdd:PLN03188 151 QLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQC 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 183 HVSYLEVYKEEFRDLLEvgTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVF 262
Cdd:PLN03188 231 RCSFLEIYNEQITDLLD--PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 263 TVTLEqrgrapSRLPRPAPG--QLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGS-- 338
Cdd:PLN03188 309 TCVVE------SRCKSVADGlsSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqr 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767984051 339 HIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 397
Cdd:PLN03188 383 HIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
743-1239 |
7.91e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 822
Cdd:COG1196 254 ELEELEAELAELEAEL---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 RLQEFRRRVAAAQSQVQVLKEK--------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLE 894
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEEleeaeaelAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 895 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 974
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 975 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKsgQLRQGSAQSQQQIRGEIDSLRQE 1054
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA--ALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1055 KDSLLKQ----RLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAK 1128
Cdd:COG1196 562 AIEYLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1129 LSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1208
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
490 500 510
....*....|....*....|....*....|.
gi 767984051 1209 LQQSRDHLGEGLADSRRQYEARIQALEKELG 1239
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-1103 |
9.06e-16 |
|
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: 83.18 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 766 GELVRTG---------KAAQALNRQhsQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAGE--RSRLQEFRRRVA 832
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKEleELEEELEqlRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 833 AAQSQVQVLKEKKQaterlvslsaQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHE 912
Cdd:TIGR02168 730 ALRKDLARLEAEVE----------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 913 QQQKILKIKTEEI------AAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILA 985
Cdd:TIGR02168 800 ALREALDELRAELtllneeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 986 KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGsaqsQQQIRGEIDSLRQEKDSLLKQRLEI 1065
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR----LEGLEVRIDNLQERLSEEYSLTLEE 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767984051 1066 DGKLRQGSLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1103
Cdd:TIGR02168 956 AEALENKIEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
785-1238 |
1.23e-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: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 785 RIRELEQEAEQVRAELSEGQRQLRELEgKELQDAgeRSRLQEFRRRVAAAQSQVqvlkEKKQATERLVslsaqsEKRLQE 864
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELE-AELAEL--EAELEELRLELEELELEL----EEAQAEEYEL------LAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 865 LERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLE 944
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 945 QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK 1024
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1025 ELSEKSGQLRQ---------GSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ----------------GSLLSPEE 1079
Cdd:COG1196 454 LEEEEEALLELlaelleeaaLLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaalllaglrglagaVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1080 ERTLFQLDEAIEALDAAIEYKNE--AITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ 1157
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDevAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1158 QQIAFSE-----------LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRR 1225
Cdd:COG1196 614 RYYVLGDtllgrtlvaarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490
....*....|...
gi 767984051 1226 QYEARIQALEKEL 1238
Cdd:COG1196 694 ELEEALLAEEEEE 706
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
108-329 |
1.24e-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: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 108 QEAVYqACVQPLLEAFFEGFN-ATVFAYGQTGSGKTYTMgeasvaslledeQGIVPRAMAEAFklidendlldclvhvSY 186
Cdd:cd01363 32 QPHVF-AIADPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAF---------------NG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 187 LEVYKEEFRDLLEvgtasrdiqlredergnvvlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHLNHLSSRSHTVFTVtl 266
Cdd:cd01363 84 INKGETEGWVYLT------------------------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI-- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984051 267 eqrgrapsrlprpapgqllvskfhFVDLAGSERvlktgstgerlkesiqINSSLLALGNVISA 329
Cdd:cd01363 137 ------------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
746-1067 |
4.31e-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: 67.77 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 746 QAQQKIRELAINIRMKEELIGE-------LVRTGKAAQALNRQHSQ-----------RIRELEQEAEQVRAELSEGQRQL 807
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNElerqlksLERQAEKAERYKELKAElrelelallvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 808 ----RELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQElernvqlmrqqQGQLQRRL 883
Cdd:TIGR02168 256 eeltAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER-----------QLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 884 REETEQKR-RLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvslEQQQKIEEQKKWLDQEMEK 962
Cdd:TIGR02168 325 LEELESKLdELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE----------ELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 963 VLQQRRALEELGEEL----HKREAILAKKEALMQEKTGLESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKSGQLRQGS 1037
Cdd:TIGR02168 395 IASLNNEIERLEARLerleDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350
....*....|....*....|....*....|
gi 767984051 1038 aQSQQQIRGEIDSLRQEKDSLLKQRLEIDG 1067
Cdd:TIGR02168 475 -QALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
745-1080 |
4.53e-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: 67.77 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 745 AQAQQKIR-----------ELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAEQVRAELSEGQRQLREL 810
Cdd:TIGR02168 207 RQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 811 EGkelqdagersRLQEFRRRVAAAQSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 890
Cdd:TIGR02168 287 QK----------ELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 891 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNgsvvsleQQQKIEEQKKWLDQEMEKVLQQRRAL 970
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-------EIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 971 EELGEElHKREAILAKKEALMQEKTGLESKRLRSSQALNedivRVSSRLEHLEKELSEKSGQLRQGSAQ--SQQQIRGEI 1048
Cdd:TIGR02168 427 LKKLEE-AELKELQAELEELEEELEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
|
330 340 350
....*....|....*....|....*....|...
gi 767984051 1049 DSLRQEKDSLLKQRLEIDGKL-RQGSLLSPEEE 1080
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILgVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
743-1058 |
5.89e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE-------LEQEAEQVRAELSEGQRQLRELEGK-- 813
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTELEAEie 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 814 --ELQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATERLVSLSAQ---SEKRLQELERNVQLMRQQQGQLQRRLREET 887
Cdd:TIGR02168 765 elEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAEltlLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 888 EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKvlqqR 967
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL------LRSELEELSEELRELESKRSEL----R 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 968 RALEELGEELHKreAILAKKEALMQEKTGLEskRLRSSQALNEDIVrvssrlehlekelseksGQLRQGSAQSQQQIRGE 1047
Cdd:TIGR02168 915 RELEELREKLAQ--LELRLEGLEVRIDNLQE--RLSEEYSLTLEEA-----------------EALENKIEDDEEEARRR 973
|
330
....*....|.
gi 767984051 1048 IDSLRQEKDSL 1058
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
781-1171 |
6.11e-11 |
|
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: 66.97 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 781 QHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELqdagersrlqefrrrvaaaQSQVQVLKEKKQATERLVSlsaQSEK 860
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL-------------------KSELKNQEKKLEEIQNQIS---QNNK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 861 RLQELERNVQLMRqqqgqlqrrlreetEQKRRLEAEMSKRQhrvKELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSv 940
Cdd:TIGR04523 336 IISQLNEQISQLK--------------KELTNSESENSEKQ---RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 941 vSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELhKREAILAKKE--ALMQEKTGLES-----KRLRSSQ-----A 1007
Cdd:TIGR04523 395 -DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEikDLTNQDSVKELiiknlDNTRESLetqlkV 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1008 LNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQsQQQIRGEIDSLRQEKDSLL-------KQRLEIDGKLRQ--GSLLSPE 1078
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSLKekiekleSEKKEKESKISDleDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1079 EERTLFQLDEAIEALDAAIEYKNEAITcrqrvlrasaSLLSqcemnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQ 1158
Cdd:TIGR04523 552 FELKKENLEKEIDEKNKEIEELKQTQK----------SLKK-------------KQEEKQELIDQKEKEKKDLIKEIEEK 608
|
410
....*....|...
gi 767984051 1159 QIAFSELEMQLEE 1171
Cdd:TIGR04523 609 EKKISSLEKELEK 621
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
744-1071 |
8.03e-11 |
|
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: 66.58 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 744 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalnrqhSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDagERSR 823
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEEKQ-NEIEK--LKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 824 LQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 903
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 904 VKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAI 983
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 984 LAKK-EALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKsgqlrqgsaqsQQqirgEIDSLRQEKDSLLK 1060
Cdd:TIGR04523 522 LKEKiEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEK-----------NK----EIEELKQTQKSLKK 582
|
330
....*....|.
gi 767984051 1061 QRLEIDGKLRQ 1071
Cdd:TIGR04523 583 KQEEKQELIDQ 593
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
836-1120 |
1.85e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 836 SQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKR-RLEAEMSKRQHRVKELELKHEQQ 914
Cdd:COG1196 200 RQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELeELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 915 QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEK 994
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 995 tgLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSL 1074
Cdd:COG1196 360 --LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767984051 1075 LSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1120
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
741-1239 |
8.00e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 741 EWRLAQAQQKIRELAINIRmkeELIGELvrtgkaaqalnrqhsQRIRELEQEAEQVRAELSEGQRQLRELEGKElqdAGE 820
Cdd:PRK03918 199 EKELEEVLREINEISSELP---ELREEL---------------EKLEKEVKELEELKEEIEELEKELESLEGSK---RKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 821 RSRLQEFRRRVAAAQSQVQVLKEK----------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 890
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKvkelkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 891 RRLEaEMSKR----QHRVKELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQ 965
Cdd:PRK03918 338 ERLE-ELKKKlkelEKRLEELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 966 QRRALEELGEELH---------KREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQL-RQ 1035
Cdd:PRK03918 413 RIGELKKEIKELKkaieelkkaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1036 GSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAIT 1105
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1106 CRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALER 1185
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEE 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1186 QRLEMDR-QLTLQQKEHEQNMQLLLQQSRDHLG-----EGLADSRRQYEARIQALEKELG 1239
Cdd:PRK03918 645 LRKELEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
752-1098 |
8.66e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 752 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFR 828
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKRELSSL----------QSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 829 RRVAAAQSQVQVLKEKkqaTERLvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 908
Cdd:TIGR02169 702 NRLDELSQELSDASRK---IGEI-------EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 909 LK-HEQQQKILKIKT-------EEIAA---FQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 976
Cdd:TIGR02169 772 EDlHKLEEALNDLEArlshsriPEIQAelsKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 977 LHKR-EAILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKSGQLRQ-----GSAQSQQQIRGEIDS 1050
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRElerkiEELEAQIEKKRKRLS 920
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767984051 1051 LRQEKDSLLKQRL-EIDGKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1098
Cdd:TIGR02169 921 ELKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
782-1055 |
1.21e-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: 63.16 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 782 HSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERS-----RLQEFRRRV--------AAAQSQVQVLKEKKQAT 848
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLT-EEISELEKRLeeieqLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 849 ERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR-----------LEAEMSKRQHRVKELELKHEQQQKI 917
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteeyaeLKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 918 LKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEElhKREAILAKKEALMQEKTGL 997
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIKKQEWKLEQLAADL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767984051 998 ESKRlrssqalnEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEK 1055
Cdd:TIGR02169 465 SKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
837-1120 |
1.36e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 837 QVQVLKEKKQATERLVSLSAQSE--------KRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 908
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 909 LKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsleqqqKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKE 988
Cdd:TIGR02168 281 EEIEELQKELYALANEIS---------------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 989 ALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIR-----------------GEIDSL 1051
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAslnneierlearlerleDRRERL 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984051 1052 RQEKDSLLKQRLEIDGKLRQGSLlsPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1120
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
746-1252 |
1.83e-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: 62.68 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 746 QAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQ--------HSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQD 817
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 818 AGERSRLQEFRRRVAAAQSQVQvlkEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreETEQKRRLEAEM 897
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQH------------------IHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 898 SKRQHRVKELELKHEQQQKIlkikteeiaAFQRKRRSGSNGSVVSLEQQQKIE-EQKKWLDQEMEKVLQ----QRRALEE 972
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATI---------DTRTSAFRDLQGQLAHAKKQQELQqRYAELCAAAITCTAQceklEKIHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 973 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKEL-----SEKSGQLRQGSAQSQQQIRGE 1047
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1048 IDSLRQEKDSLLKQRLEIdgklrqgsllspEEERTLFQLDEAIEAldaaieykneaiTCRQRVlRASASLLSQcEMNLMA 1127
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASL------------KEQMQEIQQSFSILT------------QCDNRS-KEDIPNLQN-ITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1128 KLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLV----YWLEVALERQRlEMDRQLTLQQKEHEQ 1203
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTalhaLQLTLTQERVR-EHALSIRVLPKELLA 676
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 767984051 1204 NMQLLLQ--QSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKL 1252
Cdd:TIGR00618 677 SRQLALQkmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
739-1093 |
2.56e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 739 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR-QHSQRIRELEQEAEQVRAELSEGQRQLRELE-GKELQ 816
Cdd:PTZ00121 1440 AEEAKKADEAKKKAEEA---KKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkADEAK 1516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 817 DAGERSRLQEFRRRVAAAQS-QVQVLKEKKQATE--RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 893
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKAdEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 894 EAEMSKRQHRVKELELKHEQQQKIlkiKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVlqqRRALEEL 973
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKI---KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKI---KAAEEAK 1668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 974 GEELHKREAILAKKEALMQEKTGLESKRlrssqalNEDIVRVSSRLEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQ 1053
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKK-------EAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAKKEA 1739
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767984051 1054 EKDSLLKQRLEID-GKLRQGSLLSPEEERTLFQLDEAIEAL 1093
Cdd:PTZ00121 1740 EEDKKKAEEAKKDeEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
832-1077 |
2.79e-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: 60.93 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 832 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKH 911
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 912 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELHKREAILAKKEA 989
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 990 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKL 1069
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 767984051 1070 RQGSLLSP 1077
Cdd:COG4942 251 LKGKLPWP 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
785-1060 |
2.86e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 785 RIRELEQEAEQVRAELSEGQRQLRELEG------KELQDAGE-RSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQ 857
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREelekleKEVKELEElKEEIEELEKELESLEGSKRKLEEKIRELEERI---EE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 858 SEKRLQELERNVqlmrqqqgQLQRRLREETEQKRRLEAEMSKRQHRVKELElkheqqqKILKIKTEEIAAFQRKrrsgsn 937
Cdd:PRK03918 271 LKKEIEELEEKV--------KELKELKEKAEEYIKLSEFYEEYLDELREIE-------KRLSRLEEEINGIEER------ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 938 gsvvsLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRlrssqaLNEDIVRVSS 1017
Cdd:PRK03918 330 -----IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK------LEKELEELEK 398
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767984051 1018 RLEHLEKELSEksgqlrqgsaqsqqqIRGEIDSLRQEKDSLLK 1060
Cdd:PRK03918 399 AKEEIEEEISK---------------ITARIGELKKEIKELKK 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-1237 |
8.13e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 684 RISNCSQRAGARPGSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPA-TASEWRLAQAQQKIREL--AINIRM 760
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAArkAEEVRK 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 761 KEEL-IGELVRTGKAA-QALNRQHSQRIRELEQE--------AEQVRAELSEGQRQLRELEGKELQDAgERSRLQEFRRR 830
Cdd:PTZ00121 1190 AEELrKAEDARKAEAArKAEEERKAEEARKAEDAkkaeavkkAEEAKKDAEEAKKAEEERNNEEIRKF-EEARMAHFARR 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 831 VAAAQSQ-------VQVLKEKKQATERLVS----------LSAQSEKRLQELERNVQLMRQQQGQLQRRLREET------ 887
Cdd:PTZ00121 1269 QAAIKAEearkadeLKKAEEKKKADEAKKAeekkkadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaeaa 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 888 ---EQKRRLEAEMSKRQHRVKELElKHEQQQKI--LKIKTEEIAAFQRKRRSGSNGSVVSlEQQQKIEEQKKWLDQEMEK 962
Cdd:PTZ00121 1349 kaeAEAAADEAEAAEEKAEAAEKK-KEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKK 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 963 VLQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGS--AQS 1040
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKK 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1041 QQQIRGEIDSLRQEKDSLLKQRL-EIDGKLRQGSLLSPEEERTLFQLDEAIEALDA----AIEYKNEAITCRQRVLRaSA 1115
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALR-KA 1583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1116 SLLSQCEMNLMAKLSYLSSSETRAllckyfdKVVTLREEQhQQQIAFSELEMQLEEQQRLvywleVALERQRLEMDRQLT 1195
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKM-------KAEEAKKAE-EAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAE 1650
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 767984051 1196 LQQKEHEQNMQLLLQQSRdhlgEGLADSRRQYEARIQALEKE 1237
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAK----KAEEDKKKAEEAKKAEEDEK 1688
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
741-1238 |
1.75e-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: 59.30 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 741 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDA 818
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 819 --GERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLE 894
Cdd:TIGR02168 381 leTLRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 895 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 960
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 961 EKVL-------------QQRRALEELGEELHKREAILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 1020
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1021 ----------------HLEKELSE-------------KSGQLRQGSAQSQQQI---RGEIDSLRQEK------------- 1055
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPgyrivtldgdlvrPGGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1056 -DSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1134
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1135 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRD 1214
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 767984051 1215 --HLGEGLADSRRQYEARIQALEKEL 1238
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
785-1251 |
1.76e-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: 59.26 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 785 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQE----FRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEK 860
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 861 RLQELERNVQlmrqqqgqlqrrlrEETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIaafqrkrrSGSNGSV 940
Cdd:TIGR04523 226 QNNQLKDNIE--------------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--------EQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 941 VSLEQQ-QKIEEQKKWLDQEMEKVLqqrraLEELGEELHKREailakkealmQEKTGLESKRLRSSQA---LNEDIVRVS 1016
Cdd:TIGR04523 284 KELEKQlNQLKSEISDLNNQKEQDW-----NKELKSELKNQE----------KKLEEIQNQISQNNKIisqLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1017 SRLEHLEKELSEKSGQLRQgsAQSQ-QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQgsllspeEERTLFQLDEAIEALda 1095
Cdd:TIGR04523 349 KELTNSESENSEKQRELEE--KQNEiEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKL-- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1096 aiEYKNEAITCRQRVLRASASLLSQCEMNLmaklsylssSETRALLCKYFDKVVTLREEQhQQQIafSELEMQLEEQQRL 1175
Cdd:TIGR04523 418 --QQEKELLEKEIERLKETIIKNNSEIKDL---------TNQDSVKELIIKNLDNTRESL-ETQL--KVLSRSINKIKQN 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 1176 VYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSrdhlgegladsrRQYEARIQALEKELGRymwINQELKQK 1251
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 ... |
839-1140 |
2.54e-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: 58.83 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 839 QVLKEKKQATERLVSLSAQSEKRL----------QELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 908
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLELeeeyllyldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 909 LKHEQ-QQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELH-KREAILAK 986
Cdd:pfam02463 278 EKEKKlQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 987 KEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRqgSAQSQQQIRGEIDSLRQEKDSLLKQRLEID 1066
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--EAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984051 1067 GKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRqrvLRASASLLSQCEMNLMAKLSYLSSSETRAL 1140
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
733-930 |
5.46e-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: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 733 QVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEg 812
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 813 KELQDagersRLQEFRRRVAAAQSQVQVLKEK------------------KQATERLVSLSAQSEKRLQELERNVQLMRQ 874
Cdd:COG4942 97 AELEA-----QKEELAELLRALYRLGRQPPLAlllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 875 QQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 930
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1238 |
5.48e-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: 57.76 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 963 VLQQRRALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQ 1042
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1043 ------QIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1116
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1117 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1196
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767984051 1197 QQKEHEQNMQlLLQQSRDHLGEGLADSRRQY---EARIQALEKEL 1238
Cdd:TIGR02168 902 ELRELESKRS-ELRRELEELREKLAQLELRLeglEVRIDNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
739-1070 |
6.80e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 739 ASEWRLAQAQQKIRELAiniRMKEELIGELVRTGKAAQALNR--QHSQRIRELEQEAEQVRAELSEGQRQLRELEgkELQ 816
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKAD--EAK 1540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 817 DAGERSRLQEFRR--RVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERnvqlMRQQQGQLQRRLREETEQKRRLE 894
Cdd:PTZ00121 1541 KAEEKKKADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEEEKKMKAEEAKKAE 1616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 895 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAleelG 974
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK--AEEAKKAEEDEKK----A 1690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 975 EELHKREAILAKKEALMQEKTGLESKR---LRSSQALNEDIVRVSSRLEHLEKELSE----------KSGQLRQGSAQSQ 1041
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEeakkdeeekkKIAHLKKEEEKKA 1770
|
330 340 350
....*....|....*....|....*....|.
gi 767984051 1042 QQIRGEIDSLRQE--KDSLLKQRLEIDGKLR 1070
Cdd:PTZ00121 1771 EEIRKEKEAVIEEelDEEDEKRRMEVDKKIK 1801
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
57-198 |
8.53e-08 |
|
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: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 57 VRVALRVRPLLPKELlhghqsclQVEPGLGRVTLGRDRH----FGFHVVLAEDAGQEAVYQACVQpLLEAFFEGFNATVF 132
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984051 133 AYGQTGSGKTYTMgeasvaslledeqgiVPRAMAEAFKLIDENDLLDCL-VHVSYLEVYKEEFRDLL 198
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
744-989 |
9.01e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 744 LAQAQQKIRELAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 822
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 RLQEFRRRVAAAQSQVQVLKEkkQATERLVSLSAQSEK---RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSK 899
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 900 RQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsNGSVVSlEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK 979
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIK-KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
250
....*....|
gi 767984051 980 REAILAKKEA 989
Cdd:TIGR02169 488 LQRELAEAEA 497
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
541-1071 |
1.08e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 541 EEENRDFLAALEDAMEQYKLQSDRLREQQEEMV----ELRLRLELVRPGWGGPRLLNGLPPGSFVPRPHTAPLGGAHAHV 616
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSqkesKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 617 LGMVPPACLPGDEVGSEQRGEQVTNGREAGAELLTEVNRLGSGSSAASEEEEEEEEPPRRTLHLRRNRISNCSQRAGARP 696
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 697 GSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVppaTASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQ 776
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV---KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 777 ALNRQHSQRIRELEQE----AEQVRAELSEGQRQLRELEGK---ELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATE 849
Cdd:pfam02463 704 KEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKideEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 850 RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQ 929
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 930 RKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSS 1005
Cdd:pfam02463 864 TKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984051 1006 QALNED---------IVRVSSRLEHLEKELSEKSGQLRQGSA--QSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQ 1071
Cdd:pfam02463 944 EADEKEkeennkeeeEERNKRLLLAKEELGKVNLMAIEEFEEkeERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
743-1031 |
1.36e-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: 56.23 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGK--ELQDAGE 820
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 821 RSRLQEFRRRVAAAQSQVQ----VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 896
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 897 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 975
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 976 ELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSG 1031
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
737-1089 |
1.51e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 737 ATASEWRLAQAQQKIREL---AINIRMKEELIGELVRTGKAAQALNRQHSQRIR--ELEQEAEQVRA--ELSEGQRQLRE 809
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKadEAKKKAEEAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 810 LEgkELQDAGERSRLQEFRRRVAAAQSQVQVLK---EKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREE 886
Cdd:PTZ00121 1446 AD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKkkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 887 TEQKRRLEA-----EMSKRQHRVKELELKHEQQQKilkiKTEEIAAFQRKRRS--GSNGSVVSLEQQQKIEEQ------K 953
Cdd:PTZ00121 1524 ADEAKKAEEakkadEAKKAEEKKKADELKKAEELK----KAEEKKKAEEAKKAeeDKNMALRKAEEAKKAEEArieevmK 1599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 954 KWLDQEMEKVLQQRRALEEL--GEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVS--SRLEHLEKELSEK 1029
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEE 1679
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1030 SGQLRQGSAQSQQQIRGEidslRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEA 1089
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKE----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
744-1214 |
1.68e-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: 56.28 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 744 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAEQVRAELSEGQR----QLRELEGK------ 813
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQlvlans 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 814 ELQDAgeRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRL---------------QEL-ERNVQLMRQQQG 877
Cdd:pfam15921 357 ELTEA--RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrRELdDRNMEVQRLEAL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 878 QLQRRLREETEQKRRLEAEMSKRQ--HRVKELELKHEQQQKILKIKTEEIAA----FQRKRRSGSNGSVVSLEQQQKIEE 951
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 952 QKKWLDQEMEKV---LQQRRALEELGEELHKREAILAKKEALMQEK--------------TGLESKRLRSSQALNEDIVR 1014
Cdd:pfam15921 515 TNAEITKLRSRVdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMQVEKAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1015 VSSRLEHLEKELSE-------KSGQLRQGSAQ--------------SQQQIRGeIDSLRQEKDSLLKQ----RLEIDGKL 1069
Cdd:pfam15921 595 LEKEINDRRLELQEfkilkdkKDAKIRELEARvsdlelekvklvnaGSERLRA-VKDIKQERDQLLNEvktsRNELNSLS 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1070 RQGSLL-------SPEEERTLFQLDEAIEALDAAIEYKNEAITCRQ----RVLRASASLLSQCEMN------LMAKLSYL 1132
Cdd:pfam15921 674 EDYEVLkrnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQITAKrgqidaLQSKIQFL 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1133 SSSETRALLCKYFdkvvtLREEQHQQQIAFS-----------ELEMQLEEQQRL---VYWLEVALERQRLEMDRQLTLQQ 1198
Cdd:pfam15921 754 EEAMTNANKEKHF-----LKEEKNKLSQELStvateknkmagELEVLRSQERRLkekVANMEVALDKASLQFAECQDIIQ 828
|
570
....*....|....*.
gi 767984051 1199 KEHEQNMQLLLQQSRD 1214
Cdd:pfam15921 829 RQEQESVRLKLQHTLD 844
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
726-1269 |
2.12e-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: 55.75 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 726 KARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQA-----------LNRQHSQRIReLEQEAE 794
Cdd:TIGR00618 284 ERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqqssieeqrrlLQTLHSQEIH-IRDAHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 795 Q---VRAELSEG----------QRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKR 861
Cdd:TIGR00618 363 VatsIREISCQQhtltqhihtlQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 862 LQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE---MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNG 938
Cdd:TIGR00618 443 CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkeqIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 939 SVVSLEQQQKIEEQKKWLDQEMEKVLQQrraleelGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 1018
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1019 LEHLEKELSEKSGQLRQgsAQSQQQIRGEIDSLRQEKDSLLKQrleIDGKLRQGSLLSPEEERTLFQLDEAIEALdAAIE 1098
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLAC--EQHALLRKLQPEQDLQDVRLHLQQ---CSQELALKLTALHALQLTLTQERVREHAL-SIRV 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1099 YKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQLEEQQRL 1175
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSDLAAREDA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1176 VYWLEVALERQRLEMDRQLTL--QQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRymwINQELKQKLG 1253
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKARTEahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE---IGQEIPSDED 817
|
570
....*....|....*.
gi 767984051 1254 GVNAVGHSRGGEKRSL 1269
Cdd:TIGR00618 818 ILNLQCETLVQEEEQF 833
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
726-992 |
2.16e-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: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 726 KARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAEQVRA--ELS 801
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMREleRLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 802 EGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQR 881
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 882 RLREETEQKRRlEAEMSKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQ 952
Cdd:pfam17380 465 LRQQEEERKRK-KLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEE 540
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767984051 953 KKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQ 992
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
763-1102 |
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 767984051 763 ELIGELVRTGKAAQALN-RQHSQRIRELEQEaeQVRAELSEgqrQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVL 841
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSeRQQQEKFEKMEQE--RLRQEKEE---KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 842 KEKKQATERLvslsaQSEKRLQELERnvqlmrqQQGQLQRRLREETEQKRRLEAEMSKRQHRVK-ELE-------LKHEQ 913
Cdd:pfam17380 344 MERERELERI-----RQEERKRELER-------IRQEEIAMEISRMRELERLQMERQQKNERVRqELEaarkvkiLEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 914 QQKI--LKIKTEEIAAFQRKRRSgsngsvvslEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAILAKKEALM 991
Cdd:pfam17380 412 QRKIqqQKVEMEQIRAEQEEARQ---------REVRRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 992 Q-----EKTGLESKRLRSSQALNED---IVRVSSRLEHLEKELSEksgqlRQGSAQSQQQIRGEIDSLRQEKDslLKQRL 1063
Cdd:pfam17380 480 EkekrdRKRAEEQRRKILEKELEERkqaMIEEERKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQE--MEERR 552
|
330 340 350
....*....|....*....|....*....|....*....
gi 767984051 1064 EIDGKLRQGSllspEEERTLFQLDEAIEALDAAIEYKNE 1102
Cdd:pfam17380 553 RIQEQMRKAT----EERSRLEAMEREREMMRQIVESEKA 587
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
743-1232 |
5.08e-07 |
|
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: 54.44 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAEQVR--AELSEGQRQ--LRELEGKELQDA 818
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKtnGLLHTEDREeeIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 819 GERSRLQEFRRRVAAAQSQVQVLKEK-----------KQATERLV-SLSAQsEKRLQELERNVQLMRQQQGQLQRRLREE 886
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKletltnqnsdcKQHIEVLKeSLTAK-EQRAAILQTEVDALRLRLEEKESFLNKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 887 TEQKRRLEAEMSKRQHRVKELelkheqqQKILKIKTEEIAAFQRKrrsgsngsVVSLEQQQKieEQKKWLDQEMEKV--L 964
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDL-------KDMLDVKERKINVLQKK--------IENLQEQLR--DKDKQLAGLKERVksL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 965 QQRR-----ALEELGEELHKREAILakkEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLR--QGS 1037
Cdd:pfam10174 428 QTDSsntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEH 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1038 AQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLrQGSLL----SPEEERTLFQLDEAIEALDAAIE-YKNEAITCRQRVLR 1112
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKL-ENQLKkahnAEEAVRTNPEINDRIRLLEQEVArYKEESGKAQAEVER 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1113 ASAsLLSQCEMNLMAKLSYLSSSETRALLcKYFDKVVTLREEQHQQQIAFSELEMQLEE------------QQRLVYWLE 1180
Cdd:pfam10174 584 LLG-ILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEarrrednladnsQQLQLEELM 661
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 767984051 1181 VALERQRLEMDrqltlQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQ 1232
Cdd:pfam10174 662 GALEKTRQELD-----ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILE 708
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
780-1240 |
5.09e-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: 54.46 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 780 RQHSQRIRELEQEAEQVRAELSEGQRQLRElEGKELQDAgERSRLQEFRRRVAAAQSQVQVLKEKKQATERlvslsAQSE 859
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDD-QWKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLD-----ADIE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 860 KRLQELERNVQLMRQQQGQLQRRLREETEQkRRLEAEMSKRQHRVKE-----LELKHEQQQKI----LKIKTEEIAAFQR 930
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKH-QDVTAKYNRRRSKIKEqnnrdIAGIKDKLAKIrearDRQLAVAEDDLQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 931 KR---RSGSNGSVVSLEQQQK-----IEEQKKWLDQ---EMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLES 999
Cdd:pfam12128 420 LEselREQLEAGKLEFNEEEYrlksrLGELKLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1000 KRLRSSQALNEDIVRVS---SRLEHLEKELSEKSGQLRqgsAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSlls 1076
Cdd:pfam12128 500 RRDQASEALRQASRRLEerqSALDELELQLFPQAGTLL---HFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGS--- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1077 PEEERTLFQLDEAIEALDAAiEYKNEAITCRQRVLRASASLLSQCEMN---------LMAKLSYLSSSETRALlCKYFDK 1147
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVP-EWAASEEELRERLDKAEEALQSAREKQaaaeeqlvqANGELEKASREETFAR-TALKNA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1148 VVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQR--LEMDRQLTLQQ-----KEHEQNMQLLLQQ-------SR 1213
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLkqLDKKHQAWLEEqkeqkREARTEKQAYWQVvegaldaQL 731
|
490 500
....*....|....*....|....*..
gi 767984051 1214 DHLGEGLADSRRQYEARIQALEKELGR 1240
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKR 758
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
737-1238 |
5.52e-07 |
|
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: 53.98 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 737 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAEQVRAELSEGQRQL------ 807
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknelse 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 808 --RELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLrE 885
Cdd:pfam05557 116 lrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK-S 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 886 ETEQKRRLEAEMSKRQHRVKELelkHEQQQKILKIKtEEIAAFQRK--RRSGSNGSVVSLE-----QQQKIEEQKKwLDQ 958
Cdd:pfam05557 195 ELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRKleREEKYREEAATLElekekLEQELQSWVK-LAQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 959 EMEKVLQQRRALEELGEELHKREAilakkeALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKSGQLRQ 1035
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREI------VLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1036 gsaqSQQQIRgeidSLRQEKDsLLKQRLEidgklRQGSLLSPEEerTLFQLDEAI-EALDAAIEYKNEAITCRQRV---L 1111
Cdd:pfam05557 344 ----LQRRVL----LLTKERD-GYRAILE-----SYDKELTMSN--YSPQLLERIeEAEDMTQKMQAHNEEMEAQLsvaE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1112 RASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQRLEMD 1191
Cdd:pfam05557 408 EELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERRCLQGD 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 767984051 1192 RQLTLQQK-EHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKEL 1238
Cdd:pfam05557 480 YDPKKTKVlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-1242 |
5.87e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 778 LNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLsaq 857
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 858 sEKRLQELERNVQLMRQQqgqlqrrlreETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQrkrrsgsn 937
Cdd:COG4717 145 -PERLEELEERLEELREL----------EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ-------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 938 gsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGL----ESKRLRSSQALNEDIV 1013
Cdd:COG4717 206 ------QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1014 RVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKlrqgslLSPEEERTLFQLDEAIEAL 1093
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPD------LSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1094 DAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEmqLEEQQ 1173
Cdd:COG4717 353 LREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEELEELEEQLEELL--GELEE 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 1174 RLVYWLEVALERQRLEMDRQLTLQQKEHEQNM-------QLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYM 1242
Cdd:COG4717 421 LLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
784-1252 |
1.30e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 784 QRIRELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFRRRVAAAQSQVQVLKEKKQATERLvslsaqsEKRLQ 863
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEI----------SSELPELREELEKLEKEVKELEELKEEIEEL-------EKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 864 ELERNvqlmrqqqgqlqrrlreeteqKRRLEAEMSKRQHRVKELELKHEQQQKILKiKTEEIAAFQRKRRSGSngsvvsl 943
Cdd:PRK03918 249 SLEGS---------------------KRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLS------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 944 EQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREailAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEH 1021
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1022 LEKELSEKsgqlrqgsaqSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKN 1101
Cdd:PRK03918 377 LKKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KG 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1102 EAITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEV 1181
Cdd:PRK03918 437 KCPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKEL 501
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984051 1182 ALERQRLEmdrqltlqQKEHEQNMQLLLQQSRDHlgEGLADSRRQYEARIQALEKELGRYmwinQELKQKL 1252
Cdd:PRK03918 502 AEQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKL----EELKKKL 558
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
757-1084 |
1.90e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 757 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELegkelqdageRSRLQEFRRRVAAAQS 836
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 837 QVQVLKEKKQAT-ERLVSLSAQSEKRLQELernvqlmrqqqgqlqrrlrEETEQKRRLEAEMSKrqhRVKELELKheQQQ 915
Cdd:COG1340 72 KVKELKEERDELnEKLNELREELDELRKEL-------------------AELNKAGGSIDKLRK---EIERLEWR--QQT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 916 KILKIKtEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK-REAILAKKEALMQEK 994
Cdd:COG1340 128 EVLSPE-EEKELVEKIKELEK-----ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 995 TGLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRL-EIDGKLRQGS 1073
Cdd:COG1340 202 KEADELR-KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAeEIFEKLKKGE 280
|
330
....*....|.
gi 767984051 1074 LLSPEEERTLF 1084
Cdd:COG1340 281 KLTTEELKLLQ 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
752-1189 |
2.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 752 RELAINIRMKEELIGELvRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERSRLQEFRRRV 831
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 832 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLEAEMSKRQHRVKELELK 910
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 911 HEQQQKILKIKTEEIAAFQRKRR-------SGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQ---------QRRALEELG 974
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERlkearllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfllLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 975 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIR--------- 1045
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1046 GEIDSLR------QEKDSLLKQRLEIDGKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAIT-CRQRVLRASAs 1116
Cdd:COG4717 382 EDEEELRaaleqaEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEeLREELAELEA- 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 1117 llsqcemnlmaKLSYLSSSETrallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVY---WLEVALERQRLE 1189
Cdd:COG4717 461 -----------ELEQLEEDGE-------------LAELLQELEELKAELRELAEEWAALKLaleLLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
885-1259 |
3.40e-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: 51.98 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 885 EETEQK--------RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSLEQqqKIEEQKKWL 956
Cdd:TIGR02168 175 KETERKlertrenlDRLEDILNELERQLKSLERQAEKAERYKELKAEL----RELELALLVLRLEELRE--ELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 957 DQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKSGQLRQ 1035
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISrLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1036 GSAQSQQQIRgEIDSLRQEKDSLLKQRLEIDGKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNeaitcrqrvlrasa 1115
Cdd:TIGR02168 328 LESKLDELAE-ELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLR-------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1116 sllsqcemnlmaklsylsssetrallckyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywlevalERQRLEmDRQLT 1195
Cdd:TIGR02168 386 ------------------------------SKVAQLELQIASLNNEIERLEARLERLED---------RRERLQ-QEIEE 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984051 1196 LQQKEHEQNMQLLlQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKLGGVNAVG 1259
Cdd:TIGR02168 426 LLKKLEEAELKEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
741-1202 |
5.67e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 741 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGE 820
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 821 RSRLQEFRRRVAAAQSQvQVLKEKKQATERLVSLSA---QSEKRLQELERNVQL-------MRQQQGQLQRRLREETEQK 890
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLE-ELREERDELREREAELEAtlrTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 891 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsVVSLEQQQKIEEQKkwLDQEMEKVLQQRRAL 970
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDR----------------IERLEERREDLEEL--IAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 971 EELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK--ELSEKSGQLRQ--GSAQSQQQIRG 1046
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDeiERLREKREALA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1047 EIDSLRQEKDSLLKQRL-EIDGKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCE--- 1122
Cdd:PRK02224 620 ELNDERRERLAEKRERKrELEAEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelr 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1123 ---MNLMAKLSYLSS--SETRALLCKYFDkvvtLREEQHQQQIafSELEMQLEEQQRLVYWLEvALERQRLEMDRQLTLQ 1197
Cdd:PRK02224 698 errEALENRVEALEAlyDEAEELESMYGD----LRAELRQRNV--ETLERMLNETFDLVYQND-AYSHIELDGEYELTVY 770
|
....*
gi 767984051 1198 QKEHE 1202
Cdd:PRK02224 771 QKDGE 775
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
737-1120 |
6.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 737 ATASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQ 816
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 817 DAGERSRLQEFRRRVAAAQSQVQVLKEK---------KQATERLVSLS---AQSEKRLQELERNVQLMRQQQGQLQRRLR 884
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQlslateeelQDLAEELEELQqrlAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 885 EETEQKRRLEAEMSKR--------------------------------------QHRVKELELKHEQQQKILKIKTEEIA 926
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 927 AFQRKRRSGSNGsvvsLEQQQKIEEQKKWLDQeMEKVLQQRRALEELGEELhKREAILAKKEALMQEKTGLESKRLRSSQ 1006
Cdd:COG4717 318 EEELEELLAALG----LPPDLSPEELLELLDR-IEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1007 ALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQ--------QQIRGEIDSLRQEKDSLLKQRLEIDGKLRQgsllsPE 1078
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREELAELEAELEQ-----LE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767984051 1079 EERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1120
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
761-1103 |
7.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 761 KEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAelSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQsqvqv 840
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK----- 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 841 lkeKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAemskrQHRVKELELKHEQQQKILKI 920
Cdd:PTZ00121 1177 ---KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEE 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 921 KT-EEIAAFQRKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELHKREAILAKKEAlMQEKTGLES 999
Cdd:PTZ00121 1249 RNnEEIRKFEEARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1000 KRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQiRGEIDSLRQE----KDSLLKQRLEIDGKLRQGSLL 1075
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKK 1399
|
330 340
....*....|....*....|....*...
gi 767984051 1076 SPEEERTLFQLDEAIEALDAAIEYKNEA 1103
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
780-1238 |
1.10e-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: 50.05 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 780 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAG---ERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSA 856
Cdd:TIGR00606 594 AKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLT 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 857 --------------QSEKRLQELERNVQLMRQQQgqlqrrlreETEQKRrLEAEMSKRQHRVKELELKHEQQQKILKIKT 922
Cdd:TIGR00606 674 denqsccpvcqrvfQTEAELQEFISDLQSKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 923 EEIAAFQRKRRSGSNGSVvslEQQQKIEEQKKWL-----DQEMEKVLQQR-RALEELGEELHKREAILAKKEALMQEKTG 996
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQ---RLKNDIEEQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 997 leskrLRSSQALNEdivRVSSRLEHLEKELSEksGQLRQGSAQSQQQirgEIDSLRQEKDSLLKQRLEIDGKLRQGSLLS 1076
Cdd:TIGR00606 821 -----DRTVQQVNQ---EKQEKQHELDTVVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1077 PEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTL 1151
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDG 967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1152 REEQ-HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQ----------LTLQQKEHEqnMQLLLQQSRDHLGEGL 1220
Cdd:TIGR00606 968 KDDYlKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQkiqerwlqdnLTLRKRENE--LKEVEEELKQHLKEMG 1045
|
490
....*....|....*...
gi 767984051 1221 ADSRRQYEARIQALEKEL 1238
Cdd:TIGR00606 1046 QMQVLQMKQEHQKLEENI 1063
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
701-980 |
1.13e-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: 50.06 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 701 ERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNR 780
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 781 QHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERS-----RLQEFRRRVAAAQSQVQVL----KEKKQATERL 851
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNERasleeALALLRSELEELSEELRELeskrSELRRELEEL 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 852 VSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK-RRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFqr 930
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLE--------------NKIKEL-- 984
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767984051 931 krrsgsnGSV--VSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKR 980
Cdd:TIGR02168 985 -------GPVnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
734-1065 |
1.22e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 734 VPPATASEWRLAQAQQKIRELainIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEG- 812
Cdd:pfam07888 26 VPRAELLQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 813 -KELQDAGERsrlqefrrrvaaaqsqvqvLKEKKQAterLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKR 891
Cdd:pfam07888 103 yKELSASSEE-------------------LSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 892 RLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 971
Cdd:pfam07888 161 KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 972 ELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKSGQLRQGSAQSQQQIRGEID 1049
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQ 311
|
330
....*....|....*.
gi 767984051 1050 SLRQEKDSLLKQRLEI 1065
Cdd:pfam07888 312 SAEADKDRIEKLSAEL 327
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
737-1105 |
1.33e-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: 49.97 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 737 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAEQVRAELSEG-QRQLREL 810
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlTRRMQRG 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 811 E--GKELQDAGE--RSRLQEFRRRVAAAQSQVQVLKEKKQA-TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLRE 885
Cdd:TIGR00618 534 EqtYAQLETSEEdvYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 886 ETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQKIEEQK 953
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQSEKEQLT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 954 KWLD----------QEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQALNEDIVRVSSR---- 1018
Cdd:TIGR00618 694 YWKEmlaqcqtllrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKeLMHQARTVLKARTEAHFNNNEEvtaa 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1019 ------LEHLE-------KELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQ 1085
Cdd:TIGR00618 774 lqtgaeLSHLAaeiqffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
410 420
....*....|....*....|
gi 767984051 1086 LDEAIEALDAAIEYKNEAIT 1105
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQ 873
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
780-1062 |
1.51e-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: 49.57 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 780 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAGERSRLQEFRRRVAAAQSQVQVLKEkkqaterlvslsaqSE 859
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAEAEQELEESKRE--------------TE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 860 KRLQELERNVQLMRQQQGQLQRRLREETEQ------KRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 933
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 934 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK--REAILAKKEALMQEKTGLESKRLRSSQALNED 1011
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKvmREADEESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767984051 1012 IVRVSSRL----EHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQR 1062
Cdd:COG5185 487 LTQIESRVstlkATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
890-1238 |
2.29e-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: 49.30 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 890 KRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQRR 968
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrELSSLQSELRRIENRLDELSQELSDA-----------SRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 969 ALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEksgqlrqgsaQSQQQIRGEI 1048
Cdd:TIGR02169 738 RLEELEEDL---SSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDLEARLSH----------SRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1049 DSLRQEKDSLLKQRLEIDGKLRQgslLSPEEErtlfQLDEAIEALDAAIEYKNEAITCRQRVLRasasllsqcemNLMAK 1128
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNR---LTLEKE----YLEKEIQELQEQRIDLKEQIKSIEKEIE-----------NLNGK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1129 LsylssSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1208
Cdd:TIGR02169 863 K-----EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
330 340 350
....*....|....*....|....*....|
gi 767984051 1209 LQQSRDHLGEGLADSRRQYEARIQALEKEL 1238
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
768-900 |
3.80e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 768 LVRTGKAAQALNRQHSQ----------RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQ 837
Cdd:PRK09510 54 MVDPGAVVEQYNRQQQQqksakraeeqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984051 838 VQvlKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 900
Cdd:PRK09510 134 AE--EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
781-1117 |
4.73e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 781 QHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSR---LQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSA 856
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 857 QSE----------KRLQELERNVQLMRQQQGQLQRrlreetEQKRRLEAEMSKrqhrvkeLELKHEQQQKILKIKTEEIA 926
Cdd:PRK11281 157 QPEraqaalyansQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 927 AFQrKRRSGSNgsvvslEQQQKIEEQKkwldQEMEKVLQQRRAleELGEElHKREAILAKKEALMQE----KTGLE---- 998
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQL----QLLQEAINSKRL--TLSEK-TVQEAQSQDEAARIQAnplvAQELEinlq 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 999 -SKRL-RSSQALNE---DIVRVSSRLEHL---EKELSEKSGQLrQGS------AQSQQQ-----------------IRGE 1047
Cdd:PRK11281 290 lSQRLlKATEKLNTltqQNLRVKNWLDRLtqsERNIKEQISVL-KGSlllsriLYQQQQalpsadliegladriadLRLE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1048 IDSLRQEKDSLLKQRLEIDgKL--RQGSLLSPEEERTLFQ--------LDEAIEALDAAIeykNEAITC---RQRVLRAS 1114
Cdd:PRK11281 369 QFEINQQRDALFQPDAYID-KLeaGHKSEVTDEVRDALLQllderrelLDQLNKQLNNQL---NLAINLqlnQQQLLSVS 444
|
...
gi 767984051 1115 ASL 1117
Cdd:PRK11281 445 DSL 447
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
761-1065 |
6.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 761 KEELIGELVRTGKAAQALNRQHS---QRIRELEQEAEQVRAELSEgqrqLRELEGK------ELQDAGERSRLQEFRRRV 831
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEE----LKKAKGKcpvcgrELTEEHRKELLEEYTAEL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 832 AAAQSQVQVLKEK-KQATERLVS----LSAQSE--------KRLQELERNVQLMRQQQGQLQRRLREETEQK-RRLEAEM 897
Cdd:PRK03918 462 KRIEKELKEIEEKeRKLRKELRElekvLKKESEliklkelaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKlIKLKGEI 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 898 S---KRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQ-QKIEE-QKKWL---DQEMEKVLQQRRa 969
Cdd:PRK03918 542 KslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPfYNEYLelkDAEKELEREEKE- 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 970 LEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQalnEDIVRVSSRLEHLEKELSEKSGQLrQGSAQSQQQIRGEI 1048
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKeLEELEKKYSE---EEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTL 696
|
330
....*....|....*..
gi 767984051 1049 DSLRQEKDSLLKQRLEI 1065
Cdd:PRK03918 697 EKLKEELEEREKAKKEL 713
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
743-869 |
7.12e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALnrqhsQRIRELEQEAEQVRAELSEG-------QRQLRELEgKEL 815
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLR-----AQLAELEAELAELSARYTPNhpdvialRAQIAALR-AQL 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767984051 816 QDAGERSrLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 869
Cdd:COG3206 308 QQEAQRI-LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
784-972 |
7.79e-05 |
|
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: 45.69 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 784 QRIRELEQEAEQVRAELSEGQRQLRELEgKELQDAgeRSRLQEFRRRVAAAQSQVQVLKEK-KQATERLvsLSAQSEKRL 862
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALE-ARLEAA--KTELEDLEKEIKRLELEIEEVEARiKKYEEQL--GNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 863 QELERnvqlmrqqqgqlqrrlrEETEQKRRLeaemSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 942
Cdd:COG1579 92 EALQK-----------------EIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|
gi 767984051 943 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE 972
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAA 170
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
785-1236 |
8.10e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 785 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQ-----------EFRRRVAAAQSQVQVL-KEKKQATERLV 852
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 853 SLSAQ------SEKRLQELeRNVQLMRQQQGQLQRRLREETEQ-----KRRLEAEMSKRQHRVKELELKHEQQQKILKIK 921
Cdd:pfam01576 163 EFTSNlaeeeeKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 922 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE----ELGEELH------------------- 978
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEkqrrDLGEELEalkteledtldttaaqqel 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 979 --KREAILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKSgqlRQGSAQSQQQIRGEID 1049
Cdd:pfam01576 322 rsKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1050 SLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKL 1129
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1130 SYLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNMQLL- 1208
Cdd:pfam01576 475 ELL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLe 541
|
490 500
....*....|....*....|....*....
gi 767984051 1209 -LQQSRDHLGEGLADSRRQYEARIQALEK 1236
Cdd:pfam01576 542 aLEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
885-1103 |
8.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 885 EETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEkvl 964
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 965 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALN-------EDIVRVSSRLEHLEKELSEKSGQLRQGS 1037
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparreqaEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 1038 AQSQQQiRGEIDSLRQEKDSLLKQrLEIDGKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEA 1103
Cdd:COG4942 181 AELEEE-RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAE--ELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
743-1028 |
8.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQAL---------NRQHSQRIRELEQEaeqvRAELSEGQRQLRELEgK 813
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAE----LERLDASSDDLAALE-E 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 814 ELQDAgeRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 893
Cdd:COG4913 693 QLEEL--EAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 894 EAEMSKRQHRVKelELKHEQQQKILKIkteeIAAFQRKRRSGSNGSVVSLEqqqkieeqkkwldqEMEKVLQQRRALEEL 973
Cdd:COG4913 768 RENLEERIDALR--ARLNRAEEELERA----MRAFNREWPAETADLDADLE--------------SLPEYLALLDRLEED 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767984051 974 GEELHKREAILAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 1028
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1004-1238 |
9.44e-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: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1004 SSQALNEDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRqgsllspEEERTL 1083
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1084 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1162
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984051 1163 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNMQLLLQQSRDHLGE--GLADSRRQYEARIQALEKEL 1238
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
958-1098 |
9.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 958 QEMEKVLQQRRALE---ELGEELHKREAILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 1022
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 1023 EKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1098
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
823-1071 |
1.23e-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: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslsAQSEKRLQELERnvQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 902
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELAERY----AAARERLAELEY--LRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 903 RVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHkrea 982
Cdd:COG4913 310 ELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLEALLAALG---- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 983 ilakkEALMQEKTGLESKRLRSSQALNEdivrVSSRLEHLEKELSEKSGQLRQGsaqsqqqiRGEIDSLRQEKDSLLKQR 1062
Cdd:COG4913 373 -----LPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDL--------RRELRELEAEIASLERRK 435
|
....*....
gi 767984051 1063 LEIDGKLRQ 1071
Cdd:COG4913 436 SNIPARLLA 444
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
835-1103 |
1.33e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 835 QSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 914
Cdd:COG1340 7 SSSLEELEEKI---EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 915 QKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQEMEKVLQQRraLEELGEELHKREAILAKKEA 989
Cdd:COG1340 84 NEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPEEEKELVEK--IKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 990 LMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKSGQLRqgsaQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKL 1069
Cdd:COG1340 162 LKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----EEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270
....*....|....*....|....*....|....
gi 767984051 1070 RQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1103
Cdd:COG1340 226 DE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
790-1202 |
1.55e-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: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 790 EQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEfrrrvaAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 869
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 870 qlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 949
Cdd:pfam01576 85 --------------EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 950 EEQKKWLDQEMEKVLQQRRALEELGEEL----HKREAI-------LAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 1018
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLsklkNKHEAMisdleerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1019 LEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDsLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1098
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1099 YKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFSELEMQLEEQQRLVYW 1178
Cdd:pfam01576 310 DTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALEELTEQLEQAKRNKAN 374
|
410 420
....*....|....*....|....*...
gi 767984051 1179 LE---VALERQRLEMDRQL-TLQQKEHE 1202
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 ... |
844-1194 |
1.72e-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: 46.12 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 844 KKQATERLVSLSAQSEKRLQELERNVQL--MRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIK 921
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 922 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKR 1001
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE--ELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1002 LRSS------QALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRgEIDSLRQEKDSLLKQRLEIDGKLRQGSLL 1075
Cdd:pfam02463 307 RRKVddeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE-EEEELEKLQEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1076 SPEEERTLFQLDEAIEALDAAIEYKNEAitcRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQ 1155
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLEL---ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 767984051 1156 HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL 1194
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
826-1171 |
2.84e-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: 45.44 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 826 EFRRRVAAAqsqvqvLKEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrRLREETE-------QKRRLEAEMS 898
Cdd:TIGR02169 167 EFDRKKEKA------LEELEEVEENIERLDLIIDEKRQQLER--------------LRREREKaeryqalLKEKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 899 KRQHRVKELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVSLEQQQKiEEQKKWLDQEMEKVLQQRRALEELGEELH 978
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTE-EISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 979 KREAILAKKEALMQEktgLESKRlrssQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQ----------SQQQIRGEI 1048
Cdd:TIGR02169 305 SLERSIAEKERELED---AEERL----AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1049 DSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEER---TLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNL 1125
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 767984051 1126 MaklsylsssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1171
Cdd:TIGR02169 458 E---------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
886-1028 |
3.22e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 886 ETEQKRRLEAEMSKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 964
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984051 965 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 1028
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
726-918 |
3.24e-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: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 726 KARVQARQVPPATASEW---RLAQAQQKIRELAINI---RMKEELIgelvrtgkAAQALNRQHSQRIRELEQEAEQVRAE 799
Cdd:COG3206 163 EQNLELRREEARKALEFleeQLPELRKELEEAEAALeefRQKNGLV--------DLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 800 LSEGQRQLRELEGK------ELQDAGERSRLQEFRRRVAAAQSQVQVLKEK--------KQATERLVSLSAQSEKRLQEL 865
Cdd:COG3206 235 LAEAEARLAALRAQlgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767984051 866 ERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKIL 918
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
825-1070 |
3.91e-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: 45.21 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 825 QEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 903
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 904 VKELELKHEQQQKILKIKTEeiAAFQRKRRSGSNGSVVSLEQQQKIEEQKK----WLDQEMEKVLQQRRA---------- 969
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQ--AWLEEQKEQKREARTEKQAYWQVVEGALDaqlaLLKAAIAARRSGAKAelkaletwyk 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 970 --LEELG---EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV----RVSSRLEHLEKELSEKSGQLrqgsAQS 1040
Cdd:pfam12128 758 rdLASLGvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQL----ARL 833
|
250 260 270
....*....|....*....|....*....|
gi 767984051 1041 QQQIRGEIDSLRQEKDSLLKQRLEIDGKLR 1070
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
743-1092 |
3.97e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELsEGQRQLRELEGKELQDAGErs 822
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRRDLGE-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 rlqefrrrvaaaqsQVQVLKEKKQATerLVSLSAQSEKRLQElernvqlmrqqqgqlqrrLREETEQKRRLEAEMSKRQH 902
Cdd:pfam01576 300 --------------ELEALKTELEDT--LDTTAAQQELRSKR------------------EQEVTELKKALEEETRSHEA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 903 RVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKVLQQRRALEElgeelHKRE 981
Cdd:pfam01576 346 QLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RTLQQAKQDSE-----HKRK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 982 ailaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQ-----GSAQSQQQirgEIDSLRQEKD 1056
Cdd:pfam01576 409 ----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvSSLESQLQ---DTQELLQEET 481
|
330 340 350
....*....|....*....|....*....|....*...
gi 767984051 1057 sllKQRLEIDGKLRQgsllsPEEERT--LFQLDEAIEA 1092
Cdd:pfam01576 482 ---RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
975-1238 |
5.58e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 975 EELHKREAILAKKEALMQEKTGLeSKRLRSSQALNEDIVRVSSRLEHLEKELseksgqlrQGSAQSQQQIRGEIDSLRQE 1054
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1055 KDSLLKQRLEiDGKLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSS 1134
Cdd:PRK11281 110 NDEETRETLS-TLSLRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1135 SETRAllckyfdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQL--LLQQS 1212
Cdd:PRK11281 168 NSQRL------------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQ 228
|
250 260
....*....|....*....|....*.
gi 767984051 1213 RDHLgegladsrrqyEARIQALEKEL 1238
Cdd:PRK11281 229 RDYL-----------TARIQRLEHQL 243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
785-975 |
7.43e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 785 RIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQ 863
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 864 ELERNVQLMRQQQGQLQRRLREET-----EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsng 938
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK------ 710
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767984051 939 svvslEQQQKIEEQKKWLDQEMEKV-----LQQRRALEELGE 975
Cdd:PRK03918 711 -----KELEKLEKALERVEELREKVkkykaLLKERALSKVGE 747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
735-1001 |
7.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 735 PPATASEWRLAQAQ----QKIRELAINIRMKEELIGELVRTGKAAQALnrqhSQRIRELEQEAEQVRAElsEGQRQLREL 810
Cdd:COG4913 220 EPDTFEAADALVEHfddlERAHEALEDAREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLW--FAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 811 EGKELQDAGERSRLQEfrrRVAAAQSQVQVLKEKKQATERlvSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreeteQK 890
Cdd:COG4913 294 EAELEELRAELARLEA---ELERLEARLDALREELDELEA--QIRGNGGDRLEQLER---------------------EI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 891 RRLEAEMSKRQHRVKELelkhEQQQKILKIKT-EEIAAFQRKRRsgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRA 969
Cdd:COG4913 348 ERLERELEERERRRARL----EALLAALGLPLpASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRD 416
|
250 260 270
....*....|....*....|....*....|..
gi 767984051 970 LEElgeelhkreailaKKEALMQEKTGLESKR 1001
Cdd:COG4913 417 LRR-------------ELRELEAEIASLERRK 435
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
743-1247 |
9.89e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEgKELQdagers 822
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE-EDLQ------ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 rlqefrrrvAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 902
Cdd:pfam05483 321 ---------IATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 903 RVKEL-ELKHEQQQKILKIKT----EEIAAFQRKrrsgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRaleelgEEL 977
Cdd:pfam05483 392 ELEEMtKFKNNKEVELEELKKilaeDEKLLDEKK-------------QFEKIAEELKGKEQELIFLLQARE------KEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 978 HKRE----AILAKKEALMQE----KTGLESKRLRSSQAL---------NEDIVRVSSRL-----EHLEKELSEKSGQLR- 1034
Cdd:pfam05483 453 HDLEiqltAIKTSEEHYLKEvedlKTELEKEKLKNIELTahcdkllleNKELTQEASDMtlelkKHQEDIINCKKQEERm 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1035 ----QGSAQSQQQIRGEIDSLRQEkdsLLKQRLEIDGKL-------RQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1103
Cdd:pfam05483 533 lkqiENLEEKEMNLRDELESVREE---FIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1104 ITCRQRVLRAsasllsqcemnlmakLSYLSSSETRALLCkYFDKVVTLREEQHQQQIAFSEL----EMQLEEQQRLVYWL 1179
Cdd:pfam05483 610 IEELHQENKA---------------LKKKGSAENKQLNA-YEIKVNKLELELASAKQKFEEIidnyQKEIEDKKISEEKL 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984051 1180 EVALERQRLEMDRQLTLQQKeheqnMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQE 1247
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
943-1237 |
1.43e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 943 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILakkealmqEKTGLESKRLRS-----SQALNEDIVR--- 1014
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL--------EAAEEEVDSLKSqladyQQALDVQQTRaiq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1015 ---VSSRLEHLEK-----ELSEKSGQLRQGSAQSQQQirgEIDSLRQEkdslLKQRLEIDGKLRQgsllspeeertlfQL 1086
Cdd:COG3096 415 yqqAVQALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1087 DEAIEAL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT-- 1150
Cdd:COG3096 475 EKAYELVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaa 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1151 --LREEQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NMQLLLQQSRDHLGEGLA 1221
Cdd:COG3096 553 eeLEELLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALA 623
|
330
....*....|....*.
gi 767984051 1222 DSRRQYEARIQALEKE 1237
Cdd:COG3096 624 DSQEVTAAMQQLLERE 639
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
739-992 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 739 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDA 818
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 819 GERSRLqefrrrVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE----QKRRLE 894
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 895 AEMSKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 967
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 767984051 968 RALEELGEELHKREAILAKKEALMQ 992
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
776-1061 |
2.28e-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: 42.50 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 776 QALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAA----QSQVQVLK-EKKQATER 850
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSglkkDSKLKSLEiAVEQKKEE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 851 LVSLSAQSEK----------------RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 914
Cdd:pfam10174 533 CSKLENQLKKahnaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 915 QKILKIKTEEIAAFQRKRRSGSngsvvsleqQQKIEEQKKWLDQEMEKVLQQR-----RALEELGEELHKREAILAKKEA 989
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKG---------AQLLEEARRREDNLADNSQQLQleelmGALEKTRQELDATKARLSSTQQ 683
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984051 990 LMQEKTG-LESKRLRSSQALNEdivRVSSRLEHLEKELSEKSGQ--LRQGSAQSQQQIRGEIDSLRQEKDSLLKQ 1061
Cdd:pfam10174 684 SLAEKDGhLTNLRAERRKQLEE---ILEMKQEALLAAISEKDANiaLLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
745-1102 |
2.41e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 745 AQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAE--LSEGQRQLRELEGKELQDAGE-- 820
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagLDDADAEAVEARREELEDRDEel 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 821 RSRLQEFRRRVAAAQSQVQVLKEKkqaTERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 900
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLRED---ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 901 QHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSN-----------GSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRA 969
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleaGKCPECGQPVEGSPHVETIEEDRERVEELEAE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 970 LEELGEELHKREAILAKKEALMQEKTGLES---KRLRSSQALNEDIVRVSSRLEHLEkELSEKSGQLR---QGSAQSQQQ 1043
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLVEAEDRIERleeRREDLEELIAERRETIEEKRERAE-ELRERAAELEaeaEEKREAAAE 562
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767984051 1044 IRGEIDSLRQEKDSLLKQRLEIDGKLrqgsllspEEERTLFQLDEAIEALDAAIEYKNE 1102
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERI--------ESLERIRTLLAAIADAEDEIERLRE 613
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
783-1237 |
2.44e-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: 42.41 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 783 SQRIRELEQEAEQVRAELSEGQRQLRELEgkelqdagersrlqefrrrvAAAQSQVQVLKEKKQatERLVSLSAQSEKRL 862
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALK--------------------SESQNKIELLLQQHQ--DRIEQLISEHEVEI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 863 QELERNVQLMRQQQGQLQRRLREETEQKRRLEA----EMSKRQHRVKELELKHEQQQKILKIKTEEIaafqRKRRSGSNG 938
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEEL----EKQLVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 939 SVVSLE-QQQKIEEQKKWLDQEMEKVLQqrraleelgeELHKREailaKKEALMQEktglESKRLRSSQALNedivrvSS 1017
Cdd:pfam15921 357 ELTEARtERDQFSQESGNLDDQLQKLLA----------DLHKRE----KELSLEKE----QNKRLWDRDTGN------SI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1018 RLEHLEKELSEKSGQLRQGSA-----------QSQQQ---IRGEIDSLrqEKDSLLKQRLE--------IDGKLRQGSLL 1075
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEAllkamksecqgQMERQmaaIQGKNESL--EKVSSLTAQLEstkemlrkVVEELTAKKMT 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1076 SPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrVLRASASLLSQCEMNLMAKLSYLSSSETRA----LLCKYFDKVVtl 1151
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEIT----KLRSRVDLKLQELQHLKNEGDHLRNVQTECealkLQMAEKDKVI-- 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1152 reEQHQQQIafsELEMQLEEQQ-RLVYWLEValERQRLEM---DRQLTLQQKEheqnmqlLLQQSRDhlgeglaDSRRQY 1227
Cdd:pfam15921 565 --EILRQQI---ENMTQLVGQHgRTAGAMQV--EKAQLEKeinDRRLELQEFK-------ILKDKKD-------AKIREL 623
|
490
....*....|
gi 767984051 1228 EARIQALEKE 1237
Cdd:pfam15921 624 EARVSDLELE 633
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
789-1006 |
2.83e-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: 42.05 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 789 LEQEAEQVRAELSEGQRQLRElegkelqdagERSRLQ-EFRRRVAAAQSQVQVLKEKKQAT-ERLVSLSAQSEKRLQELE 866
Cdd:pfam07111 468 PPPPAPPVDADLSLELEQLRE----------ERNRLDaELQLSAHLIQQEVGRAREQGEAErQQLSEVAQQLEQELQRAQ 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 867 RNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH--------RVKELELKHEQQQKILKIKTEEIAAFQRKrrsgsng 938
Cdd:pfam07111 538 ESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEiygqalqeKVAEVETRLREQLSDTKRRLNEARREQAK------- 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984051 939 SVVSLEQQQKIEEQKKWLDQEMEKVlqQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQ 1006
Cdd:pfam07111 611 AVVSLRQIQHRATQEKERNQELRRL--QDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQ 676
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
743-1242 |
3.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAEQVRAELSEGQRQLRELEGKElqDAGERS 822
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 902
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 903 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 963
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 964 L---------------QQRRALEE--LGEELHKREAILAKKEALMQE------------KTGLESKRLRSSQALNEDIVR 1014
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPRldpdslagkldfKPHPFRAWLEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1015 VSS--RLEHLEKELSeKSGQLRQGSAQSQQQIRGEIDSLR------QEKDSLLKQRLEidgklrqgsllspEEERTLFQL 1086
Cdd:COG4913 564 VDSpeELRRHPRAIT-RAGQVKGNGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELA-------------ELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1087 DEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQI 1160
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1161 AFSELEMQLE-----------EQQRLVYWLEVALER-QRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYE 1228
Cdd:COG4913 700 ELEELEEELDelkgeigrlekELEQAEEELDELQDRlEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
570
....*....|....
gi 767984051 1229 ARIQALEKELGRYM 1242
Cdd:COG4913 780 ARLNRAEEELERAM 793
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
745-864 |
3.60e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 745 AQAQQKIRELAINIrmkEELIGELvrtgkaaQALNRQHSQRIRELE---QEAEQVRAELSEGQRQLRELEGKELQDAger 821
Cdd:PRK00409 505 EEAKKLIGEDKEKL---NELIASL-------EELERELEQKAEEAEallKEAEKLKEELEEKKEKLQEEEDKLLEEA--- 571
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767984051 822 srLQEFRRRVAAAQSQV-QVLKEKKQatERLVSLSAQSEKRLQE 864
Cdd:PRK00409 572 --EKEAQQAIKEAKKEAdEIIKELRQ--LQKGGYASVKAHELIE 611
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
823-1098 |
3.71e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 823 RLQEFRRRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------KRLQELErnvqlmrqqqgqlqRRLREETEQKRRLE 894
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 895 AEMSKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 971
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 972 ELGEElhkREAILAkkealmqeKTGLESKrlrssqalneDIVRVSSRLEHLEKELSEKSGQLRQgSAQSQQQIRGEIDSL 1051
Cdd:PRK02224 290 ELEEE---RDDLLA--------EAGLDDA----------DAEAVEARREELEDRDEELRDRLEE-CRVAAQAHNEEAESL 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767984051 1052 RQEKDSLlkqRLEIDGKLRQGSLLSPEEERTLFQLD---EAIEALDAAIE 1098
Cdd:PRK02224 348 REDADDL---EERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIE 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
743-1010 |
3.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKaaqalNRQHSQRIRELEQEAEQVRAE-LSEGQRQLRELEGKELQDAGER 821
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 822 SRLQEFRRRVAAAQSQVQVLKEKKQATE--------RLVSLSAQS----EKRLQELE---------RNVQLMRQQQGQLQ 880
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEeelaellkELEELGFESveelEERLKELEpfyneylelKDAEKELEREEKEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 881 RRLREETEQKRrleAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEM 960
Cdd:PRK03918 622 KKLEEELDKAF---EELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767984051 961 EKVLQQRRALEELGEELHKREAILAKKEALmQEKTgLESKRLRSSQALNE 1010
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEEL-REKV-KKYKALLKERALSK 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
734-939 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 734 VPPATASEWRLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAEQVRAELSEGQRQLREL 810
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 811 E---GKELQDAGERSR-------------LQEFRRRVAA----AQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQ 870
Cdd:COG3883 85 ReelGERARALYRSGGsvsyldvllgsesFSDFLDRLSAlskiADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984051 871 LMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGS 939
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
743-865 |
4.75e-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: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 743 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS 822
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767984051 823 RLQefrRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQEL 865
Cdd:COG4942 189 ALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
780-1064 |
4.80e-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: 40.82 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 780 RQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERS-------RLQEFRRRVAAAQSQVQVLKEK-KQA---- 847
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKsqnslqeKLAQEKSRVADAEEKILELQQKlEHAhkvc 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 848 -TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRL------REETEQKRR--------LEAEMSKRQHRVKELELKHE 912
Cdd:pfam15742 145 lTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRklldqnVNELQQQVRslqdkeaqLEMTNSQQQLRIQQQEAQLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 913 QQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELHKReailakKEALM 991
Cdd:pfam15742 225 QLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEKHH 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984051 992 QEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQsQQQIRGEIDSLRQEKDSLLKQRLE 1064
Cdd:pfam15742 281 HHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
831-963 |
5.09e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 831 VAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrLREETEQ-KRRLEAEMSKRQHRVKELE 908
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767984051 909 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV 963
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKK 623
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
751-1012 |
5.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 751 IRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQE---- 826
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEeles 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 827 -------FRRRVAAAQSQVQVLKEKKQATE----RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEA 895
Cdd:COG4372 106 lqeeaeeLQEELEELQKERQDLEQQRKQLEaqiaELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 896 EMSKRQHR---VKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEE 972
Cdd:COG4372 186 DELLKEANrnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767984051 973 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDI 1012
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
822-1241 |
5.98e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 822 SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQ 901
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 902 HRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKRE 981
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 982 AILAKKEALMQEKTGLESKR------LRSSQALNEDIVRVSSRLEHLEKELSEKSG----------QLRQGSAQSQQQIR 1045
Cdd:PRK01156 343 KKKSRYDDLNNQILELEGYEmdynsyLKSIESLKKKIEEYSKNIERMSAFISEILKiqeidpdaikKELNEINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1046 GEIDSLRQEKDSLLKQRLEIDgklRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNE---AITCRQRVLRASASLLSQCE 1122
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELS---RNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEkksRLEEKIREIEIEVKDIDEKI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1123 MNLMAKLSYLSSSET-------------RALLCKYFDKVVTLREEQHQQQIAFSELE-MQLEE-QQRLVYWLEVALERQR 1187
Cdd:PRK01156 500 VDLKKRKEYLESEEInksineynkiesaRADLEDIKIKINELKDKHDKYEEIKNRYKsLKLEDlDSKRTSWLNALAVISL 579
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 767984051 1188 LEMDrqlTLQQKEHEQNMQLLLQQSRDHLGE-GLADSRRQYEARIQALEKELGRY 1241
Cdd:PRK01156 580 IDIE---TNRSRSNEIKKQLNDLESRLQEIEiGFPDDKSYIDKSIREIENEANNL 631
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
899-1061 |
6.76e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 899 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 977
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 978 HKREAILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKSGQLrQGSAQSQQQIRGEIDSLRQE-- 1054
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEea 155
|
....*..
gi 767984051 1055 KDSLLKQ 1061
Cdd:PRK12704 156 KEILLEK 162
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
790-1064 |
8.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 790 EQEAEQVRAELSEGQRQLRELEGKELQdagersrlqefrrrvaaAQSQVQVLKEKKQATERLVSLSA-----QSEKRLQE 864
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQ-----------------QRSQLEQAKEGLSALNRLLPRLNlladeTLADRVEE 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 865 LernvqlmrqqqgqlqrrlreETEQKRRLEAEMSKRQHRVKELELkhEQQQKILKIKTEEIAAFQRkrrsgsngSVVSLE 944
Cdd:PRK04863 899 I--------------------REQLDEAEEAKRFVQQHGNALAQL--EPIVSVLQSDPEQFEQLKQ--------DYQQAQ 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 945 QQQKieeqkkwldqemeKVLQQRRALEELGEelhkREAILAKKEAlmqektgleSKRLRSSQALNEdivRVSSRLEHLEK 1024
Cdd:PRK04863 949 QTQR-------------DAKQQAFALTEVVQ----RRAHFSYEDA---------AEMLAKNSDLNE---KLRQRLEQAEQ 999
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767984051 1025 ELSEKSGQLRQGSAQSQQ------QIRGEIDSLRQEKDSlLKQRLE 1064
Cdd:PRK04863 1000 ERTRAREQLRQAQAQLAQynqvlaSLKSSYDAKRQMLQE-LKQELQ 1044
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
783-1122 |
9.18e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 783 SQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRL----QEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQS 858
Cdd:PRK10929 101 NMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLpqqqTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 859 EK-----RLQELErnvqlmrqqqgqLQRRLREETEQKRRLEAEMSKRQHrvKELELKHEQQQKILKikteeiaaFQRKRR 933
Cdd:PRK10929 181 ESaalkaLVDELE------------LAQLSANNRQELARLRSELAKKRS--QQLDAYLQALRNQLN--------SQRQRE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 934 SGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEAL-----MQEKTGLESKR-----LR 1003
Cdd:PRK10929 239 AER-----ALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQaasqtLQVRQALNTLReqsqwLG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 1004 SSQALNEDIVRVSSRLEHLEKelseksgqlrqgsaqsQQQIRGEIDSLRQEK----DSLLKQRLEIDGKLRQGSLLSPEE 1079
Cdd:PRK10929 314 VSNALGEALRAQVARLPEMPK----------------PQQLDTEMAQLRVQRlryeDLLNKQPQLRQIRQADGQPLTAEQ 377
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767984051 1080 ERTlfqldeaieaLDAAIEYKNEAITcrqrvlrasaSLLSQCE 1122
Cdd:PRK10929 378 NRI----------LDAQLRTQRELLN----------SLLSGGD 400
|
|
| COG5223 |
COG5223 |
Uncharacterized conserved protein [Function unknown]; |
891-1069 |
9.24e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 227548 [Multi-domain] Cd Length: 240 Bit Score: 39.63 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 891 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTE-------EIAAFQRKRRSGSNGSVVSLEQQQKIEEQ---KKWLDQEM 960
Cdd:COG5223 23 RRKYGKLEKKKDYVKRAQDINKKQDELKKLREKarernpdEYYHGMHSVKTDGGVSSIYREDEPTIMDLakmLKTQDNEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984051 961 EKVLQQ--RRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSA 1038
Cdd:COG5223 103 QRCRRKleRYKPMPCGTQIKFEESSLHTIFVDMRFGQK-EFIPEEFFRTTEELVVRRENRLEKDQIENNELEDSVFSGKL 181
|
170 180 190
....*....|....*....|....*....|....*
gi 767984051 1039 QSQQQIRGEID-SLRQEKDSLLK---QRLEIDGKL 1069
Cdd:COG5223 182 HSKLKEKAATElLLRQKRDKKLAaaeERVELDRLL 216
|
|
| |
