|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
1.23e-163 |
|
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: 493.00 E-value: 1.23e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRITLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 95 QTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTASR-DIQLREDE 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 173 HGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSRLPRPAQGQL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 251 VDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 1622954645 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
7.64e-139 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 427.37 E-value: 7.64e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRIT-------LGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 88 ATVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLevGTASRD 165
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMiGT-------PDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 166 IQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSRlprpaqGQLLV 245
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:smart00129 226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304
|
330 340 350
....*....|....*....|....*....|.
gi 1622954645 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
5.50e-135 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 416.59 E-value: 5.50e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 21 RVRPLLPKELLHGHQSCLQVEPGLGRITL-------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 94 GQTGSGKTYTMGEasvaslLEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 172 EHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSrlprpAQGQLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTG-----GEESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 252 DLAGSERVLKTG-STGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 1622954645 331 SDFDETLNTLNYASRAQNI 349
Cdd:pfam00225 308 SNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
15-347 |
1.58e-123 |
|
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: 386.23 E-value: 1.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKELLHGHqSCLQVEPG------LGRITLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 89 TVFAYGQTGSGKTYTMGEASvasllEDEQGIVPRAMAEAFKLIDENDLLD--CLVHVSYLEVYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 167 QLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSrlprpaQGQLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 1622954645 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
16-349 |
9.90e-108 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 344.33 E-value: 9.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELLHGHQSCLQV--------EPGLGRITL--------------GRDRHFGFHVVLAEDAGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 153 FRDLLEvgTASRDIQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 233 SRLPRPAQGQLLVskfhfVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQQVRQGKLSL-----IDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622954645 313 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
16-356 |
1.33e-104 |
|
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: 336.25 E-value: 1.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKEL---------LHGHQSCLQVEPGL---GRITLGRDRHFGFHVVL----AED---AGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQAdknNKATREVPKSFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLID--ENDLLDCLVHVSYLEVYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 155 DLLEVGTASRDIQLREDEH---GNVVLcGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRgRA 231
Cdd:cd01365 157 DLLNPKPKKNKGNLKVREHpvlGPYVE-DLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 232 PSRLPRPAQgqlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQR-----RGSHIPYRDSKI 306
Cdd:cd01365 235 DAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622954645 307 TRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01365 312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
16-349 |
1.11e-103 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 332.89 E-value: 1.11e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRITL--GRD------RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 88 ATVFAYGQTGSGKTYTMGEASVAsllEDEQGIVPRAMAEAFKLID-ENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 167 QLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQrgrapSRLPRPAQGQLLVS 246
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHIRVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01371 234 KLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANI 311
|
330 340
....*....|....*....|...
gi 1622954645 327 SPSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01371 312 GPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
16-349 |
5.62e-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: 327.37 E-value: 5.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELLHG--------HQSCLQVEPGLGRitlgrdrhFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 88 ATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 168 LREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPsrlprPAQGQLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 248 FHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 1622954645 328 PSSSDFDETLNTLNYASRAQNI 349
Cdd:cd01374 300 PAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
16-351 |
2.97e-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: 312.22 E-value: 2.97e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELlHGHQSCLQVEPGLG-RITL---GRDRH-FGFHVVLAEDAGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 91 FAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLIDENDLLDCLVH--VSYLEVYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTMEGP------PESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 166 IQlREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLeqRGRAPSRlprpaqGQLLV 245
Cdd:cd01366 156 IR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 1622954645 326 VSPSSSDFDETLNTLNYASRAQNIRN 351
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
16-358 |
4.93e-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: 306.94 E-value: 4.93e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRITL--------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 88 ATVFAYGQTGSGKTYTM-GEASVASLLEDEQ----GIVPRAMAEAFKLIDENDLlDCLVHVSYLEVYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 162 ASRDIQLREDEH--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSrlprpA 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID-----G 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 240 QGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGNAK 319
Cdd:cd01364 238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGRTK 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622954645 320 TVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWR 358
Cdd:cd01364 315 TSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
16-349 |
3.85e-93 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 303.48 E-value: 3.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELLHGHQSCLQVEPGlGRITLGRD---RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPE-DTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 93 YGQTGSGKTYTMgEASvaslLEDEQ--GIVPRAMAEAFKLIDEND-LLDCLVHVSYLEVYKEEFRDLLEVgtaSRD-IQL 168
Cdd:cd01369 83 YGQTSSGKTYTM-EGK----LGDPEsmGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 169 REDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRApsrlprpaQGQLLVSKF 248
Cdd:cd01369 155 HEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE--------TEKKKSGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 249 HFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSP 328
Cdd:cd01369 227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSP 304
|
330 340
....*....|....*....|.
gi 1622954645 329 SSSDFDETLNTLNYASRAQNI 349
Cdd:cd01369 305 SSYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
15-356 |
1.72e-83 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 277.08 E-value: 1.72e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRITLG-RDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 94 GQTGSGKTYTM-GEA-SVASLLEDEQGIVPRAMAEAFKLID-----ENDLLDCLVHVSYLEVYKEEFRDLLEvgTASRDI 166
Cdd:cd01373 82 GQTGSGKTYTMwGPSeSDNESPHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 167 QLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEqrgrapSRLPRPAQGQLLVS 246
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE------SWEKKACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340 350
....*....|....*....|....*....|.
gi 1622954645 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01373 314 VHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
2.77e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 284.32 E-value: 2.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 55 FGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 135 DLLDCL-VHVSYLEVYKEEFRDLLEVGTASRDIqlREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 214 SSRSHTVFTVTLEQRGRAPSRLPRpaqgqllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954645 294 RRGsHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:COG5059 282 KSG-HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
15-347 |
1.54e-79 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 265.80 E-value: 1.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKELLHGHQSCLQVE--------------PGLGRITLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhppkgsaANKSERNGGQKETkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDlldclVHVSYLEVYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 160 GTASRD-----IQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSR 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 235 LPRPAQGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRG--SHIPYRDSKITRILKD 312
Cdd:cd01368 231 DVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSKLTHLFQN 310
|
330 340 350
....*....|....*....|....*....|....*
gi 1622954645 313 SLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01368 311 YFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
15-345 |
2.80e-78 |
|
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: 261.85 E-value: 2.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKEL---------LHGHQSCLQVEPGLG-RITLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLLEAFF 83
Cdd:cd01367 1 KIKVCVRKRPLNKKEVakkeidvvsVPSKLTLIVHEPKLKvDLTKYIENHtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 84 EGFNATVFAYGQTGSGKTYTMGEASvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTa 162
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 163 srDIQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLeqrgrapsrlpRPAQGQ 242
Cdd:cd01367 158 --RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGTN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 243 LLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSSLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAKT 320
Cdd:cd01367 225 KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKT 301
|
330 340
....*....|....*....|....*
gi 1622954645 321 VMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01367 302 CMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
15-347 |
3.97e-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: 258.20 E-value: 3.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLgRITLGRDRHFG------FHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 89 TVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDENDLLDClVHVSYLEVYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlGS-------PEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 168 LREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGR-APSRLPRpaqgqllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERlAPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 1622954645 327 SPSSSDFDETLNTLNYASRAQ 347
Cdd:cd01376 299 APERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
55-345 |
1.05e-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: 246.34 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 55 FGFHVVLaEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASlleDEQGIVPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 135 DLLDCLVHVSYLEVYKEEFRDLL----EVGTASRDIQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHL 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 211 NRLSSRSHTVFTVTLEQRGRAPSrlprpaQGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLS------SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622954645 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
16-356 |
2.47e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 224.81 E-value: 2.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKEllhghQSCLQVEPGLGRITLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQ 95
Cdd:PLN03188 100 VKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 96 TGSGKTYTM-GEASVAS---LLEDEQGIVPRAMAEAFKLIDENDL------LDCLVHVSYLEVYKEEFRDLLEvgTASRD 165
Cdd:PLN03188 175 TGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 166 IQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEqrgrapSRLPRPAQG--QL 243
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVE------SRCKSVADGlsSF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 244 LVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLGGNAKTV 321
Cdd:PLN03188 327 KTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLGGNAKLA 406
|
330 340 350
....*....|....*....|....*....|....*
gi 1622954645 322 MIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 407 MVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-1199 |
3.56e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQ----EAERVRAELSEGQRQLRELEGKEPQDA 778
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 779 GERSRLQEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEM 857
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 858 SKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEEL 937
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 938 HKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKngQLRQGSAQSQQQIRREIDSLRQEKDS 1017
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA--ALEAALAAALQNIVVEDDEVAAAAIE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1018 LLKQ----RLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAKLSY 1091
Cdd:COG1196 565 YLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVTLAG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1092 LSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQ 1171
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
490 500
....*....|....*....|....*...
gi 1622954645 1172 SRDHLSEGLADSRRQYEARIQALEKDLG 1199
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
745-1196 |
1.48e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 745 RIRELEQEAERVRAELSEGQRQLRELEGKEpqdAGERSRLQEFRRRVAAAQSQVqvlkEKKQATERLVslsaqsEKRLQE 824
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAEL---AELEAELEELRLELEELELEL----EEAQAEEYEL------LAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 825 LERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLE 904
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 905 QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK 984
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 985 ELSEKNGQLRQ---------GSAQSQQQIRREIDSLRQEKDSLLKQR-----LEIDSKLRQGSLLSPEEERTLFQLDEAI 1050
Cdd:COG1196 454 LEEEEEALLELlaelleeaaLLEAALAELLEELAEAAARLLLLLEAEadyegFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1051 EALDAAIE-------------YKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ 1117
Cdd:COG1196 534 AAYEAALEaalaaalqnivveDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1118 QQIAFSE-----------LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRR 1185
Cdd:COG1196 614 RYYVLGDtllgrtlvaarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490
....*....|.
gi 1622954645 1186 QYEARIQALEK 1196
Cdd:COG1196 694 ELEEALLAEEE 704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
726-1063 |
2.41e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 726 GELVRTG---------KAAQALNRQhsQRIRELEQEAERVRAELSEGQRQLRELEGK----EPQDAGERSRLQEFRRRVA 792
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKEleelEEELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 793 AAQSQVQVLKEKKQaterlvslsaQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHE 872
Cdd:TIGR02168 730 ALRKDLARLEAEVE----------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 873 QQQKILKIKTEEI------AAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILA 945
Cdd:TIGR02168 800 ALREALDELRAELtllneeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 946 KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRqEKDSLLkqrLEI 1025
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLT---LEE 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622954645 1026 DSKLRQGSLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1063
Cdd:TIGR02168 956 AEALENKIEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
708-1131 |
1.61e-13 |
|
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: 75.44 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 708 QQKIREL-AINIRMKEELIGELVRTGKAAQALNRQHSQrIRELEQEAERVRAELSEGQRQLRELEGKepqdagersrLQE 786
Cdd:TIGR04523 217 ESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQ-LNQLKDEQNKIKKQLSEKQKELEQNNKK----------IKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 787 FRRRVAAAQSQVQVLKEKKQA--TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQhrv 864
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 865 KELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSvvSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELhKREAI 943
Cdd:TIGR04523 363 RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN--DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 944 LAKKE--ALMQEKTGLES-----KRLRSSQ-----ALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQ------QIR 1005
Cdd:TIGR04523 437 KNNSEikDLTNQDSVKELiiknlDNTRESLetqlkVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleekvkDLT 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1006 REIDSLRQEKDSLLKQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrvlrasaSLLSqcem 1083
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK----------SLKK---- 582
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622954645 1084 nlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1131
Cdd:TIGR04523 583 ---------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
744-1080 |
2.26e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 744 QRIRELEQEAERVRAELSEGQRQLRELEgkepqdagersrlqefrRRVAAAQsQVQVLKEKKQATERLVSLsaqseKRLQ 823
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLE-----------------RQAEKAE-RYRELKEELKELEAELLL-----LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 824 ELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSL 903
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 904 EQQQKIEEQkkwLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLE 983
Cdd:COG1196 316 ERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 984 KELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1063
Cdd:COG1196 393 RAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330
....*....|....*..
gi 1622954645 1064 ITCRQRVLRASASLLSQ 1080
Cdd:COG1196 472 AALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
677-1018 |
9.36e-12 |
|
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: 70.09 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 677 PGSRAVGGSKAR---VQARQVPSATASEwRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE----- 748
Cdd:TIGR02168 657 PGGVITGGSAKTnssILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdl 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 749 --LEQEAERVRAELSEGQRQLRELEGK----EPQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATERLVSLSAQ---S 818
Cdd:TIGR02168 736 arLEAEVEQLEERIAQLSKELTELEAEieelEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAEltlL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 819 EKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsng 898
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL---- 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 899 svVSLEQQQKIEEQKKWLDQEMEKvlqqRRALEELGEELHKreAILAKKEALMQEKTGLEskRLRSSQALNEDIVrvssr 978
Cdd:TIGR02168 892 --LRSELEELSEELRELESKRSEL----RRELEELREKLAQ--LELRLEGLEVRIDNLQE--RLSEEYSLTLEEA----- 956
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622954645 979 lehlekelseknGQLRQGSAQSQQQIRREIDSLRQEKDSL 1018
Cdd:TIGR02168 957 ------------EALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
67-288 |
1.37e-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: 64.29 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 67 QEAVYqACVQPLLEAFFEGFN-ATVFAYGQTGSGKTYTMgeasvaslledeQGIVPRAMAEAFklidendlldclvhvSY 145
Cdd:cd01363 32 QPHVF-AIADPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAF---------------NG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 146 LEVYKEEFRDLLEvgtasrdiqlredehgnvvlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHLNRLSSRSHTVFTVtl 225
Cdd:cd01363 84 INKGETEGWVYLT------------------------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI-- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954645 226 eqrgrapsrlprpaqgqllvskfhFVDLAGSERvlktgstgerlkesiqINSSLLALGNVISA 288
Cdd:cd01363 137 ------------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
704-1031 |
2.01e-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: 68.51 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 704 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalnrqhSQRIRELEQEAERVRAELSEGQRQLRElegKEPQDAGERSR 783
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEE---KQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 784 LQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 863
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 864 VKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREAI 943
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 944 LAKK-EALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKNgqlrqgsaqsqqqirREIDSLRQEKDSLLK 1020
Cdd:TIGR04523 522 LKEKiEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEKN---------------KEIEELKQTQKSLKK 582
|
330
....*....|.
gi 1622954645 1021 QRLEIDSKLRQ 1031
Cdd:TIGR04523 583 KQEEKQELIDQ 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
712-1058 |
6.65e-11 |
|
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: 67.40 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 712 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAERVRAELSEGQRQLRELegkepqdageRSRLQEFR 788
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKRELSSL----------QSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 789 RRVAAAQSQVQVLKEKkqaTERLvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 868
Cdd:TIGR02169 702 NRLDELSQELSDASRK---IGEI-------EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 869 LK-HEQQQKILKIKT-------EEIAA---FQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 936
Cdd:TIGR02169 772 EDlHKLEEALNDLEArlshsriPEIQAelsKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 937 LHKR-EAILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKNGQLRQ-----GSAQSQQQIRREIDS 1010
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRElerkiEELEAQIEKKRKRLS 920
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622954645 1011 LRQEKDSLLKQRL-EIDSKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1058
Cdd:TIGR02169 921 ELKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
706-1212 |
1.15e-10 |
|
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: 66.53 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 706 QAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQ--------HSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQD 777
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 778 AGERSRLQEFRRRVAAAQSQVQvlkEKKQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreETEQKRRLEAEM 857
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQH------------------IHTLQQQKTTLT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 858 SKRQHRVKELELKHEQQQKIlkikteeiaAFQRKRRSGSNGSVVSLEQQQKIE-EQKKWLDQEMEKVLQ----QRRALEE 932
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATI---------DTRTSAFRDLQGQLAHAKKQQELQqRYAELCAAAITCTAQceklEKIHLQE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 933 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKEL-----SEKNGQLRQGSAQSQQQIRRE 1007
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1008 IDSLRQEKDSLLKQRLEIdsklrqgsllspEEERTLFQLDEAIEAldaaieykneaiTCRQRVlRASASLLSQcEMNLMA 1087
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASL------------KEQMQEIQQSFSILT------------QCDNRS-KEDIPNLQN-ITVRLQ 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1088 KLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLV----YWLEVALERQRlEMDRQLTLQQKEHEQ 1163
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTalhaLQLTLTQERVR-EHALSIRVLPKELLA 676
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622954645 1164 NMQLLLQ--QSRDHLSEGLADSRRQYEARIQALEKDLGRYMWINQELKQKL 1212
Cdd:TIGR00618 677 SRQLALQkmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-1040 |
1.75e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 705 AQAQQKIR-----------ELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELSEGQRQLREL 770
Cdd:TIGR02168 207 RQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 771 EGkepqdagersRLQEFRRRVAAAQSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 850
Cdd:TIGR02168 287 QK----------ELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 851 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNgsvvsleQQQKIEEQKKWLDQEMEKVLQQRRAL 930
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-------EIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 931 EELGEElHKREAILAKKEALMQEKTGLESKRLRSSQALNedivRVSSRLEHLEKELSEKNGQLRQGSAQ--SQQQIRREI 1008
Cdd:TIGR02168 427 LKKLEE-AELKELQAELEELEEELEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
|
330 340 350
....*....|....*....|....*....|...
gi 1622954645 1009 DSLRQEKDSLLKQRLEIDSKL-RQGSLLSPEEE 1040
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILgVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
744-1080 |
1.20e-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: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 744 QRIRELEQEAERVRAELSEGQRQLRELEGkepqdagersRLQEFRRRVAAAQsQVQVLKEKKQATERLVSLsaqseKRLQ 823
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELER----------QLKSLERQAEKAE-RYKELKAELRELELALLV-----LRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 824 ELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsl 903
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----------------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 904 eqqqKIEEQKKWLDQEMEKVLQQ-----------RRALEELGEELHKREAILAK-------KEALMQEKTGLESKRLRSS 965
Cdd:TIGR02168 299 ----RLEQQKQILRERLANLERQleeleaqleelESKLDELAEELAELEEKLEElkeelesLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 966 QALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQsQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLlsPEEERTLFQ 1045
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEE 451
|
330 340 350
....*....|....*....|....*....|....*
gi 1622954645 1046 LDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1080
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
792-1037 |
1.40e-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: 61.70 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 792 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKH 871
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 872 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELHKREAILAKKEA 949
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 950 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKL 1029
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 1622954645 1030 RQGSLLSP 1037
Cdd:COG4942 251 LKGKLPWP 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-1199 |
1.52e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 701 EWRLAQAQQKIRELAINIRmkeELIGELvrtgkaaqalnrqhsQRIRELEQEAERVRAELSEGQRQLRELEGKEpqdAGE 780
Cdd:PRK03918 199 EKELEEVLREINEISSELP---ELREEL---------------EKLEKEVKELEELKEEIEELEKELESLEGSK---RKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 781 RSRLQEFRRRVAAAQSQVQVLKEK----------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 850
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKvkelkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 851 RRLEaEMSKR----QHRVKELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQ 925
Cdd:PRK03918 338 ERLE-ELKKKlkelEKRLEELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 926 QRRALEELGEELH---------KREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQL-RQ 995
Cdd:PRK03918 413 RIGELKKEIKELKkaieelkkaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 996 GSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAIT 1065
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1066 CRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALER 1145
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEE 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1146 QRLEMDR-QLTLQQKEHEQNMQLLLQQSRDHLS-----EGLADSRRQYEARIQALEKDLG 1199
Cdd:PRK03918 645 LRKELEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
745-1211 |
1.80e-09 |
|
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: 62.35 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 745 RIRELEQEAERVRAELSEGQRQLRELEGK----EPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEK 820
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENElnllEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 821 RLQELERNVQlmrqqqgqlqrrlrEETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIaafqrkrrSGSNGSV 900
Cdd:TIGR04523 226 QNNQLKDNIE--------------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--------EQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 901 VSLEQQ-QKIEEQKKWLDQEMEKVLqqrraLEELGEELHKREailakkealmQEKTGLESKRLRSSQA---LNEDIVRVS 976
Cdd:TIGR04523 284 KELEKQlNQLKSEISDLNNQKEQDW-----NKELKSELKNQE----------KKLEEIQNQISQNNKIisqLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 977 SRLEHLEKELSEKNGQLRQgsAQSQ-QQIRREIDSLRQEKDSLLKQRLEIDSKLRQgsllspeEERTLFQLDEAIEALda 1055
Cdd:TIGR04523 349 KELTNSESENSEKQRELEE--KQNEiEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKL-- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1056 aiEYKNEAITCRQRVLRASASLLSQCEMNLmaklsylssSETRALLCKYFDKVVTLREEQhQQQIafSELEMQLEEQQRL 1135
Cdd:TIGR04523 418 --QQEKELLEKEIERLKETIIKNNSEIKDL---------TNQDSVKELIIKNLDNTRESL-ETQL--KVLSRSINKIKQN 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 1136 VYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRDHLSegladsrrqyeaRIQALEKDLGRymwINQELKQK 1211
Cdd:TIGR04523 484 LEQKQKELKSKEKELK-KLNEEKKELEEKVKDLTKKISSLKE------------KIEKLESEKKE---KESKISDL 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-957 |
1.90e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 704 LAQAQQKIRELAINIRMKEELI-------GELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGkepQ 776
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA---Q 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 777 DAGERSRLQEFRRRVAAAQSQVQVLKEKKQAT----ERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR 852
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLeaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 853 LEAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEe 932
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE- 481
|
250 260
....*....|....*....|....*
gi 1622954645 933 lgEELHKREAILAKKEALMQEKTGL 957
Cdd:TIGR02168 482 --RELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
697-1015 |
3.21e-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: 61.62 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 697 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELSEGQRQLRELEGk 773
Cdd:TIGR02169 208 EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEELNKKIKDLGE- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 774 epqdaGERSRLQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR 852
Cdd:TIGR02169 287 -----EEQLRVKEKIGELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 853 LEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEE 932
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 933 LGEElhKREAILAKKEALMQEKTGLESKRlrssqalnEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLR 1012
Cdd:TIGR02169 442 EKED--KALEIKKQEWKLEQLAADLSKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
...
gi 1622954645 1013 QEK 1015
Cdd:TIGR02169 512 VEE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
686-1030 |
9.28e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 686 KARVQARQVPSATASEWRLAQAQQKIRELainiRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQR 765
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 766 QLR---ELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERnvqlmRQQQGQLQRR 842
Cdd:PTZ00121 1550 ELKkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 843 LREETEQKRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSGsngsvvslEQQQKIEEQKKWLDQEME 921
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEeLKKAEEENKIKAAEEAKKAEEDKKKAE--------EAKKAEEDEKKAAEALKK 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 922 KVLQQRRAleelgEELHKREAILAKK-EALMQEktglESKRLRSSQALNEDIVRVSSRLEHLEKELSEKN--GQLRQGSA 998
Cdd:PTZ00121 1697 EAEEAKKA-----EELKKKEAEEKKKaEELKKA----EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEEE 1767
|
330 340 350
....*....|....*....|....*....|....
gi 1622954645 999 QSQQQIRREIDSLRQE--KDSLLKQRLEIDSKLR 1030
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIK 1801
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
799-1100 |
9.82e-09 |
|
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: 59.99 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 799 QVLKEKKQATERLVSLSAQSEKRL----------QELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 868
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLELeeeyllyldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 869 LKHEQ-QQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELH-KREAILAK 946
Cdd:pfam02463 278 EKEKKlQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 947 KEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRqgSAQSQQQIRREIDSLRQEKDSLLKQRLEID 1026
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--EAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954645 1027 SKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRqrvLRASASLLSQCEMNLMAKLSYLSSSETRAL 1100
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
701-1198 |
1.19e-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: 59.69 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 701 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGK--EPQDA 778
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 779 --GERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLE 854
Cdd:TIGR02168 381 leTLRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 855 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 920
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 921 EKVL-------------QQRRALEELGEELHKREAILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 980
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 981 ----------------HLEKELSEKN-------------GQLRQGSAQSQQQI---RREIDSLRQEK------------- 1015
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPGYrivtldgdlvrpgGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1016 -DSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1094
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1095 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRD 1174
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 1622954645 1175 --HLSEGLADSRRQYEARIQALEKDL 1198
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
662-1196 |
1.84e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 662 RKGPELCLEELDAAIPGSRAVGGSKARVQARQVPSA-TASEWRLAQAQQKIREL--AINIRMKEEL-IGELVRTGKAA-Q 736
Cdd:PTZ00121 1128 RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAArkAEEVRKAEELrKAEDARKAEAArK 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 737 ALNRQHSQRIRELEQE--------AERVRAELSEGQRQlRELEGKEPQDAGERSRLQEFRRRVAAAQSQ-------VQVL 801
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAkkaeavkkAEEAKKDAEEAKKA-EEERNNEEIRKFEEARMAHFARRQAAIKAEearkadeLKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 802 KEKKQATERLVS----------LSAQSEKRLQELERNVQLMRQQQGQLQRRLREET---------EQKRRLEAEMSKRQH 862
Cdd:PTZ00121 1287 EEKKKADEAKKAeekkkadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaeaakaeAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 863 RVKELElKHEQQQKI--LKIKTEEIAAFQRKRRSGSNGSVVSlEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKR 940
Cdd:PTZ00121 1367 EAAEKK-KEEAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 941 EAILAKKEAlmQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGS--AQSQQQIRREIDSLRQEKDSL 1018
Cdd:PTZ00121 1445 KADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAK 1522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1019 LKQRL-EIDSKLRQGSLLSPEEERTLFQLDEAIEALDA----AIEYKNEAITCRQRVLRaSASLLSQCEMNLMAKLSYLS 1093
Cdd:PTZ00121 1523 KADEAkKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLY 1601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1094 SSETRAllckyfdKVVTLREEQhQQQIAFSELEMQLEEQQRLvywleVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSR 1173
Cdd:PTZ00121 1602 EEEKKM-------KAEEAKKAE-EAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
570 580
....*....|....*....|...
gi 1622954645 1174 dhlsEGLADSRRQYEARIQALEK 1196
Cdd:PTZ00121 1669 ----KAEEDKKKAEEAKKAEEDE 1687
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
736-1202 |
1.96e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 736 QALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLS 815
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 816 AQsEKRLQELERNVqlmrqqqgqlqRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 895
Cdd:COG4717 129 PL-YQELEALEAEL-----------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 896 SNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGL----ESKRLRSSQALNE 970
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 971 DIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKlrqgslLSPEEERTLFQLDEAI 1050
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPD------LSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1051 EALDAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLE 1130
Cdd:COG4717 350 QELLREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEE-------LEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1131 E-----QQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNM-------QLLLQQSRDHLSEGLADSRRQYEARIQALEKDL 1198
Cdd:COG4717 413 EllgelEELLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEEW 492
|
....
gi 1622954645 1199 GRYM 1202
Cdd:COG4717 493 AALK 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
923-1212 |
2.07e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 923 VLQQRRALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQ 1002
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1003 ------QIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1076
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1077 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1156
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 1157 QQKEHEQNMQLLlqqsrDHLSEGLADSRRQYEARIQALEKDLgrymwinQELKQKL 1212
Cdd:TIGR02168 902 ELRELESKRSEL-----RRELEELREKLAQLELRLEGLEVRI-------DNLQERL 945
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
703-1197 |
3.40e-08 |
|
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: 58.29 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAERVR--AELSEGQRQ--LRELEGKEPQDA 778
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKtnGLLHTEDREeeIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 779 GERSRLQEFRRRVAAAQSQVQVLKEK-----------KQATERLV-SLSAQsEKRLQELERNVQLMRQQQGQLQRRLREE 846
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKletltnqnsdcKQHIEVLKeSLTAK-EQRAAILQTEVDALRLRLEEKESFLNKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 847 TEQKRRLEAEMSKRQHRVKELelkheqqQKILKIKTEEIAAFQRKrrsgsngsVVSLEQQQKieEQKKWLDQEMEKV--L 924
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDL-------KDMLDVKERKINVLQKK--------IENLQEQLR--DKDKQLAGLKERVksL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 925 QQRR-----ALEELGEELHKREAILakkEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLR--QGS 997
Cdd:pfam10174 428 QTDSsntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEH 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 998 AQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLrQGSLL----SPEEERTLFQLDEAIEALDAAIE-YKNEAITCRQRVLR 1072
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKL-ENQLKkahnAEEAVRTNPEINDRIRLLEQEVArYKEESGKAQAEVER 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1073 ASAsLLSQCEMNLMAKLSYLSSSETRALLcKYFDKVVTLREEQHQQQIAFSELEMQLEE------------QQRLVYWLE 1140
Cdd:pfam10174 584 LLG-ILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEarrrednladnsQQLQLEELM 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 1141 VALERQRLEMDrqltlQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARI----QAL-----EKD 1197
Cdd:pfam10174 662 GALEKTRQELD-----ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILemkqEALlaaisEKD 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
692-1080 |
3.63e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 692 RQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELE 771
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 772 gkepqdagerSRLQEFRRRVAAAQSQVQVLKEKKQATERLV-SLSAQSEKRLQELERNVqlmrqqqGQLQRRLREETEQK 850
Cdd:COG4717 153 ----------ERLEELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEEL-------EELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 851 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAF------------------------------------------ 888
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllar 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 889 QRKRRSGSNGSVVSLEQQQKIEEQK-------------------KWLDQEMEKVLQQRRALEELGEELhKREAILAKKEA 949
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQELLREAEELEEEL-QLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 950 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQ--------QQIRREIDSLRQEKDSLLKQ 1021
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREE 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622954645 1022 RLEIDSKLRQgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1080
Cdd:COG4717 455 LAELEAELEQ-----LEEDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
693-890 |
3.85e-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: 57.08 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 693 QVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEG 772
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 773 KepqdagERSRLQEFRRRVAAAQSQVQVLKEK------------------KQATERLVSLSAQSEKRLQELERNVQLMRQ 834
Cdd:COG4942 98 E------LEAQKEELAELLRALYRLGRQPPLAlllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 835 QQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 890
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
746-1082 |
4.73e-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: 57.77 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 746 IRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRrrvaAAQSQVQVLKEKKQATERLVSLsaqseKRLQEL 825
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREYEGYELL-----KEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 826 ERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKEL--ELKHEQQQKILKIKtEEIAAFQRKRRSGSNGSVVSL 903
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkKIKDLGEEEQLRVK-EKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 904 EQQQKIEEQKKWLDQEMEKVLQQRRALE-ELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHL 982
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELErEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 983 EKELSEKNGQLRQGS--AQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYK 1060
Cdd:TIGR02169 395 EKLKREINELKRELDrlQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340
....*....|....*....|..
gi 1622954645 1061 NEAITCRQRVLRASASLLSQCE 1082
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAE 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
690-1064 |
4.84e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 690 QARQVPSATASEWRLAQAQQKIRElainIRMKEELigelvrTGKAAQALNRQHSQRIRELEQEAERVRAElSEGQRQLRE 769
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEE----KKKADEA------KKKAEEAKKADEAKKKAEEAKKAEEAKKK-AEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 770 LEGKepqdAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQ 849
Cdd:PTZ00121 1475 AKKK----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 850 KRRLEaEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSV-------------------VSLEQQQKIE 910
Cdd:PTZ00121 1551 LKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeekkmkaeeakkaeeakIKAEELKKAE 1629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 911 EQKKWLDQEMEKVLQQRRALEELGEELH---------KREAILAKKEAlmQEKTGLESKRLRSSQALNEdivrvssrleh 981
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEenkikaaeeAKKAEEDKKKA--EEAKKAEEDEKKAAEALKK----------- 1696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 982 lEKELSEKNGQLRQGSAQSQ---QQIRREiDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1058
Cdd:PTZ00121 1697 -EAEEAKKAEELKKKEAEEKkkaEELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
....*.
gi 1622954645 1059 YKNEAI 1064
Cdd:PTZ00121 1775 KEKEAV 1780
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
5.91e-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: 52.99 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 16 VRVALRVRPLLPKELlhghqsclQVEPGLGRITLGRDRH----FGFHVVLAEDAGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622954645 92 AYGQTGSGKTYTMgeasvaslledeqgiVPRAMAEAFKLIDENDLLDCL-VHVSYLEVYKEEFRDLL 157
Cdd:pfam16796 93 AYGQTGSGSNDGM---------------IPRAREQIFRFISSLKKGWKYtIELQFVEIYNESSQDLL 144
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
686-952 |
6.44e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.06 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 686 KARVQARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAERVRA-ELSE 762
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMRElERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 763 GQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQR 841
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 842 RLREETEQKRRlEAEMSKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQ 912
Cdd:pfam17380 465 LRQQEEERKRK-KLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEE 540
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622954645 913 KKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQ 952
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
699-1060 |
7.45e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 699 ASEWRLAQAQQKIREL--AINIRMKEEL-IGELVRtgKAAQALNRQHSQRIRELEQEAERvRAELSEGQRQLRELEGKEP 775
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAkkAEEKKKADELkKAEELK--KAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 776 QDAGERSRLQEFRRRVAAAQSQVQVLK--EKKQATERLVSLSAQSEKRLQELERnvQLMRQQQGQLQRRLREETEQKRRL 853
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKaeEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 854 EAEMSKRQHRVKELELKHEQQQK-----ILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRR 928
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 929 ALEELGEELHKREAILAKKEALMQEktGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREI 1008
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVA 1836
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622954645 1009 DS---LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYK 1060
Cdd:PTZ00121 1837 DSknmQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
686-949 |
8.40e-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: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 686 KARVQARQVPSATAS-EWRLAQAQQKIRELAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIRELEQEAERVRAELSEG 763
Cdd:TIGR02169 234 ALERQKEAIERQLASlEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 764 QRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEkkQATERLVSLSAQSEK---RLQELERNVQLMRQQQGQLQ 840
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 841 RRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsNGSVVSlEQQQKIEEQKKWLDQEM 920
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIK-KQEWKLEQLAADLSKYE 468
|
250 260
....*....|....*....|....*....
gi 1622954645 921 EKVLQQRRALEELGEELHKREAILAKKEA 949
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
663-1163 |
1.04e-07 |
|
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: 56.65 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 663 KGPELCLEELDAAIPGSRAVGGSKARVQARQVpsATASEWRLAQAQQKIRELAINIRMKEELI-GELVRTGKAAQALNRQ 741
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQKALEEDLQI--ATKTICQLTEEKEAQMEELNKAKAAHSFVvTEFEATTCSLEELLRT 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 742 HSQRIRELEQEAERVRAELsegQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQS------QVQVLKEKKQATER-LVSL 814
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMEL---QKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkQFEKIAEELKGKEQeLIFL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 815 SAQSEKRLQELERNVQLMRQQQGQLQRRLRE-----ETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQ 889
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 890 RKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVlqqRRALEELGEELHKReaiLAKKEALMQEKTGLESKRLRSSQALN 969
Cdd:pfam05483 525 CKKQEER-----MLKQIENLEEKEMNLRDELESV---REEFIQKGDEVKCK---LDKSEENARSIEYEVLKKEKQMKILE 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 970 EDIVRVSSRLEHLEK---ELSEKNGQL-RQGSAQSQQQIRREI--DSLRQEKDSlLKQRLE--IDSKLRQGSLLSPEEER 1041
Cdd:pfam05483 594 NKCNNLKKQIENKNKnieELHQENKALkKKGSAENKQLNAYEIkvNKLELELAS-AKQKFEeiIDNYQKEIEDKKISEEK 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1042 TLFQLDEAIEALDAAIEYKNEA-ITCRQRVLRASAsllsqcemnLMAKLSYlsssetrallckYFDKVVtlrEEQHQQQI 1120
Cdd:pfam05483 673 LLEEVEKAKAIADEAVKLQKEIdKRCQHKIAEMVA---------LMEKHKH------------QYDKII---EERDSELG 728
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1622954645 1121 AFSELEmqlEEQQRLVYWLEVALERQRLEM---DRQLTLQQKEHEQ 1163
Cdd:pfam05483 729 LYKNKE---QEQSSAKAALEIELSNIKAELlslKKQLEIEKEEKEK 771
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
704-1031 |
1.20e-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: 56.52 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 704 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQE----AERVRAELSEGQRQLRELEGK---EPQ 776
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKideEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 777 DAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 856
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 857 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEE 932
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 933 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV--------RVSSRLEHLEKELSEKNGQLRQGSA---QSQ 1001
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEennkeeeeERNKRLLLAKEELGKVNLMAIEEFEekeERY 990
|
330 340 350
....*....|....*....|....*....|
gi 1622954645 1002 QQIRREIDSLRQEKDSLLKQRLEIDSKLRQ 1031
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
745-1212 |
1.53e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 745 RIRELEQEAERVraelsegQRQLRELEGKEPQDAGERSRLQEFRRRVAAaqsqvqvLKEKKQATERLVSLSAQSEKRLQE 824
Cdd:PRK03918 194 LIKEKEKELEEV-------LREINEISSELPELREELEKLEKEVKELEE-------LKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 825 LERNVqlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsvvSLE 904
Cdd:PRK03918 260 KIREL--------------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE------------------YLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 905 QQQKIEEqkkwldqEMEKVLQQRRALEELGEELHKREailAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEHL 982
Cdd:PRK03918 308 ELREIEK-------RLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 983 EKELSEKngqlrqgsaqSQQQIRREIDSLRQEKDSLLKQRLEIDSKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKNE 1062
Cdd:PRK03918 378 KKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1063 AITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVA 1142
Cdd:PRK03918 438 CPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKELA 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1143 LERQRLEmdrqltlqQKEHEQNMQLLLQQSRDHlsEGLADSRRQYEARIQALEKDLGRYmwinQELKQKL 1212
Cdd:PRK03918 503 EQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKL----EELKKKL 558
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
703-1015 |
1.56e-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: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGK--EPQDAGE 780
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 781 RSRLQEFRRRVAAAQSQVQ----VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 856
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 857 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 935
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 936 ELHKREAILAKKEALMQEKTGLESKRLRSSQalneDIVRVSSRLehleKELSEKNGQLrqgsAQSQQQIRREIDSLRQEK 1015
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQ----EYEEVLKRL----DELKEKRAKL----EEERKAILERIEEYEKKK 1016
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
704-1174 |
4.02e-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: 54.74 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 704 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAERVRAELSEGQR----QLRELEGKEPQDAG 779
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 780 E----RSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRL---------------QEL-ERNVQLMRQQQGQL 839
Cdd:pfam15921 357 ElteaRTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrRELdDRNMEVQRLEALLK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 840 QRRLREETEQKRRLEAEMSKRQ--HRVKELELKHEQQQKILKIKTEEIAA----FQRKRRSGSNGSVVSLEQQQKIEEQK 913
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 914 KWLDQEMEKV---LQQRRALEELGEELHKREAILAKKEALMQEK--------------TGLESKRLRSSQALNEDIVRVS 976
Cdd:pfam15921 517 AEITKLRSRVdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMQVEKAQLE 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 977 SRLEHLEKELSE-------KNGQLRQGSAQ-------------SQQQIRREIDSLRQEKDSLLKQ----RLEIDSKLRQG 1032
Cdd:pfam15921 597 KEINDRRLELQEfkilkdkKDAKIRELEARvsdlelekvklvnAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDY 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1033 SLL-------SPEEERTLFQLDEAIEALDAAIEYKNEAITCRQ----RVLRASASLLSQCEMN------LMAKLSYLSSS 1095
Cdd:pfam15921 677 EVLkrnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEA 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1096 ETRALLCKYFdkvvtLREEQHQQQIAFS-----------ELEMQLEEQQRL---VYWLEVALERQRLEMDRQLTLQQKEH 1161
Cdd:pfam15921 757 MTNANKEKHF-----LKEEKNKLSQELStvateknkmagELEVLRSQERRLkekVANMEVALDKASLQFAECQDIIQRQE 831
|
570
....*....|...
gi 1622954645 1162 EQNMQLLLQQSRD 1174
Cdd:pfam15921 832 QESVRLKLQHTLD 844
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
717-1044 |
4.55e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.38 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 717 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELegkepqdageRSRLQEFRRRVAAAQS 796
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 797 QVQVLKEKKQAT-ERLVSLSAQSEKRLQELernvqlmrqqqgqlqrrlrEETEQKRRLEAEMSKrqhRVKELELKheQQQ 875
Cdd:COG1340 72 KVKELKEERDELnEKLNELREELDELRKEL-------------------AELNKAGGSIDKLRK---EIERLEWR--QQT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 876 KILKIKtEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK-REAILAKKEALMQEK 954
Cdd:COG1340 128 EVLSPE-EEKELVEKIKELEK-----ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 955 TGLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRL-EIDSKLRQGS 1033
Cdd:COG1340 202 KEADELR-KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAeEIFEKLKKGE 280
|
330
....*....|.
gi 1622954645 1034 LLSPEEERTLF 1044
Cdd:COG1340 281 KLTTEELKLLQ 291
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
699-1062 |
4.62e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 699 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDA 778
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 779 GERSRLQEFRRRVAAAQSQ-----VQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 853
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAEleeeeEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 854 ---------------------------EAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAF------------QRKRRS 894
Cdd:COG1196 515 llaglrglagavavligveaayeaaleAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkiraraalAAALAR 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 895 GSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDivr 974
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 975 vSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALD 1054
Cdd:COG1196 672 -AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
....*...
gi 1622954645 1055 AAIEYKNE 1062
Cdd:COG1196 751 EALEELPE 758
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
697-1198 |
5.11e-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: 54.36 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 697 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAELSEGQRQL------ 767
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknelse 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 768 --RELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLrE 845
Cdd:pfam05557 116 lrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK-S 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 846 ETEQKRRLEAEMSKRQHRVKELelkHEQQQKILKIKtEEIAAFQRK--RRSGSNGSVVSLE-----QQQKIEEQKKwLDQ 918
Cdd:pfam05557 195 ELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRKleREEKYREEAATLElekekLEQELQSWVK-LAQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 919 EMEKVLQQRRALEELGEELHKREAilakkeALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKNGQLRQ 995
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREI------VLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 996 gsaqsqqqIRREIDSLRQEKDsLLKQRLE-IDSKLRqgsllspEEERTLFQLDEAIEALDAAIEYKNEAITCRQRV---L 1071
Cdd:pfam05557 344 --------LQRRVLLLTKERD-GYRAILEsYDKELT-------MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLsvaE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1072 RASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQRLEMD 1151
Cdd:pfam05557 408 EELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERRCLQGD 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622954645 1152 RQLTLQQK-EHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQALEKDL 1198
Cdd:pfam05557 480 YDPKKTKVlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
738-1229 |
8.27e-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: 53.82 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 738 LNRQHS--QRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKekkqatERLVSLS 815
Cdd:TIGR00618 371 SCQQHTltQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ------RYAELCA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 816 AQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 895
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 896 SNGSVVsleqqQKIEEQKKWLDQEMEKVLQQrraleelGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRV 975
Cdd:TIGR00618 525 PLTRRM-----QRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 976 SSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRqekdslLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDA 1055
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD------VRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1056 AIEYKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQLEEQ 1132
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSDLAAR 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1133 QRLVYWLEVALERQRLEMDRQLTL--QQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQALEKDLGRymwINQELKQ 1210
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE---IGQEIPS 814
|
490
....*....|....*....
gi 1622954645 1211 KLGGVNTVGHSRGGEKRSL 1229
Cdd:TIGR00618 815 DEDILNLQCETLVQEEEQF 833
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
691-1065 |
1.11e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 691 ARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAERVRAELSEG-- 763
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlt 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 764 ---QRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQA-TERLVSLSAQSEKRLQELERNVQLMRQQQGQL 839
Cdd:TIGR00618 528 rrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 840 QRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQ 907
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 908 KIEEQKKWLD----------QEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQALNEDIVRVS 976
Cdd:TIGR00618 688 EKEQLTYWKEmlaqcqtllrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKeLMHQARTVLKARTEAHFNNN 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 977 SR----------LEHLEKELSEKN-------GQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEE 1039
Cdd:TIGR00618 768 EEvtaalqtgaeLSHLAAEIQFFNrlreedtHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
410 420
....*....|....*....|....*.
gi 1622954645 1040 ERTLFQLDEAIEALDAAIEYKNEAIT 1065
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
712-1178 |
1.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 712 RELAINIRMKEELIGELvRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGERSRLQEFRRRV 791
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 792 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLEAEMSKRQHRVKELELK 870
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 871 HEQQQKILKIKTEEIAAFQRKRR-------SGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQ---------QRRALEELG 934
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERlkearllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfllLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 935 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREI------ 1008
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1009 ---DSLR------QEKDSLLKQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAIT-CRQRVLRASAs 1076
Cdd:COG4717 382 edeEELRaaleqaEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEeLREELAELEA- 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1077 llsqcemnlmaKLSYLSSSETrallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVYwLEVALERqrlemdrqltL 1156
Cdd:COG4717 461 -----------ELEQLEEDGE-------------LAELLQELEELKAELRELAEEWAALKL-ALELLEE----------A 505
|
490 500
....*....|....*....|..
gi 1622954645 1157 QQKEHEQNMQLLLQQSRDHLSE 1178
Cdd:COG4717 506 REEYREERLPPVLERASEYFSR 527
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
740-1069 |
2.11e-06 |
|
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: 52.27 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 740 RQHSQRIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEkkqaterlvslsaqSE 819
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAEAEQELEESKRE--------------TE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 820 KRLQELERNVQLMRQQQGQLQRRLREETEQ------KRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 893
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 894 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKReailakkealmqEKTGLESKRLRSSQALNEDIV 973
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKV------------MREADEESQSRLEEAYDEINR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 974 RVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEAL 1053
Cdd:COG5185 475 SVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
330
....*....|....*.
gi 1622954645 1054 DAAIEYKNEAITCRQR 1069
Cdd:COG5185 555 NAKTDGQAANLRTAVI 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1219 |
3.23e-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: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 845 EETEQK--------RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSLEQqqKIEEQKKWL 916
Cdd:TIGR02168 175 KETERKlertrenlDRLEDILNELERQLKSLERQAEKAERYKELKAEL----RELELALLVLRLEELRE--ELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 917 DQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKNGQLRQ 995
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISrLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 996 GSAQSQQQiRREIDSLRQEKDSLLKQRLEIDSKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNeaitcrqrvlrasa 1075
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLR-------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1076 sllsqcemnlmaklsylsssetrallckyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywlevalERQRLEmDRQLT 1155
Cdd:TIGR02168 386 ------------------------------SKVAQLELQIASLNNEIERLEARLERLED---------RRERLQ-QEIEE 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954645 1156 LQQKEHEQNMQLLlQQSRDHLSEGLADSRRQYEARIQALEKDLGRYMWINQELKQKLGGVNTVG 1219
Cdd:TIGR02168 426 LLKKLEEAELKEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
596-940 |
5.45e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 596 EQVTNGREAGVELLTEVNRLGSGSSAASEEEEEEEEELPRRTLHLRRNGISNCSQRAgalpgslpERKGPELCLEELDAA 675
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA--------EIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 676 IPGSRAVGGSKARVQARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAER 755
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 756 VRAELSEGQRQLRE----LEGKEPQDAGERSRLQEFRRRVAAAQSQVQVL----KEKKQATERLVSLSAQSEKRLQELER 827
Cdd:TIGR02168 857 LAAEIEELEELIEEleseLEALLNERASLEEALALLRSELEELSEELRELeskrSELRRELEELREKLAQLELRLEGLEV 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 828 NVQLMRQQQGQLQRRLREETEQK-RRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFqrkrrsgsnGSV--VSLE 904
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLE--------------NKIKEL---------GPVnlAAIE 993
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622954645 905 QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKR 940
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
774-1031 |
7.87e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 774 EPQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK-R 851
Cdd:COG4913 219 EEPDTFEAaDALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 852 RLEAEMSKRQHRVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 931
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 932 ELGEELHkreailakkEALMQEKTGLESKRLRSSQALNEdivrvssrlehlEKELSEKNGQLRQGSAQSQQQIRREIDSL 1011
Cdd:COG4913 366 ALLAALG---------LPLPASAEEFAALRAEAAALLEA------------LEEELEALEEALAEAEAALRDLRRELREL 424
|
250 260
....*....|....*....|
gi 1622954645 1012 RQEKDSLLKQRLEIDSKLRQ 1031
Cdd:COG4913 425 EAEIASLERRKSNIPARLLA 444
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1198 |
9.66e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 850 KRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQRR 928
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrELSSLQSELRRIENRLDELSQELSDA-----------SRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 929 ALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEkngqlrqgsaQSQQQIRREI 1008
Cdd:TIGR02169 738 RLEELEEDL---SSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDLEARLSH----------SRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1009 DSLRQEKDSLLKQRLEIDSKLRQgslLSPEEErtlfQLDEAIEALDAAIEYKNEAITCRQRVLRasasllsqcemNLMAK 1088
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNR---LTLEKE----YLEKEIQELQEQRIDLKEQIKSIEKEIE-----------NLNGK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1089 LsylssSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1168
Cdd:TIGR02169 863 K-----EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
330 340 350
....*....|....*....|....*....|
gi 1622954645 1169 LQQSRDHLSEGLADSRRQYEARIQALEKDL 1198
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
750-1196 |
9.69e-06 |
|
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: 50.17 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 750 EQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEfrrrvaAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 829
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 830 qlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 909
Cdd:pfam01576 85 --------------EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 910 EEQKKWLDQEMEKVLQQRRALEELGEEL----HKREAI-------LAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 978
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLsklkNKHEAMisdleerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 979 LEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDsLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1058
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1059 YKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFSELEMQLEEQQRLVYW 1138
Cdd:pfam01576 310 DTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALEELTEQLEQAKRNKAN 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954645 1139 LE---VALERQRLEMDRQL-TLQQ--KEHEQNMQLLLQQSRDhLSEGLADSRRQYEARIQALEK 1196
Cdd:pfam01576 375 LEkakQALESENAELQAELrTLQQakQDSEHKRKKLEGQLQE-LQARLSESERQRAELAEKLSK 437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
731-1063 |
1.00e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 731 TGKAAQALNRQHSQRIRELEQEAERVRAelSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVlkEKKQATER 810
Cdd:PTZ00121 1108 TGKAEEARKAEEAKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA--KKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 811 LVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAemskrQHRVKELELKHEQQQKILKIKT-EEIAAFQ 889
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEERNnEEIRKFE 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 890 RKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELHKREAILAKKEAlMQEKTGLESKRLRSSQALN 969
Cdd:PTZ00121 1259 EARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 970 EDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQiRREIDSLRQE----KDSLLKQRLEIDSKLRQGSLLSPEEERTLFQ 1045
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
330
....*....|....*...
gi 1622954645 1046 LDEAIEALDAAIEYKNEA 1063
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKA 1427
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
743-1195 |
1.28e-05 |
|
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: 49.73 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 743 SQRIRELEQEAERVRAELSEGQRQLRELEGkEPQDAGERsRLQEFRRRVAAAQSQVQV----LKEKKqATERLVSLSAQS 818
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKS-ESQNKIEL-LLQQHQDRIEQLISEHEVeitgLTEKA-SSARSQANSIQS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 819 EKRL-QELERNvqlmRQQQGQLQRRLREETEQKRRLEAEMSKRQHrvkelELKHEQQQKILKIKTEEIAAFQRKRRSGSN 897
Cdd:pfam15921 300 QLEIiQEQARN----QNSMYMRQLSDLESTVSQLRSELREAKRMY-----EDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 898 GSVVSLEQQQKI---------------EEQKKWLDQEMEKVL---QQRRALEELGEELHKREAILakkEALMQEKTGLES 959
Cdd:pfam15921 371 ESGNLDDQLQKLladlhkrekelslekEQNKRLWDRDTGNSItidHLRRELDDRNMEVQRLEALL---KAMKSECQGQME 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 960 KRLRSSQALNEDIVRVSSRLEHLEkelsekngqlrqgsaQSQQQIRREIDSLRQEKDSLlkqrleidsklrqgsllsPEE 1039
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQLE---------------STKEMLRKVVEELTAKKMTL------------------ESS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1040 ERTLFQLDEAIEALDAAIEYKNEAITcrqrVLRASASLLSQCEMNLMAKLSYLSSSETRallCKyfdkvvTLREEQHQQQ 1119
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEIT----KLRSRVDLKLQELQHLKNEGDHLRNVQTE---CE------ALKLQMAEKD 561
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 1120 IAFSELEMQLEEQQRLVYwlevalERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQALE 1195
Cdd:pfam15921 562 KVIEILRQQIENMTQLVG------QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
747-1027 |
1.48e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 747 RELEQE-----AERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKR 821
Cdd:PRK03918 443 RELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 822 LQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFQRKRRSGSNGSVV 901
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE--------------EELAELLKELEELGFESVE 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 902 SLEQQ-QKIEE-QKKWL---DQEMEKVLQQRRaLEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQalnEDIVRV 975
Cdd:PRK03918 589 ELEERlKELEPfYNEYLelkDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKeLEELEKKYSE---EEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622954645 976 SSRLEHLEKELSEKNGQLrQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDS 1027
Cdd:PRK03918 665 REEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
694-1025 |
1.53e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 694 VPSATASEWRLAQAQQKIRELainIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGK 773
Cdd:pfam07888 26 VPRAELLQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 774 EPQDAGERSRLQEFRRRVAAAQsqvqvlkekkqaterlvslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 853
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQR--------------------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 854 EAEMSKRQHRVKELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL 933
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 934 GEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKNGQLRQGSAQSQQQIRREIDSL 1011
Cdd:pfam07888 240 RSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330
....*....|....
gi 1622954645 1012 RQEKDSLLKQRLEI 1025
Cdd:pfam07888 314 EADKDRIEKLSAEL 327
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
918-1058 |
1.74e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 918 QEMEKVLQQRRALE---ELGEELHKREAILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 982
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 983 EKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1058
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
935-1194 |
2.05e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 935 EELHKREAILAKKEALMQEKTGLeSKRLRSSQALNEDIVRVSSRLEHLEKELsekngqlrQGSAQSQQQIRREIDSLRQE 1014
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1015 KDSLLKQRLEIDSkLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSS 1094
Cdd:PRK11281 110 NDEETRETLSTLS-LRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1095 SETRAllckyfdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQL--LLQQS 1172
Cdd:PRK11281 168 NSQRL------------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQ 228
|
250 260
....*....|....*....|..
gi 1622954645 1173 RDHLSEGLAdsrrQYEARIQAL 1194
Cdd:PRK11281 229 RDYLTARIQ----RLEHQLQLL 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
705-1191 |
2.05e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 705 AQAQQKIRElaINIRMKEELIGELVRTGKAAQALNRQHSQRiRELEQEAERVR------AELSEGQRQLR-ELEGKEPQD 777
Cdd:TIGR00606 545 MDKDEQIRK--IKSRHSDELTSLLGYFPNKKQLEDWLHSKS-KEINQTRDRLAklnkelASLEQNKNHINnELESKEEQL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 778 A-------------GERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSA--------------QSEKRLQELERNVQ 830
Cdd:TIGR00606 622 SsyedklfdvcgsqDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 831 LMRQQQgqlqrrlreETEQKRrLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVvslEQQQKIE 910
Cdd:TIGR00606 702 SKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ---RLKNDIE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 911 EQKKWL-----DQEMEKVLQQR-RALEELGEELHKREAILAKKEALMQEKTGleskrLRSSQALNEdivRVSSRLEHLEK 984
Cdd:TIGR00606 769 EQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL-----DRTVQQVNQ---EKQEKQHELDT 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 985 ELSEknGQLRQGSAQSQQQirrEIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1064
Cdd:TIGR00606 841 VVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1065 TCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTLREEQ-HQQQIAFSELEMQLEEQQRLVYW 1138
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEK 995
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622954645 1139 LEVALERQRLEMDRQltlQQKEHEQNMQLLLQQSRDHLSEgLADSRRQYEARI 1191
Cdd:TIGR00606 996 INEDMRLMRQDIDTQ---KIQERWLQDNLTLRKRENELKE-VEEELKQHLKEM 1044
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
703-1213 |
2.24e-05 |
|
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: 48.95 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINI----RMKEELIGElvrtgkaaqalNRQ--HSQR--IRELEQEAERVRAELSEG----------- 763
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIeaelKQKENKLQE-----------NRKiiEAQRkaIQELQFENEKVSLKLEEEiqenkdliken 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 764 --QRQLRELEGKEPQDAGERSRLQEFRR------------------------RVAAAQSQVQVLKEKKQATERLVSLSAQ 817
Cdd:pfam05483 151 naTRHLCNLLKETCARSAEKTKKYEYEReetrqvymdlnnniekmilafeelRVQAENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 818 SEKRLQELERNVQLMRQQQGQLQRRLREET-------------EQKRRLEAE-----MSKRQHRVKELE-LKHEQQQKI- 877
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTflleesrdkanqlEEKTKLQDEnlkelIEKKDHLTKELEdIKMSLQRSMs 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 878 --------LKIKTEEIAAFQRKRRSGS-----------------NGSVVSLE-----QQQKI---EEQKKWLDQEMEKvl 924
Cdd:pfam05483 311 tqkaleedLQIATKTICQLTEEKEAQMeelnkakaahsfvvtefEATTCSLEellrtEQQRLeknEDQLKIITMELQK-- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 925 qQRRALEELGE-------ELHKREAILAKKEALMQEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKNGQLrQGS 997
Cdd:pfam05483 389 -KSSELEEMTKfknnkevELEELKKILAEDEKLLDEKKQFE----KIAEELKGKEQELIFLLQAREKEIHDLEIQL-TAI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 998 AQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLlspeEERTLFQldeaiEALDAAIEYKNEA---ITCRQRVLRAS 1074
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL----ENKELTQ-----EASDMTLELKKHQediINCKKQEERML 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1075 ASL--LSQCEMNLMAKLSYlsssetrallckyfdkvvtLREEQHQQQiafSELEMQL---EEQQRLVYWLEVALERQRLE 1149
Cdd:pfam05483 534 KQIenLEEKEMNLRDELES-------------------VREEFIQKG---DEVKCKLdksEENARSIEYEVLKKEKQMKI 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622954645 1150 MDRQ---LTLQQKEHEQNMQLLLQQSRDHLSEGLADSRR--QYEARIQALEKDLgrymwinQELKQKLG 1213
Cdd:pfam05483 592 LENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELEL-------ASAKQKFE 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
964-1198 |
3.27e-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: 47.84 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 964 SSQALNEDIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRqgsllspEEERTL 1043
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1044 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1122
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622954645 1123 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNMQLLLQQSRDHLSE--GLADSRRQYEARIQALEKDL 1198
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
741-1055 |
5.60e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 741 QHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSR---LQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSA 816
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 817 QSE----------KRLQELERNVQLMRQQQGQLQRrlreetEQKRRLEAEMSKrqhrvkeLELKHEQQQKILKIKTEEIA 886
Cdd:PRK11281 157 QPEraqaalyansQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 887 AFQrKRRSGSNgsvvslEQQQKIEEQKkwldQEMEKVLQQRRAleELGEElHKREAILAKKEALMQEKTgLESKRLRSSQ 966
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQL----QLLQEAINSKRL--TLSEK-TVQEAQSQDEAARIQANP-LVAQELEINL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 967 ALNEDIVRVSSRLehleKELSEKNGQLRQ---GSAQSQQQIRREIDSLR----------QEKDSL----LKQRL--EI-D 1026
Cdd:PRK11281 289 QLSQRLLKATEKL----NTLTQQNLRVKNwldRLTQSERNIKEQISVLKgslllsrilyQQQQALpsadLIEGLadRIaD 364
|
330 340 350
....*....|....*....|....*....|
gi 1622954645 1027 SKLRQGSLlspEEER-TLFQLDEAIEALDA 1055
Cdd:PRK11281 365 LRLEQFEI---NQQRdALFQPDAYIDKLEA 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
701-1162 |
6.20e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 701 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGE 780
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 781 RSRLQEFRRRVAAAQSQvQVLKEKKQATERLVSLSA---QSEKRLQELERNVQL-------MRQQQGQLQRRLREETEQK 850
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLE-ELREERDELREREAELEAtlrTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 851 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsVVSLEQQQKIEEQKkwLDQEMEKVLQQRRAL 930
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDR----------------IERLEERREDLEEL--IAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 931 EELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK-----ELSEKNGQlRQGSAQSQQQIR 1005
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllAAIADAED-EIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1006 REIDSLRQEKDSLLKQRL-EIDSKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCE-- 1082
Cdd:PRK02224 619 AELNDERRERLAEKRERKrELEAEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEel 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1083 ----MNLMAKLSYLSS--SETRALLCKYFDkvvtLREEQHQQQIafSELEMQLEEQQRLVYWLEvALERQRLEMDRQLTL 1156
Cdd:PRK02224 697 rerrEALENRVEALEAlyDEAEELESMYGD----LRAELRQRNV--ETLERMLNETFDLVYQND-AYSHIELDGEYELTV 769
|
....*.
gi 1622954645 1157 QQKEHE 1162
Cdd:PRK02224 770 YQKDGE 775
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
703-829 |
6.88e-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: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIGELVRTGkAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERS 782
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622954645 783 R-LQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 829
Cdd:COG3206 313 RiLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
804-1154 |
9.66e-05 |
|
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: 46.89 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 804 KKQATERLVSLSAQSEKRLQELERNVQL--MRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIK 881
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 882 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKR 961
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE--ELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 962 LRSS------QALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLL 1035
Cdd:pfam02463 307 RRKVddeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1036 SPEEERTLFQLDEAIEALDAAieykNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQ 1115
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEA----QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622954645 1116 HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL 1154
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
785-1030 |
1.64e-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: 46.37 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 785 QEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 863
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 864 VKELELKHEQQQKILKIKTEeiAAFQRKRRSGSNGSVVSLEQQQKIEEQKK----WLDQEMEKVLQQRRA---------- 929
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQ--AWLEEQKEQKREARTEKQAYWQVVEGALDaqlaLLKAAIAARRSGAKAelkaletwyk 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 930 --LEELG---EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV----RVSSRLEHLEKELSEKNGQLrqgsAQS 1000
Cdd:pfam12128 758 rdLASLGvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQL----ARL 833
|
250 260 270
....*....|....*....|....*....|
gi 1622954645 1001 QQQIRREIDSLRQEKDSLLKQRLEIDSKLR 1030
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 ... |
703-1052 |
1.90e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEEligELvrtgKAAQAlnrqhsqrirELEQEAervrAELSEGQRQLRELEgkepqdaGERS 782
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEE---EL----QAALA----------RLEEET----AQKNNALKKIRELE-------AQIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 783 RLQEFRRRVAAAQSQVQvlKEKKQATERLVSLSAqsekrlqELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 862
Cdd:pfam01576 275 ELQEDLESERAARNKAE--KQRRDLGEELEALKT-------ELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 863 RVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKVLQQRRALEElgeelHKRE 941
Cdd:pfam01576 346 QLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RTLQQAKQDSE-----HKRK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 942 ailaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQ-----GSAQSQQQirrEIDSLRQEKD 1016
Cdd:pfam01576 409 ----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvSSLESQLQ---DTQELLQEET 481
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622954645 1017 sllKQRLEIDSKLRQgsllsPEEERT--LFQLDEAIEA 1052
Cdd:pfam01576 482 ---RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
728-860 |
2.03e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 728 LVRTGKAAQALNRQHSQ----------RIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGERSRLQEFRRRVAAAQsQ 797
Cdd:PRK09510 54 MVDPGAVVEQYNRQQQQqksakraeeqRKKKEQQQAEELQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALK-Q 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954645 798 VQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 860
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
745-1196 |
2.33e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 745 RIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQ-----------EFRRRVAAAQSQVQVL-KEKKQATERLV 812
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 813 SLSAQ------SEKRLQELeRNVQLMRQQQGQLQRRLREETEQ-----KRRLEAEMSKRQHRVKELELKHEQQQKILKIK 881
Cdd:pfam01576 163 EFTSNlaeeeeKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 882 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE----ELGEELH------------------- 938
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEkqrrDLGEELEalkteledtldttaaqqel 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 939 --KREAILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKNgqlRQGSAQSQQQIRREID 1009
Cdd:pfam01576 322 rsKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1010 SLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKL 1089
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1090 SYLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNMQLL- 1168
Cdd:pfam01576 475 ELL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLe 541
|
490 500
....*....|....*....|....*....
gi 1622954645 1169 -LQQSRDHLSEGLADSRRQYEARIQALEK 1196
Cdd:pfam01576 542 aLEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
795-1063 |
2.68e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 795 QSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 874
Cdd:COG1340 7 SSSLEELEEKI---EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 875 QKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQEMEKVLQQRraLEELGEELHKREAILAKKEA 949
Cdd:COG1340 84 NEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPEEEKELVEK--IKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 950 LMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKNGQLRqgsaQSQQQIRREIDSLRQEKDSLLKQRLEIDSKL 1029
Cdd:COG1340 162 LKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----EEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270
....*....|....*....|....*....|....
gi 1622954645 1030 RQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1063
Cdd:COG1340 226 DE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
846-988 |
3.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 846 ETEQKRRLEAEMSKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 924
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954645 925 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 988
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
720-1234 |
3.58e-04 |
|
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: 45.11 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 720 MKEELIGELVRTGKAAQALNR---QHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQS 796
Cdd:pfam15921 438 MKSECQGQMERQMAAIQGKNEsleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 797 QV-----------QVLKEKKQATERLVSLSAQSE----------KRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEA 855
Cdd:pfam15921 518 EItklrsrvdlklQELQHLKNEGDHLRNVQTECEalklqmaekdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 856 EMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSGSNGSvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 934
Cdd:pfam15921 598 EINDRRLELQEFKiLKDKKDAKIRELEARVSDLELEKVKLVNAGS----ERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 935 EELHKREAILAKKEALMQEKTGLESKRLRSSQalnedivrvsSRLEHLEKELSEKNGQlrQGSAQsqqqirreidslrqe 1014
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ----------SELEQTRNTLKSMEGS--DGHAM--------------- 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1015 KDSLLKQRlEIDSKLRQgsllspeeertlfqldeaIEALDAAIEYKNEAITC---RQRVLRASASLLSQ------CEMNL 1085
Cdd:pfam15921 727 KVAMGMQK-QITAKRGQ------------------IDALQSKIQFLEEAMTNankEKHFLKEEKNKLSQelstvaTEKNK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1086 MA-KLSYLSSSETRallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVYWLEvaLERQRLEMDRQL---TLQQKEH 1161
Cdd:pfam15921 788 MAgELEVLRSQERR------------LKEKVANMEVALDKASLQFAECQDIIQRQE--QESVRLKLQHTLdvkELQGPGY 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1162 EQNMQL---LLQQS---RDH----LSEGLADSRRQYEARIQALEKDLGRYM-WINQELKQKLGGVNTVGHSRGGEKRSLC 1230
Cdd:pfam15921 854 TSNSSMkprLLQPAsftRTHsnvpSSQSTASFLSHHSRKTNALKEDPTRDLkQLLQELRSVINEEPTVQLSKAEDKGRAP 933
|
....
gi 1622954645 1231 SEGR 1234
Cdd:pfam15921 934 SLGA 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
703-1202 |
3.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAERVRAELSEGQRQLRELEGKEpqDAGERS 782
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 783 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 862
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 863 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 923
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 924 L---------------QQRRALEE--LGEELHKREAILAKKEALMQE------------KTGLESKRLRSSQALNEDIVR 974
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPRldpdslagkldfKPHPFRAWLEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 975 VSS--RLEHLEKELSeKNGQLRQGSAQSQQQIRREIDSLR------QEKDSLLKQRLEidsklrqgsllspEEERTLFQL 1046
Cdd:COG4913 564 VDSpeELRRHPRAIT-RAGQVKGNGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELA-------------ELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1047 DEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQI 1120
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1121 AFSELEMQLE-----------EQQRLVYWLEVALER-QRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYE 1188
Cdd:COG4913 700 ELEELEEELDelkgeigrlekELEQAEEELDELQDRlEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
570
....*....|....
gi 1622954645 1189 ARIQALEKDLGRYM 1202
Cdd:COG4913 780 ARLNRAEEELERAM 793
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
744-932 |
4.47e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 744 QRIRELEQEAERVRAELSEGQRQLRELEGKEpqdAGERSRLQEFRRRVAAAQSQVQVLKEK-KQATERLvsLSAQSEKRL 822
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQL--GNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 823 QELERnvqlmrqqqgqlqrrlrEETEQKRRLeaemSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 902
Cdd:COG1579 92 EALQK-----------------EIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|
gi 1622954645 903 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE 932
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
703-988 |
5.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQAL---------NRQHSQRIRELEQEaervRAELSEGQRQLRELEGk 773
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAE----LERLDASSDDLAALEE- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 774 epQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 853
Cdd:COG4913 693 --QLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 854 EAEMSKRQHRVKelELKHEQQQKILKIkteeIAAFQRKRRSGSNGSVVSLEqqqkieeqkkwldqEMEKVLQQRRALEEL 933
Cdd:COG4913 768 RENLEERIDALR--ARLNRAEEELERA----MRAFNREWPAETADLDADLE--------------SLPEYLALLDRLEED 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622954645 934 GEELHKREAILAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 988
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
711-961 |
5.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 711 IRELAINIRMKEELIGELVRTGKAAQALnrqhSQRIRELEQEAERVRAElsEGQRQLRELEGKEPQDAGERSRLQEfrrR 790
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEA---E 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 791 VAAAQSQVQVLKEKKQATERlvSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreeteQKRRLEAEMSKRQHRVKELelk 870
Cdd:COG4913 311 LERLEARLDALREELDELEA--QIRGNGGDRLEQLER---------------------EIERLERELEERERRRARL--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 871 hEQQQKILKIKT-EEIAAFQRKRRsgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEElgeelhkreailaKKEA 949
Cdd:COG4913 365 -EALLAALGLPLpASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRDLRR-------------ELRE 423
|
250
....*....|..
gi 1622954645 950 LMQEKTGLESKR 961
Cdd:COG4913 424 LEAEIASLERRK 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
749-1026 |
1.11e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 749 LEQEAERVRAELSEGQRQLRElegkepqdagersRLQEFRRRVAAAQSQVQVLKEKKQaterLVSLSAQSEKRLQELERn 828
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE-------------QLPELRKELEEAEAALEEFRQKNG----LVDLSEEAKLLLQQLSE- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 829 vqlmrqqqgqlqrrlreeteqkrrLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQrkrrsgSNGSVVSLEQQQk 908
Cdd:COG3206 224 ------------------------LESQLAEARAELAEAEARLAALRAQLGSGPDALPELL------QSPVIQQLRAQL- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 909 ieeqkkwldQEMEkvLQQRRALEELGEELHKREAILAKKEALMQEktgLESKRLRSSQALNEDIVRVSSRLEHLEKELSE 988
Cdd:COG3206 273 ---------AELE--AELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622954645 989 KNGQLRQGSAQSQQ--QIRREIDSLRQEKDSLLKQRLEID 1026
Cdd:COG3206 339 LEARLAELPELEAElrRLEREVEVARELYESLLQRLEEAR 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
699-952 |
1.96e-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: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 699 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDA 778
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 779 GERSRLqefrrrVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE----QKRRLE 854
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 855 AEMSKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 927
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 1622954645 928 RALEELGEELHKREAILAKKEALMQ 952
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
699-1049 |
2.42e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 699 ASEWrLAQAQQKIReLAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIrELEQEAERVRAELSEGQRQLRELegkepQD 777
Cdd:COG3096 332 ASDH-LNLVQTALR-QQEKIERYQEDLEELtERLEEQEEVVEEAAEQLA-EAEARLEAAEEEVDSLKSQLADY-----QQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 778 AgersrLQEFRRRVAAAQSQVQVLKEKKQAT-------ERLVSLSAQSEKRLQELERNVQlmrqqqgqlqrrlreETEQK 850
Cdd:COG3096 404 A-----LDVQQTRAIQYQQAVQALEKARALCglpdltpENAEDYLAAFRAKEQQATEEVL---------------ELEQK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 851 RRLeAEMSKRQHRvKELEL------------KHEQQQKILKIKTEEIAAFQRkrRSGSNGSVVSLEQ----QQKIEEQKK 914
Cdd:COG3096 464 LSV-ADAARRQFE-KAYELvckiageversqAWQTARELLRRYRSQQALAQR--LQQLRAQLAELEQrlrqQQNAERLLE 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 915 WLDQEMEKVLQQRRALEELGEELH-KREAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSR----------LEHLE 983
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEaQLEELEEQAAEAVEQRSELRQQL----EQLRARIKELAARapawlaaqdaLERLR 615
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 984 KELSEKNGQLRQGSAQSQQQIRREIDsLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEA 1049
Cdd:COG3096 616 EQSGEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIERLSQPGGAEDPRLLALAER 680
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
745-935 |
2.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 745 RIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQ 823
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 824 ELERNVQLMRQQQGQLQRRLREET-----EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsng 898
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK------ 710
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622954645 899 svvslEQQQKIEEQKKWLDQEMEKV-----LQQRRALEELGE 935
Cdd:PRK03918 711 -----KELEKLEKALERVEELREKVkkykaLLKERALSKVGE 747
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
899-1186 |
2.56e-03 |
|
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: 42.03 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 899 SVVSLEQQQKIEE-QKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALnedivrvss 977
Cdd:pfam17380 283 AVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 978 RLEHLEKELSekngQLRQGSAQSQQQIRREIDSL---RQEKDSLLKQRLEIDSKLRqgsLLSPEEERTLFQLDEAIEALD 1054
Cdd:pfam17380 354 RQEERKRELE----RIRQEEIAMEISRMRELERLqmeRQQKNERVRQELEAARKVK---ILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1055 AAIEykneaiTCRQRVLRAsasllsqcemnlmaklsyLSSSETRALlckyfdKVVTLREEQHQQQIafsELEMQLEEQQR 1134
Cdd:pfam17380 427 AEQE------EARQREVRR------------------LEEERAREM------ERVRLEEQERQQQV---ERLRQQEEERK 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622954645 1135 lvywlevaleRQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQ 1186
Cdd:pfam17380 474 ----------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR 515
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
903-1196 |
3.04e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 903 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILakkealmqEKTGLESKRLRS-----SQALNEDIVR--- 974
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL--------EAAEEEVDSLKSqladyQQALDVQQTRaiq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 975 ---VSSRLEHLEK-----ELSEKNGQLRQGSAQSQQQirrEIDSLRQEkdslLKQRLEIDSKLRQgsllspeeertlfQL 1046
Cdd:COG3096 415 yqqAVQALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1047 DEAIEAL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT-- 1110
Cdd:COG3096 475 EKAYELVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaa 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1111 --LREEQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NMQLLLQQSRDHLSEGLA 1181
Cdd:COG3096 553 eeLEELLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALA 623
|
330
....*....|....*
gi 1622954645 1182 DSRRQYEARIQALEK 1196
Cdd:COG3096 624 DSQEVTAAMQQLLER 638
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
688-1022 |
3.06e-03 |
|
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: 42.04 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 688 RVQARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNrqhsQRIRELEQEAERVRAELsegQRQL 767
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLK----NELSELRRQIQRAELEL---QSTN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 768 RELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEK------------KQATERLVSLSAQSE-KRLQELERNVQLMRQ 834
Cdd:pfam05557 132 SELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAeqrikelefeiqSQEQDSEIVKNSKSElARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 835 QQGQLQRRLR------EETEQ-KRRLEAEMSKRQHRVK-ELELKHEQQQ-----------------------KILKIKTE 883
Cdd:pfam05557 212 HNKHLNENIEnklllkEEVEDlKRKLEREEKYREEAATlELEKEKLEQElqswvklaqdtglnlrspedlsrRIEQLQQR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 884 EIAAFQRKrrSGSNGSVVSLEQQQKIEEQKkwLDQEMEKVLQQRRALEE---LGEELHKREAILAK-------------K 947
Cdd:pfam05557 292 EIVLKEEN--SSLTSSARQLEKARRELEQE--LAQYLKKIEDLNKKLKRhkaLVRRLQRRVLLLTKerdgyrailesydK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 948 EALMQEKTGLESKRLRSSQALNEDI----VRVSSRLEHLEKELSEKNGQL-----------RQGSAQSQQQIRREIDSLR 1012
Cdd:pfam05557 368 ELTMSNYSPQLLERIEEAEDMTQKMqahnEEMEAQLSVAEEELGGYKQQAqtlerelqalrQQESLADPSYSKEEVDSLR 447
|
410
....*....|
gi 1622954645 1013 QEKDSLLKQR 1022
Cdd:pfam05557 448 RKLETLELER 457
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
736-1021 |
3.58e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 736 QALNRQHSQRIRELEQEAERVRAELSEGQRQL----RELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATER 810
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVsalqPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEiAVEQKKEE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 811 LVSLSAQSEK----------------RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 874
Cdd:pfam10174 533 CSKLENQLKKahnaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 875 QKILKIKTEEIAAFQRKRRSGSngsvvsleqQQKIEEQKKWLDQEMEKVLQQR-----RALEELGEELHKREAILAKKEA 949
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKG---------AQLLEEARRREDNLADNSQQLQleelmGALEKTRQELDATKARLSSTQQ 683
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622954645 950 LMQEKTG-LESKRLRSSQALNEdivRVSSRLEHLEKELSEK--NGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQ 1021
Cdd:pfam10174 684 SLAEKDGhLTNLRAERRKQLEE---ILEMKQEALLAAISEKdaNIALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
904-1076 |
3.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 904 EQQQKIEEQKKWLDQEMEKVLQQ----RRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQ------------A 967
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEynelQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 968 LNEDIVRVSSRLEHLEKeLSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLD 1047
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 1622954645 1048 EAIEALDAAIEYKNEAITCRQRVLRASAS 1076
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
783-1058 |
4.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 783 RLQEFRRRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------KRLQELErnvqlmrqqqgqlqRRLREETEQKRRLE 854
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 855 AEMSKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 931
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 932 ELGEElhkREAILAkkealmqeKTGLESKrlrssqalneDIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSL 1011
Cdd:PRK02224 290 ELEEE---RDDLLA--------EAGLDDA----------DAEAVEARREELEDRDEELRDRLEE-CRVAAQAHNEEAESL 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622954645 1012 RQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1058
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
793-1207 |
4.26e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 793 AAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKEL-ELKH 871
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMtKFKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 872 EQQQKILKIKT----EEIAAFQRKrrsgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRaleelgEELHKRE----AI 943
Cdd:pfam05483 402 NKEVELEELKKilaeDEKLLDEKK-------------QFEKIAEELKGKEQELIFLLQARE------KEIHDLEiqltAI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 944 LAKKEALMQE----KTGLESKRLRSSQAL---------NEDIVRVSSRL-----EHLEKELSEKNGQLR-----QGSAQS 1000
Cdd:pfam05483 463 KTSEEHYLKEvedlKTELEKEKLKNIELTahcdkllleNKELTQEASDMtlelkKHQEDIINCKKQEERmlkqiENLEEK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1001 QQQIRREIDSLRQEkdsLLKQRLEIDSKL-------RQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRA 1073
Cdd:pfam05483 543 EMNLRDELESVREE---FIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1074 sasllsqcemnlmakLSYLSSSETRALLCkYFDKVVTLREEQHQQQIAFSEL----EMQLEEQQRLVYWLEVALERQRLE 1149
Cdd:pfam05483 620 ---------------LKKKGSAENKQLNA-YEIKVNKLELELASAKQKFEEIidnyQKEIEDKKISEEKLLEEVEKAKAI 683
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622954645 1150 MDRQLTLQQKeheqnMQLLLQQSRDHLSEGLADSRRQYEARIQALEKDLGRYMWINQE 1207
Cdd:pfam05483 684 ADEAVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
921-1195 |
4.36e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 921 EKVLQQRRAL----EELGEELHKREAILAKKEALMQEKTGLE------SKRLRSSQA---LNEDIVRVSSRLEHLEKELS 987
Cdd:PRK04863 286 EEALELRRELytsrRQLAAEQYRLVEMARELAELNEAESDLEqdyqaaSDHLNLVQTalrQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 988 EKNgQLRQGSAQSQQQIRREIDSLRQEKDSLLKQ------RLEIDSK-----------LRQGSLLSPEEERTLFQLDEAI 1050
Cdd:PRK04863 366 EQN-EVVEEADEQQEENEARAEAAEEEVDELKSQladyqqALDVQQTraiqyqqavqaLERAKQLCGLPDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1051 EALDAAIEYKNEAITCRQRVLRASASLLSQCE--MNLMAKL----SYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSE 1124
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqaYQLVRKIagevSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSE 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622954645 1125 LEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLllqqsrDHLSEGLADSRRQYEARIQALE 1195
Cdd:PRK04863 525 LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL------ESLSESVSEARERRMALRQQLE 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
903-1064 |
4.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 903 LEQQQKIEEQKKWLDQEMEKVLQQ----RRALEELGEELHKREAILAKKEALMQEKTGLE---SKRLRSSQALNEDIVRV 975
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREineiSSELPELREELEKLEKEVKELEELKEEIEELEkelESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 976 SSRLEHLEKELSEkngqlrqgsaqsQQQIRREIDSLRQEKDS---LLKQRLEIDSKLRQGSllspEEERTLFQLDEAIEA 1052
Cdd:PRK03918 265 EERIEELKKEIEE------------LEEKVKELKELKEKAEEyikLSEFYEEYLDELREIE----KRLSRLEEEINGIEE 328
|
170
....*....|..
gi 1622954645 1053 LDAAIEYKNEAI 1064
Cdd:PRK03918 329 RIKELEEKEERL 340
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
715-1063 |
4.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 715 AINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQdagERSRLQEFRRRVAAA 794
Cdd:COG4372 23 GILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE---LNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 795 QSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE---LKH 871
Cdd:COG4372 100 QEELESLQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqelQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 872 EQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL-GEELHKREAILAKKEAL 950
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALlDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 951 MQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLR 1030
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|...
gi 1622954645 1031 QGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1063
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
791-923 |
4.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 791 VAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrLREETEQ-KRRLEAEMSKRQHRVKELE 868
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 869 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV 923
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKK 623
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
703-970 |
5.88e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 703 RLAQAQQKIRELAINIRMKEELIGELVRTGKaaqalNRQHSQRIRELE--------QEAERVRAELSEGQRQLRELEGKE 774
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEeklkkynlEELEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 775 PQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATER-LVSLSAQS----EKRLQELE---------RNVQLMRQQQGQLQ 840
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeLEELGFESveelEERLKELEpfyneylelKDAEKELEREEKEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 841 RRLREETEQKRrleAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEM 920
Cdd:PRK03918 622 KKLEEELDKAF---EELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622954645 921 EKVLQQRRALEELGEELHKREAILAKKEALmQEKTgLESKRLRSSQALNE 970
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEEL-REKV-KKYKALLKERALSK 744
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
740-1024 |
6.24e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 740 RQHSQRIRELEQEAERVRAELSEGQRQLRELE---GKEPQDAGERSRLQE----FRRRVAAAQSQVQVLKEK-KQA---- 807
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELElevLKQAQSIKSQNSLQEklaqEKSRVADAEEKILELQQKlEHAhkvc 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 808 -TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRL------REETEQKRR--------LEAEMSKRQHRVKELELKHE 872
Cdd:pfam15742 145 lTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRklldqnVNELQQQVRslqdkeaqLEMTNSQQQLRIQQQEAQLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 873 QQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELHKReailakKEALM 951
Cdd:pfam15742 225 QLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEKHH 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954645 952 QEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQsQQQIRREIDSLRQEKDSLLKQRLE 1024
Cdd:pfam15742 281 HHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| COG5223 |
COG5223 |
Uncharacterized conserved protein [Function unknown]; |
851-1029 |
6.65e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 227548 [Multi-domain] Cd Length: 240 Bit Score: 40.01 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 851 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTE-------EIAAFQRKRRSGSNGSVVSLEQQQKIEEQ---KKWLDQEM 920
Cdd:COG5223 23 RRKYGKLEKKKDYVKRAQDINKKQDELKKLREKarernpdEYYHGMHSVKTDGGVSSIYREDEPTIMDLakmLKTQDNEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 921 EKVLQQ--RRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSA 998
Cdd:COG5223 103 QRCRRKleRYKPMPCGTQIKFEESSLHTIFVDMRFGQK-EFIPEEFFRTTEELVVRRENRLEKDQIENNELEDSVFSGKL 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1622954645 999 QSQQQIRREID-SLRQEKDSLLK---QRLEIDSKL 1029
Cdd:COG5223 182 HSKLKEKAATElLLRQKRDKKLAaaeERVELDRLL 216
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
819-1194 |
7.00e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 819 EKRLQELERNvqlmrqqqgqlqrrLREETEQKRRLEAEMSKRQHRVKELELKHEQ----QQKILKIKTEEIAAFQrkrrs 894
Cdd:pfam03528 7 QQRVAELEKE--------------NAEFYRLKQQLEAEFNQKRAKFKELYLAKEEdlkrQNAVLQEAQVELDALQ----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 895 gsngsvVSLEQQQkieeqkkwldQEMEKVlqqrRALEELGEELhKREAILAKKEALMQEKTGLeskrlrssQALNEDIVR 974
Cdd:pfam03528 68 ------NQLALAR----------AEMENI----KAVATVSENT-KQEAIDEVKSQWQEEVASL--------QAIMKETVR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 975 VSSRLEH--LEKELSEKNgQLRQGSAQSQQQIRREIDSLRQEK--DSLLKQRLEIDSKLRqgSLLSPEEERTLFQLDEAI 1050
Cdd:pfam03528 119 EYEVQFHrrLEQERAQWN-QYRESAEREIADLRRRLSEGQEEEnlEDEMKKAQEDAEKLR--SVVMPMEKEIAALKAKLT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1051 EALDAAIEYKNEAITCRQRVLRASASLLSQCEMnLMAKLSYLSS--SETRALLCKYFDKVVTLREEQHQQQI----AFSE 1124
Cdd:pfam03528 196 EAEDKIKELEASKMKELNHYLEAEKSCRTDLEM-YVAVLNTQKSvlQEDAEKLRKELHEVCHLLEQERQQHNqlkhTWQK 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1125 LEMQLEEQQRLvywLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQAL 1194
Cdd:pfam03528 275 ANDQFLESQRL---LMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAV 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
859-1021 |
7.31e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 859 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 937
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 938 HKREAILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKNGQLrQGSAQSQQQIRREIDSLRQE-- 1014
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEea 155
|
....*..
gi 1622954645 1015 KDSLLKQ 1021
Cdd:PRK12704 156 KEILLEK 162
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
725-1171 |
7.66e-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: 40.51 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 725 IGELVRTGKAAQALNRQHSQRIRELEQEAERVRA--------ELSEGQRQLRELEGKEPQDAgersrLQEFRRRVAAAQS 796
Cdd:pfam07111 189 AKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESlrkyvgeqVPPEVHSQTWELERQELLDT-----MQHLQEDRADLQA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 797 QVQVLKEKKQATERLVSLSAQS-EKRLQELERNVQLMRQQQGQLQRRLREET------EQKRRLEAEMSKRQHRVKELEL 869
Cdd:pfam07111 264 TVELLQVRVQSLTHMLALQEEElTRKIQPSDSLEPEFPKKCRSLLNRWREKVfalmvqLKAQDLEHRDSVKQLRGQVAEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 870 KHE-----QQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQK-----------IEEQKK-----------WLDQEMEK 922
Cdd:pfam07111 344 QEQvtsqsQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEarrrqqqqtasAEEQLKfvvnamsstqiWLETTMTR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 923 VLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRS---SQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQ 999
Cdd:pfam07111 424 VEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScppPPPAPPVDADLSLELEQLREERNRLDAELQLSAHL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1000 SQQQIRREIDSLRQEKDSLLK--QRLEIDSKLRQGSLLSPEEertlfQLDEAI----EALDAAIEYKNEAITCRQRVLRA 1073
Cdd:pfam07111 504 IQQEVGRAREQGEAERQQLSEvaQQLEQELQRAQESLASVGQ-----QLEVARqgqqESTEEAASLRQELTQQQEIYGQA 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1074 SASLLSQCEMNLMAKLSYLSS--SETRALLCKyfdKVVTLREEQHQ--QQIAFSELEMQLEEQQRLVYWLEVALERQRLE 1149
Cdd:pfam07111 579 LQEKVAEVETRLREQLSDTKRrlNEARREQAK---AVVSLRQIQHRatQEKERNQELRRLQDEARKEEGQRLARRVQELE 655
|
490 500
....*....|....*....|..
gi 1622954645 1150 MDRQLTLQQKEHEQNMQLLLQQ 1171
Cdd:pfam07111 656 RDKNLMLATLQQEGLLSRYKQQ 677
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
745-829 |
8.80e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.10 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 745 RIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQE 824
Cdd:pfam00529 66 QLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVT 145
|
....*
gi 1622954645 825 LERNV 829
Cdd:pfam00529 146 AGALV 150
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
751-1056 |
8.86e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 751 QEAERVRAELSEGQRQLR-ELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERlVSLSAQSEKRLQELERNv 829
Cdd:pfam01576 422 SESERQRAELAEKLSKLQsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR-QKLNLSTRLRQLEDERN- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 830 qlmrqqqgQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 909
Cdd:pfam01576 500 --------SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 910 EEQKKWLDQEMEKVL----QQRRALEELGEELHKREAILAKKEALmqeKTGLESKRLRSSQALNEDIVRVSSRLEHLEKE 985
Cdd:pfam01576 572 EKTKNRLQQELDDLLvdldHQRQLVSNLEKKQKKFDQMLAEEKAI---SARYAEERDRAEAEAREKETRALSLARALEEA 648
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622954645 986 LSEKNGQLRQgsaqsQQQIRREIDSLRQEKDSLLKQRLEIDsKLRQGSLLSPEEERTlfQLDEAIEALDAA 1056
Cdd:pfam01576 649 LEAKEELERT-----NKQLRAEMEDLVSSKDDVGKNVHELE-RSKRALEQQVEEMKT--QLEELEDELQAT 711
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
755-1177 |
8.88e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 755 RVRAELSEgqRQLRELegkepqdageRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSE---KRLQ---ELERN 828
Cdd:pfam05622 86 RIKCEELE--KEVLEL----------QHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVEtykKKLEdlgDLRRQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 829 VQLMRQQQGQLQRRLREETEQKRRLEA-----EMSKRQhrVKELELKHEQQQKilkiKTEEiAAFQRKrrsgsngsvvsl 903
Cdd:pfam05622 154 VKLLEERNAEYMQRTLQLEEELKKANAlrgqlETYKRQ--VQELHGKLSEESK----KADK-LEFEYK------------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 904 eqqqKIEEQKKWLDQEMEKVLQQRRALEELGEELH---------KREAILAKKEALMQEKTG----------------LE 958
Cdd:pfam05622 215 ----KLEEKLEALQKEKERLIIERDTLRETNEELRcaqlqqaelSQADALLSPSSDPGDNLAaeimpaeireklirlqHE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 959 SKRLRSSQ--ALNEDIVRVSSRLEHLEKELSEKNGQLRQgsaqSQQQIRreidSLRQEKDSLLKQRLEIDSKLRQGSLLS 1036
Cdd:pfam05622 291 NKMLRLGQegSYRERLTELQQLLEDANRRKNELETQNRL----ANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 1037 PEEERTLFQLDEAIEALDAAIEYKNEAitcRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQH 1116
Cdd:pfam05622 363 QKLEEHLEKLHEAQSELQKKKEQIEEL---EPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPK 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954645 1117 QQQIAFSE---LEMQLEEQQRLVYWLEVALERQRL--EMDRQL----------TLQQKEHEQNMQLLLQQSRDHLS 1177
Cdd:pfam05622 440 QNPASPPEiqaLKNQLLEKDKKIEHLERDFEKSKLqrEQEEKLivtawynmgmALHRKAIEERLAGLSSPGQSFLA 515
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
694-899 |
9.52e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 694 VPSATASEWRLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELSEGQRQLREL 770
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954645 771 EgkepQDAGERSR--------------------LQEFRRRVAA----AQSQVQVLKEKKQATERLVSLSAQSEKRLQELE 826
Cdd:COG3883 85 R----EELGERARalyrsggsvsyldvllgsesFSDFLDRLSAlskiADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954645 827 RNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGS 899
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| |
