|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
15-350 |
1.20e-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: 1.20e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRITLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYG 94
Cdd:cd01372 2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 95 QTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTASR-DIQLREDE 172
Cdd:cd01372 82 QTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKkKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKpTISIREDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 173 HGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSRLPRPAQGQL--LVSKFHF 250
Cdd:cd01372 162 KGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNstFTSKFHF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 251 VDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:cd01372 242 VDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 321
|
330 340
....*....|....*....|
gi 1622954647 331 SDFDETLNTLNYASRAQNIR 350
Cdd:cd01372 322 SNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
15-356 |
7.92e-139 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 426.99 E-value: 7.92e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRIT-------LGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLtvrspknRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 88 ATVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLevGTASRD 165
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMiGT-------PDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLL--NPSSKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 166 IQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSRlprpaqGQLLV 245
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS------GSGKA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:smart00129 226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKS-RHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304
|
330 340 350
....*....|....*....|....*....|.
gi 1622954647 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
21-349 |
5.82e-135 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 416.59 E-value: 5.82e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 21 RVRPLLPKELLHGHQSCLQVEPGLGRITL-------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 94 GQTGSGKTYTMGEasvaslLEDEQGIVPRAMAEAFKLIDEN-DLLDCLVHVSYLEVYKEEFRDLLEVGTAS-RDIQLRED 171
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTkERSEFSVKVSYLEIYNEKIRDLLSPSNKNkRKLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 172 EHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSrlprpAQGQLLVSKFHFV 251
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTG-----GEESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 252 DLAGSERVLKTG-STGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSS 330
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS--KHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSS 307
|
330
....*....|....*....
gi 1622954647 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 |
1.57e-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: 1.57e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKELLHGHqSCLQVEPG------LGRITLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd00106 1 NVRVAVRVRPLNGREARSAK-SVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 89 TVFAYGQTGSGKTYTMGEASvasllEDEQGIVPRAMAEAFKLIDENDLLD--CLVHVSYLEVYKEEFRDLLEvGTASRDI 166
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKssFSVSASYLEIYNEKIYDLLS-PVPKKPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 167 QLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSrlprpaQGQLLVS 246
Cdd:cd00106 154 SLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKS------GESVTSS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgsHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd00106 228 KLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 1622954647 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 |
1.01e-107 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 344.33 E-value: 1.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELLHGHQSCLQV--------EPGLGRITL--------------GRDRHFGFHVVLAEDAGQEAVYQA 73
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVmdnhmlvfDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 74 CVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEE 152
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTM------LGTPQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 153 FRDLLEvgTASRDIQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAP 232
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 233 SRLPRPAQGQLLVskfhfVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKD 312
Cdd:cd01370 234 SINQQVRQGKLSL-----IDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622954647 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 |
1.31e-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: 1.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKEL---------LHGHQSCLQVEPGL---GRITLGRDRHFGFHVVL----AED---AGQEAVYQACVQ 76
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQAdknNKATREVPKSFSFDYSYwshdSEDpnyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 77 PLLEAFFEGFNATVFAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLID--ENDLLDCLVHVSYLEVYKEEFR 154
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT------QEQPGIIPRLCEDLFSRIAdtTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 155 DLLEVGTASRDIQLREDEH---GNVVLcGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRgRA 231
Cdd:cd01365 157 DLLNPKPKKNKGNLKVREHpvlGPYVE-DLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQK-RH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 232 PSRLPRPAQgqlLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQR-----RGSHIPYRDSKI 306
Cdd:cd01365 235 DAETNLTTE---KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSVL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622954647 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 |
1.10e-103 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 332.89 E-value: 1.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRITL--GRD------RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 88 ATVFAYGQTGSGKTYTMGEASVAsllEDEQGIVPRAMAEAFKLID-ENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRdI 166
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEGKRED---PELRGIIPNSFAHIFGHIArSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKR-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 167 QLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQrgrapSRLPRPAQGQLLVS 246
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC-----SEKGEDGENHIRVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPqrRGSHIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01371 234 KLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMCANI 311
|
330 340
....*....|....*....|...
gi 1622954647 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 |
5.57e-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: 5.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELLHG--------HQSCLQVEPGLGRitlgrdrhFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINeqvaweidNDTIYLVEPPSTS--------FTFDHVFGGDSTNREVYELIAKPVVKSALEGYN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 88 ATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGtaSRDIQ 167
Cdd:cd01374 74 GTIFAYGQTSSGKTFTM------SGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPT--SQNLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 168 LREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPsrlprPAQGQLLVSK 247
Cdd:cd01374 146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGE-----LEEGTVRVST 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 248 FHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGsHIPYRDSKITRILKDSLGGNAKTVMIACVS 327
Cdd:cd01374 221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-HIPYRDSKLTRILQPSLGGNSRTAIICTIT 299
|
330 340
....*....|....*....|..
gi 1622954647 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 |
3.04e-96 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 311.84 E-value: 3.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELlHGHQSCLQVEPGLG-RITL---GRDRH-FGFHVVLAEDAGQEAVYQAcVQPLLEAFFEGFNATV 90
Cdd:cd01366 4 IRVFCRVRPLLPSEE-NEDTSHITFPDEDGqTIELtsiGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 91 FAYGQTGSGKTYTMGEAsvasllEDEQGIVPRAMAEAFKLIDENDLLDCLVH--VSYLEVYKEEFRDLLEVGTASR---D 165
Cdd:cd01366 82 FAYGQTGSGKTYTMEGP------PESPGIIPRALQELFNTIKELKEKGWSYTikASMLEIYNETIRDLLAPGNAPQkklE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 166 IQlREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLeqRGRAPSRlprpaqGQLLV 245
Cdd:cd01366 156 IR-HDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQT------GEISV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 246 SKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGdpqRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01366 227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 1622954647 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 |
4.99e-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: 4.99e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELLHGHQSCLQVEPGLGRITL--------GRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFN 87
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 88 ATVFAYGQTGSGKTYTM-GEASVASLLEDEQ----GIVPRAMAEAFKLIDENDLlDCLVHVSYLEVYKEEFRDLLEV-GT 161
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMeGDRSPNEEYTWELdplaGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPsSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 162 ASRDIQLREDEH--GNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSrlprpA 239
Cdd:cd01364 163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID-----G 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 240 QGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDpqrRGSHIPYRDSKITRILKDSLGGNAK 319
Cdd:cd01364 238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGRTK 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622954647 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 |
3.82e-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: 3.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELLHGHQSCLQVEPGlGRITLGRD---RHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFA 92
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPE-DTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 93 YGQTGSGKTYTMgEASvaslLEDEQ--GIVPRAMAEAFKLIDEND-LLDCLVHVSYLEVYKEEFRDLLEVgtaSRD-IQL 168
Cdd:cd01369 83 YGQTSSGKTYTM-EGK----LGDPEsmGIIPRIVQDIFETIYSMDeNLEFHVKVSYFEIYMEKIRDLLDV---SKTnLSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 169 REDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRApsrlprpaQGQLLVSKF 248
Cdd:cd01369 155 HEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE--------TEKKKSGKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 249 HFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSP 328
Cdd:cd01369 227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK--THIPYRDSKLTRILQDSLGGNSRTTLIICCSP 304
|
330 340
....*....|....*....|.
gi 1622954647 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 |
1.73e-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: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLGRITLG-RDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAY 93
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 94 GQTGSGKTYTM-GEA-SVASLLEDEQGIVPRAMAEAFKLID-----ENDLLDCLVHVSYLEVYKEEFRDLLEvgTASRDI 166
Cdd:cd01373 82 GQTGSGKTYTMwGPSeSDNESPHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLD--PASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 167 QLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEqrgrapSRLPRPAQGQLLVS 246
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE------SWEKKACFVNIRTS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGD-PQRRGSHIPYRDSKITRILKDSLGGNAKTVMIAC 325
Cdd:cd01373 234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
|
330 340 350
....*....|....*....|....*....|.
gi 1622954647 326 VSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:cd01373 314 VHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
55-356 |
3.07e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 284.32 E-value: 3.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 55 FGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDEN 134
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTM------SGTEEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 135 DLLDCL-VHVSYLEVYKEEFRDLLEVGTASRDIqlREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRL 213
Cdd:COG5059 132 SMTKDFaVSISYLEIYNEKIYDLLSPNEESLNI--REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 214 SSRSHTVFTVTLEQRGRAPSRLPRpaqgqllvSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQ 293
Cdd:COG5059 210 SSRSHSIFQIELASKNKVSGTSET--------SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954647 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 |
1.64e-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: 1.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKELLHGHQSCLQVE--------------PGLGRITLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLL 79
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhppkgsaANKSERNGGQKETkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 80 EAFFEGFNATVFAYGQTGSGKTYTMgeasvaSLLEDEQGIVPRAMAEAFKLIDENDlldclVHVSYLEVYKEEFRDLLEV 159
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTM------QGSPGDGGILPRSLDVIFNSIGGYS-----VFVSYIEIYNEYIYDLLEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 160 GTASRD-----IQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGRAPSR 234
Cdd:cd01368 151 SPSSPTkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 235 LPRPAQGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRG--SHIPYRDSKITRILKD 312
Cdd:cd01368 231 DVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSKLTHLFQN 310
|
330 340 350
....*....|....*....|....*....|....*
gi 1622954647 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 |
2.82e-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: 2.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKEL---------LHGHQSCLQVEPGLG-RITLGRDRH-FGFHVVLAEDAGQEAVYQACVQPLLEAFF 83
Cdd:cd01367 1 KIKVCVRKRPLNKKEVakkeidvvsVPSKLTLIVHEPKLKvDLTKYIENHtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 84 EGFNATVFAYGQTGSGKTYTMGEASvaSLLEDEQGIVPRAMAEAFKLIDE-NDLLDCLVHVSYLEVYKEEFRDLLEVGTa 162
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKlPYKDNLGVTVSFFEIYGGKVFDLLNRKK- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 163 srDIQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLeqrgrapsrlpRPAQGQ 242
Cdd:cd01367 158 --RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-----------RDRGTN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 243 LLVSKFHFVDLAGSER-VLKTGSTGERLKESIQINSSLLALGNVISALGDPQrrgSHIPYRDSKITRILKDSL-GGNAKT 320
Cdd:cd01367 225 KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNK---AHIPFRGSKLTQVLKDSFiGENSKT 301
|
330 340
....*....|....*....|....*
gi 1622954647 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 |
4.12e-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: 4.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 15 PVRVALRVRPLLPKELLHGHQSCLQVEPGLgRITLGRDRHFG------FHVVLAEDAGQEAVYQACVQPLLEAFFEGFNA 88
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSC-SVELADPRNHGetlkyqFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 89 TVFAYGQTGSGKTYTM-GEasvasllEDEQGIVPRAMAEAFKLIDENDLLDClVHVSYLEVYKEEFRDLLEVgtASRDIQ 167
Cdd:cd01376 80 TVFAYGSTGAGKTFTMlGS-------PEQPGLMPLTVMDLLQMTRKEAWALS-FTMSYLEIYQEKILDLLEP--ASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 168 LREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEQRGR-APSRLPRpaqgqllvS 246
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERlAPFRQRT--------G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 247 KFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRgshIPYRDSKITRILKDSLGGNAKTVMIACV 326
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANI 298
|
330 340
....*....|....*....|.
gi 1622954647 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 |
1.06e-72 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 245.95 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 55 FGFHVVLaEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASlleDEQGIVPRAMAEAFKLIDEN 134
Cdd:cd01375 50 FKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPRALQQVFRMIEER 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 135 DLLDCLVHVSYLEVYKEEFRDLL----EVGTASRDIQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHL 210
Cdd:cd01375 126 PTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 211 NRLSSRSHTVFTVTLEQRGRAPSrlprpaQGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALG 290
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLS------SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622954647 291 DPQRrgSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASR 345
Cdd:cd01375 280 DKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
16-356 |
2.46e-59 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 224.81 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKEllhghQSCLQVEPGLGRITLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQ 95
Cdd:PLN03188 100 VKVIVRMKPLNKGE-----EGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 96 TGSGKTYTM-GEASVAS---LLEDEQGIVPRAMAEAFKLIDENDL------LDCLVHVSYLEVYKEEFRDLLEvgTASRD 165
Cdd:PLN03188 175 TGSGKTYTMwGPANGLLeehLSGDQQGLTPRVFERLFARINEEQIkhadrqLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 166 IQLREDEHGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNRLSSRSHTVFTVTLEqrgrapSRLPRPAQG--QL 243
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVE------SRCKSVADGlsSF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 244 LVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGS--HIPYRDSKITRILKDSLGGNAKTV 321
Cdd:PLN03188 327 KTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLGGNAKLA 406
|
330 340 350
....*....|....*....|....*....|....*
gi 1622954647 322 MIACVSPSSSDFDETLNTLNYASRAQNIRNRATVN 356
Cdd:PLN03188 407 MVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-1198 |
3.35e-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: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQ----EAERVRAELSEGQRQLRELEGKEPQDA 777
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 778 GERSRLQEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEM 856
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAElAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 857 SKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEEL 936
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 937 HKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKngQLRQGSAQSQQQIRREIDSLRQEKDS 1016
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEA--ALEAALAAALQNIVVEDDEVAAAAIE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1017 LLKQ----RLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEM--NLMAKLSY 1090
Cdd:COG1196 565 YLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAalRRAVTLAG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1091 LSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQ 1170
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
490 500
....*....|....*....|....*...
gi 1622954647 1171 SRDHLSEGLADSRRQYEARIQALEKDLG 1198
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
744-1195 |
1.44e-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: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 744 RIRELEQEAERVRAELSEGQRQLRELEGKEpqdAGERSRLQEFRRRVAAAQSQVqvlkEKKQATERLVslsaqsEKRLQE 823
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAEL---AELEAELEELRLELEELELEL----EEAQAEEYEL------LAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 824 LERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsvVSLE 903
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 904 QQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK 983
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 984 ELSEKNGQLRQ---------GSAQSQQQIRREIDSLRQEKDSLLKQR-----LEIDSKLRQGSLLSPEEERTLFQLDEAI 1049
Cdd:COG1196 454 LEEEEEALLELlaelleeaaLLEAALAELLEELAEAAARLLLLLEAEadyegFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1050 EALDAAIE-------------YKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQ 1116
Cdd:COG1196 534 AAYEAALEaalaaalqnivveDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1117 QQIAFSE-----------LEMQLEEQQRLVY-WLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRR 1184
Cdd:COG1196 614 RYYVLGDtllgrtlvaarLEAALRRAVTLAGrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490
....*....|.
gi 1622954647 1185 QYEARIQALEK 1195
Cdd:COG1196 694 ELEEALLAEEE 704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1062 |
2.36e-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: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 725 GELVRTG---------KAAQALNRQhsQRIRELEQEAERVRAELSEGQRQLRELEGK----EPQDAGERSRLQEFRRRVA 791
Cdd:TIGR02168 652 GDLVRPGgvitggsakTNSSILERR--REIEELEEKIEELEEKIAELEKALAELRKEleelEEELEQLRKELEELSRQIS 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 792 AAQSQVQVLKEKKQaterlvslsaQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHE 871
Cdd:TIGR02168 730 ALRKDLARLEAEVE----------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 872 QQQKILKIKTEEI------AAFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILA 944
Cdd:TIGR02168 800 ALREALDELRAELtllneeAANLRERLESLERRIAATERRlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 945 KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRqEKDSLLkqrLEI 1024
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS-EEYSLT---LEE 955
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622954647 1025 DSKLRQGSLLSPEE-ERTLFQLDEAIEA-----LDAAIEYKNEA 1062
Cdd:TIGR02168 956 AEALENKIEDDEEEaRRRLKRLENKIKElgpvnLAAIEEYEELK 999
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
707-1130 |
1.83e-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: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 707 QQKIREL-AINIRMKEELIGELVRTGKAAQALNRQHSQrIRELEQEAERVRAELSEGQRQLRELEGKepqdagersrLQE 785
Cdd:TIGR04523 217 ESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQ-LNQLKDEQNKIKKQLSEKQKELEQNNKK----------IKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 786 FRRRVAAAQSQVQVLKEKKQA--TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQhrv 863
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 864 KELElkhEQQQKILKIKTEEIAAFQRKRRSGSNGSvvSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELhKREAI 942
Cdd:TIGR04523 363 RELE---EKQNEIEKLKKENQSYKQEIKNLESQIN--DLESKiQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 943 LAKKE--ALMQEKTGLES-----KRLRSSQ-----ALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQ------QIR 1004
Cdd:TIGR04523 437 KNNSEikDLTNQDSVKELiiknlDNTRESLetqlkVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleekvkDLT 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1005 REIDSLRQEKDSLLKQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITcrqrvlrasaSLLSqcem 1082
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK----------SLKK---- 582
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622954647 1083 nlmaklsylSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEE 1130
Cdd:TIGR04523 583 ---------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
743-1079 |
2.24e-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: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 743 QRIRELEQEAERVRAELSEGQRQLRELEgkepqdagersrlqefrRRVAAAQsQVQVLKEKKQATERLVSLsaqseKRLQ 822
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLE-----------------RQAEKAE-RYRELKEELKELEAELLL-----LKLR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 823 ELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSL 902
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 903 EQQQKIEEQkkwLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLE 982
Cdd:COG1196 316 ERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 983 KELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1062
Cdd:COG1196 393 RAAAELAAQLEE-LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330
....*....|....*..
gi 1622954647 1063 ITCRQRVLRASASLLSQ 1079
Cdd:COG1196 472 AALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
678-1017 |
4.75e-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: 70.86 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 678 GSRVGGSKAR---VQARQVPSATASEwRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRE------- 747
Cdd:TIGR02168 659 GVITGGSAKTnssILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlar 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 748 LEQEAERVRAELSEGQRQLRELEGK----EPQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATERLVSLSAQ---SEK 819
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEieelEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELRAEltlLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 820 RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsngsv 899
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL------ 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 900 VSLEQQQKIEEQKKWLDQEMEKvlqqRRALEELGEELHKreAILAKKEALMQEKTGLEskRLRSSQALNEDIVrvssrle 979
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSEL----RRELEELREKLAQ--LELRLEGLEVRIDNLQE--RLSEEYSLTLEEA------- 956
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622954647 980 hlekelseknGQLRQGSAQSQQQIRREIDSLRQEKDSL 1017
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 |
1.36e-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: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 67 QEAVYqACVQPLLEAFFEGFN-ATVFAYGQTGSGKTYTMgeasvaslledeQGIVPRAMAEAFklidendlldclvhvSY 145
Cdd:cd01363 32 QPHVF-AIADPAYQSMLDGYNnQSIFAYGESGAGKTETM------------KGVIPYLASVAF---------------NG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 146 LEVYKEEFRDLLEvgtasrdiqlredehgnvvlcgvkEVDVEGLDEVLSLLEMGNAARhTGATHLNRLSSRSHTVFTVtl 225
Cdd:cd01363 84 INKGETEGWVYLT------------------------EITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI-- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954647 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 ... |
703-1030 |
2.15e-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: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 703 LAQAQQKIRELAINIRMKEELIGELvrtgkaaqalnrqhSQRIRELEQEAERVRAELSEGQRQLRElegKEPQDAGERSR 782
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEE---KQNEIEKLKKE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 783 LQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 862
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKL---NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 863 VKELELKHEQQQKILKIKTEEIAAFQRKrrsgsngsvvsLEQQQKIEEQKKwldQEMEKVLQQRRALEELGEELHKREA- 941
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQN-----------LEQKQKELKSKE---KELKKLNEEKKELEEKVKDLTKKISs 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 942 ILAKKEALMQEKTGLESKrLRSsqaLNEDIVRVSSRL--EHLEKELSEKNgqlrqgsaqsqqqirREIDSLRQEKDSLLK 1019
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESK-ISD---LEDELNKDDFELkkENLEKEIDEKN---------------KEIEELKQTQKSLKK 582
|
330
....*....|.
gi 1622954647 1020 QRLEIDSKLRQ 1030
Cdd:TIGR04523 583 KQEEKQELIDQ 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
711-1057 |
6.70e-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: 67.02 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 711 RELAINIRMKEeLIGELVRTGKAAQALNRQHSQRI---RELEQEAERVRAELSEGQRQLRELegkepqdageRSRLQEFR 787
Cdd:TIGR02169 633 RRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGGIlfsRSEPAELQRLRERLEGLKRELSSL----------QSELRRIE 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 788 RRVAAAQSQVQVLKEKkqaTERLvslsaqsEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 867
Cdd:TIGR02169 702 NRLDELSQELSDASRK---IGEI-------EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 868 LK-HEQQQKILKIKT-------EEIAA---FQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEE 935
Cdd:TIGR02169 772 EDlHKLEEALNDLEArlshsriPEIQAelsKLEEEVSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 936 LHKR-EAILAKKEALMQEktgLESKRLRSSQalnedivrVSSRLEHLEKELSEKNGQLRQ-----GSAQSQQQIRREIDS 1009
Cdd:TIGR02169 852 IEKEiENLNGKKEELEEE---LEELEAALRD--------LESRLGDLKKERDELEAQLRElerkiEELEAQIEKKRKRLS 920
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622954647 1010 LRQEKDSLLKQRL-EIDSKLRQGSlLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:TIGR02169 921 ELKAKLEALEEELsEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIR 968
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
661-1211 |
9.33e-11 |
|
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: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 661 ERKGPELCLEELDAAIPGSRVGGSKARVQARQVPSATA-SEWRLAQ-------AQQKIRELAINIRMKEELIGELVRTGK 732
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqSHAYLTQkreaqeeQLKKQQLLKQLRARIEELRAQEAVLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 733 AAQALNRQ--------HSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQvlkEKK 804
Cdd:TIGR00618 282 TQERINRArkaaplaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI---HIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 805 QATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreETEQKRRLEAEMSKRQHRVKELELKHEQQQKIlkikteei 884
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQH------------------IHTLQQQKTTLTQKLQSLCKELDILQREQATI-------- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 885 aAFQRKRRSGSNGSVVSLEQQQKIE-EQKKWLDQEMEKVLQ----QRRALEELGEELHKREAILAKKEALMQEKTGLESK 959
Cdd:TIGR00618 413 -DTRTSAFRDLQGQLAHAKKQQELQqRYAELCAAAITCTAQceklEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 960 RLRSSQALNEDIVRVSSRLEHLEKEL-----SEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIdsklrqgsll 1034
Cdd:TIGR00618 492 VLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL---------- 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1035 spEEERTLFQLDEAIEAldaaieykneaiTCRQRVlRASASLLSQcEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQ 1114
Cdd:TIGR00618 562 --KEQMQEIQQSFSILT------------QCDNRS-KEDIPNLQN-ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1115 HQQQIAFSELEMQLEEQQRLV----YWLEVALERQRlEMDRQLTLQQKEHEQNMQLLLQ--QSRDHLSEGLADSRRQYEA 1188
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTalhaLQLTLTQERVR-EHALSIRVLPKELLASRQLALQkmQSEKEQLTYWKEMLAQCQT 704
|
570 580
....*....|....*....|...
gi 1622954647 1189 RIQALEKDLGRYMWINQELKQKL 1211
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENAS 727
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-1039 |
1.78e-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: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 704 AQAQQKIR-----------ELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELSEGQRQLREL 769
Cdd:TIGR02168 207 RQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 770 EGkepqdagersRLQEFRRRVAAAQSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 849
Cdd:TIGR02168 287 QK----------ELYALANEISRLEQQKQILRERL---ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 850 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNgsvvsleQQQKIEEQKKWLDQEMEKVLQQRRAL 929
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-------EIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 930 EELGEElHKREAILAKKEALMQEKTGLESKRLRSSQALNedivRVSSRLEHLEKELSEKNGQLRQGSAQ--SQQQIRREI 1007
Cdd:TIGR02168 427 LKKLEE-AELKELQAELEELEEELEELQEELERLEEALE----ELREELEEAEQALDAAERELAQLQARldSLERLQENL 501
|
330 340 350
....*....|....*....|....*....|...
gi 1622954647 1008 DSLRQEKDSLLKQRLEIDSKL-RQGSLLSPEEE 1039
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILgVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
743-1079 |
1.21e-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: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 743 QRIRELEQEAERVRAELSEGQRQLRELEGkepqdagersRLQEFRRRVAAAQsQVQVLKEKKQATERLVSLsaqseKRLQ 822
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELER----------QLKSLERQAEKAE-RYKELKAELRELELALLV-----LRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 823 ELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAafqrkrrsgsngsvvsl 902
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----------------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 903 eqqqKIEEQKKWLDQEMEKVLQQ-----------RRALEELGEELHKREAILAK-------KEALMQEKTGLESKRLRSS 964
Cdd:TIGR02168 299 ----RLEQQKQILRERLANLERQleeleaqleelESKLDELAEELAELEEKLEElkeelesLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 965 QALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQsQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLlsPEEERTLFQ 1044
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEE 451
|
330 340 350
....*....|....*....|....*....|....*
gi 1622954647 1045 LDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQ 1079
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
791-1036 |
1.36e-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: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 791 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKH 870
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 871 EQQQKILKIKTEEIAAFQRKR-RSGSNGSVVSLEQQQKIEEQKKWLdQEMEKVLQQRRA-LEELGEELHKREAILAKKEA 948
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREqAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 949 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKL 1028
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE-LQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*...
gi 1622954647 1029 RQGSLLSP 1036
Cdd:COG4942 251 LKGKLPWP 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-1198 |
1.61e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 700 EWRLAQAQQKIRELAINIRmkeELIGELvrtgkaaqalnrqhsQRIRELEQEAERVRAELSEGQRQLRELEGKEpqdAGE 779
Cdd:PRK03918 199 EKELEEVLREINEISSELP---ELREEL---------------EKLEKEVKELEELKEEIEELEKELESLEGSK---RKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 780 RSRLQEFRRRVAAAQSQVQVLKEK----------KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK 849
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKvkelkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 850 RRLEaEMSKR----QHRVKELELKHEQQQKILKIKTEeiaaFQRKRRSGSNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQ 924
Cdd:PRK03918 338 ERLE-ELKKKlkelEKRLEELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 925 QRRALEELGEELH---------KREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQL-RQ 994
Cdd:PRK03918 413 RIGELKKEIKELKkaieelkkaKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 995 GSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQ----------GSLLSPEEErtLFQLDEAIEALDAAIEYKNEAIT 1064
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEklkekliklkGEIKSLKKE--LEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1065 CRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywLEVALER 1144
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELK--DAEKELEREEKELKKLEEELDKAFEELAE----TEKRLEE 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1145 QRLEMDR-QLTLQQKEHEQNMQLLLQQSRDHLS-----EGLADSRRQYEARIQALEKDLG 1198
Cdd:PRK03918 645 LRKELEElEKKYSEEEYEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-956 |
1.89e-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: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 703 LAQAQQKIRELAINIRMKEELI-------GELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGkepQ 775
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA---Q 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 776 DAGERSRLQEFRRRVAAAQSQVQVLKEKKQAT----ERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR 851
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLeaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 852 LEAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEe 931
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE- 481
|
250 260
....*....|....*....|....*
gi 1622954647 932 lgEELHKREAILAKKEALMQEKTGL 956
Cdd:TIGR02168 482 --RELAQLQARLDSLERLQENLEGF 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
744-1210 |
2.02e-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: 61.96 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 744 RIRELEQEAERVRAELSEGQRQLRELEGK----EPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEK 819
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENElnllEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 820 RLQELERNVQlmrqqqgqlqrrlrEETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIaafqrkrrSGSNGSV 899
Cdd:TIGR04523 226 QNNQLKDNIE--------------KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL--------EQNNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 900 VSLEQQ-QKIEEQKKWLDQEMEKVLqqrraLEELGEELHKREailakkealmQEKTGLESKRLRSSQA---LNEDIVRVS 975
Cdd:TIGR04523 284 KELEKQlNQLKSEISDLNNQKEQDW-----NKELKSELKNQE----------KKLEEIQNQISQNNKIisqLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 976 SRLEHLEKELSEKNGQLRQgsAQSQ-QQIRREIDSLRQEKDSLLKQRLEIDSKLRQgsllspeEERTLFQLDEAIEALda 1054
Cdd:TIGR04523 349 KELTNSESENSEKQRELEE--KQNEiEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKL-- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1055 aiEYKNEAITCRQRVLRASASLLSQCEMNLmaklsylssSETRALLCKYFDKVVTLREEQhQQQIafSELEMQLEEQQRL 1134
Cdd:TIGR04523 418 --QQEKELLEKEIERLKETIIKNNSEIKDL---------TNQDSVKELIIKNLDNTRESL-ETQL--KVLSRSINKIKQN 483
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 1135 VYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRDHLSegladsrrqyeaRIQALEKDLGRymwINQELKQK 1210
Cdd:TIGR04523 484 LEQKQKELKSKEKELK-KLNEEKKELEEKVKDLTKKISSLKE------------KIEKLESEKKE---KESKISDL 543
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
696-1014 |
3.23e-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: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 696 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELSEGQRQLRELEGk 772
Cdd:TIGR02169 208 EKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEELNKKIKDLGE- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 773 epqdaGERSRLQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRR 851
Cdd:TIGR02169 287 -----EEQLRVKEKIGELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 852 LEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEE 931
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 932 LGEElhKREAILAKKEALMQEKTGLESKRlrssqalnEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLR 1011
Cdd:TIGR02169 442 EKED--KALEIKKQEWKLEQLAADLSKYE--------QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
...
gi 1622954647 1012 QEK 1014
Cdd:TIGR02169 512 VEE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
685-1029 |
9.04e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 685 KARVQARQVPSATASEWRLAQAQQKIRELainiRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQR 764
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEA----KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 765 QLR---ELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERnvqlmRQQQGQLQRR 841
Cdd:PTZ00121 1550 ELKkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 842 LREETEQKRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSGsngsvvslEQQQKIEEQKKWLDQEME 920
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEeLKKAEEENKIKAAEEAKKAEEDKKKAE--------EAKKAEEDEKKAAEALKK 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 921 KVLQQRRAleelgEELHKREAILAKK-EALMQEktglESKRLRSSQALNEDIVRVSSRLEHLEKELSEKN--GQLRQGSA 997
Cdd:PTZ00121 1697 EAEEAKKA-----EELKKKEAEEKKKaEELKKA----EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEEE 1767
|
330 340 350
....*....|....*....|....*....|....
gi 1622954647 998 QSQQQIRREIDSLRQE--KDSLLKQRLEIDSKLR 1029
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 ... |
798-1099 |
9.98e-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: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 798 QVLKEKKQATERLVSLSAQSEKRL----------QELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE 867
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLELeeeyllyldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 868 LKHEQ-QQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELH-KREAILAK 945
Cdd:pfam02463 278 EKEKKlQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 946 KEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRqgSAQSQQQIRREIDSLRQEKDSLLKQRLEID 1025
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--EAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954647 1026 SKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRqrvLRASASLLSQCEMNLMAKLSYLSSSETRAL 1099
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
700-1197 |
1.18e-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: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 700 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGK--EPQDA 777
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 778 --GERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLE 853
Cdd:TIGR02168 381 leTLRSKVAQLELQIASLNNEIERLEARLERLEdRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqEELERLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 854 AEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR--SGSNGSVVSLEQQQK------------IEEQKKWlDQEM 919
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvlselISVDEGY-EAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 920 EKVL-------------QQRRALEELGEELHKREAILA---KKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLE---- 979
Cdd:TIGR02168 540 EAALggrlqavvvenlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 980 ----------------HLEKELSEKN-------------GQLRQGSAQSQQQI---RREIDSLRQEK------------- 1014
Cdd:TIGR02168 620 yllggvlvvddldnalELAKKLRPGYrivtldgdlvrpgGVITGGSAKTNSSIlerRREIEELEEKIeeleekiaeleka 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1015 -DSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEykneaiTCRQRVLRASASLLSQcEMNLMAKLSYLSS 1093
Cdd:TIGR02168 700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTEL-EAEIEELEERLEE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1094 SETRALLCKyfDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTLQQKEHEQNMQLLLQQSRD 1173
Cdd:TIGR02168 773 AEEELAEAE--AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE-SLERRIAATERRLEDLEEQIEE 849
|
570 580
....*....|....*....|....*.
gi 1622954647 1174 --HLSEGLADSRRQYEARIQALEKDL 1197
Cdd:TIGR02168 850 lsEDIESLAAEIEELEELIEELESEL 875
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
670-1195 |
1.20e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 670 EELDAAIPGSRVGGSKARVQARQVPSA-TASEWRLAQAQQKIREL--AINIRMKEEL-IGELVRTGKAA-QALNRQHSQR 744
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAArkAEEVRKAEELrKAEDARKAEAArKAEEERKAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 745 IRELEQE--------AERVRAELSEGQRQlRELEGKEPQDAGERSRLQEFRRRVAAAQSQ-------VQVLKEKKQATER 809
Cdd:PTZ00121 1217 ARKAEDAkkaeavkkAEEAKKDAEEAKKA-EEERNNEEIRKFEEARMAHFARRQAAIKAEearkadeLKKAEEKKKADEA 1295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 810 LVS----------LSAQSEKRLQELERNVQLMRQQQGQLQRRLREET---------EQKRRLEAEMSKRQHRVKELElKH 870
Cdd:PTZ00121 1296 KKAeekkkadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaeaakaeAEAAADEAEAAEEKAEAAEKK-KE 1374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 871 EQQQKI--LKIKTEEIAAFQRKRRSGSNGSVVSlEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEA 948
Cdd:PTZ00121 1375 EAKKKAdaAKKKAEEKKKADEAKKKAEEDKKKA-DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA 1453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 949 lmQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGS--AQSQQQIRREIDSLRQEKDSLLKQRL-EID 1025
Cdd:PTZ00121 1454 --EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeAKKAAEAKKKADEAKKAEEAKKADEAkKAE 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1026 SKLRQGSLLSPEEERTLFQLDEAIEALDA----AIEYKNEAITCRQRVLRaSASLLSQCEMNLMAKLSYLSSSETRAllc 1101
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAeekkKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKM--- 1607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1102 kyfdKVVTLREEQhQQQIAFSELEMQLEEQQRLvywleVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRdhlsEGLAD 1181
Cdd:PTZ00121 1608 ----KAEEAKKAE-EAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK----KAEED 1673
|
570
....*....|....
gi 1622954647 1182 SRRQYEARIQALEK 1195
Cdd:PTZ00121 1674 KKKAEEAKKAEEDE 1687
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
735-1201 |
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 1622954647 735 QALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLS 814
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 815 AQsEKRLQELERNVqlmrqqqgqlqRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 894
Cdd:COG4717 129 PL-YQELEALEAEL-----------AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 895 SNGSVVSLEQQ-QKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGL----ESKRLRSSQALNE 969
Cdd:COG4717 197 LAEELEELQQRlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallgLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 970 DIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKlrqgslLSPEEERTLFQLDEAI 1049
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLG-KEAEELQALPALEELEEEELEELLAALGLPPD------LSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1050 EALDAAIEYKNEAITcRQRVLRASASLLSQCEMnlmaklsylSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLE 1129
Cdd:COG4717 350 QELLREAEELEEELQ-LEELEQEIAALLAEAGV---------EDEEELRAALEQAEEYQELKEE-------LEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1130 E-----QQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNM-------QLLLQQSRDHLSEGLADSRRQYEARIQALEKDL 1197
Cdd:COG4717 413 EllgelEELLEALDEEELEEELEELEEELEELEEELEELReelaeleAELEQLEEDGELAELLQELEELKAELRELAEEW 492
|
....
gi 1622954647 1198 GRYM 1201
Cdd:COG4717 493 AALK 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
922-1211 |
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 1622954647 922 VLQQRRALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQ 1001
Cdd:TIGR02168 672 ILERRREIEELEEKI---EELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1002 ------QIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASAS 1075
Cdd:TIGR02168 745 leeriaQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1076 LLSQCEMNLMAKLSYLSssETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDrQLTL 1155
Cdd:TIGR02168 825 RLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSE 901
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 1156 QQKEHEQNMQLLlqqsrDHLSEGLADSRRQYEARIQALEKDLgrymwinQELKQKL 1211
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 ... |
702-1196 |
3.39e-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: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIGELVRTgkaaqalnrqhsqrIRELEQEAERVR--AELSEGQRQ--LRELEGKEPQDA 777
Cdd:pfam10174 220 QLQPDPAKTKALQTVIEMKDTKISSLERN--------------IRDLEDEVQMLKtnGLLHTEDREeeIKQMEVYKSHSK 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 778 GERSRLQEFRRRVAAAQSQVQVLKEK-----------KQATERLV-SLSAQsEKRLQELERNVQLMRQQQGQLQRRLREE 845
Cdd:pfam10174 286 FMKNKIDQLKQELSKKESELLALQTKletltnqnsdcKQHIEVLKeSLTAK-EQRAAILQTEVDALRLRLEEKESFLNKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 846 TEQKRRLEAEMSKRQHRVKELelkheqqQKILKIKTEEIAAFQRKrrsgsngsVVSLEQQQKieEQKKWLDQEMEKV--L 923
Cdd:pfam10174 365 TKQLQDLTEEKSTLAGEIRDL-------KDMLDVKERKINVLQKK--------IENLQEQLR--DKDKQLAGLKERVksL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 924 QQRR-----ALEELGEELHKREAILakkEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLR--QGS 996
Cdd:pfam10174 428 QTDSsntdtALTTLEEALSEKERII---ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIdlKEH 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 997 AQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLrQGSLL----SPEEERTLFQLDEAIEALDAAIE-YKNEAITCRQRVLR 1071
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIAVEQKKEECSKL-ENQLKkahnAEEAVRTNPEINDRIRLLEQEVArYKEESGKAQAEVER 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1072 ASAsLLSQCEMNLMAKLSYLSSSETRALLcKYFDKVVTLREEQHQQQIAFSELEMQLEE------------QQRLVYWLE 1139
Cdd:pfam10174 584 LLG-ILREVENEKNDKDKKIAELESLTLR-QMKEQNKKVANIKHGQQEMKKKGAQLLEEarrrednladnsQQLQLEELM 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 1140 VALERQRLEMDrqltlQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARI----QAL-----EKD 1196
Cdd:pfam10174 662 GALEKTRQELD-----ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILemkqEALlaaisEKD 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
691-1079 |
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 1622954647 691 RQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELvrtgkAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELE 770
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 771 gkepqdagerSRLQEFRRRVAAAQSQVQVLKEKKQATERLV-SLSAQSEKRLQELERNVqlmrqqqGQLQRRLREETEQK 849
Cdd:COG4717 153 ----------ERLEELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEEL-------EELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 850 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAF------------------------------------------ 887
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllar 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 888 QRKRRSGSNGSVVSLEQQQKIEEQK-------------------KWLDQEMEKVLQQRRALEELGEELhKREAILAKKEA 948
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQELLREAEELEEEL-QLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 949 LMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQ--------QQIRREIDSLRQEKDSLLKQ 1020
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeelEELEEELEELEEELEELREE 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622954647 1021 RLEIDSKLRQgsllsPEEERTLFQLDEAIEALDAAIEYKNEAItcrqRVLRASASLLSQ 1079
Cdd:COG4717 455 LAELEAELEQ-----LEEDGELAELLQELEELKAELRELAEEW----AALKLALELLEE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
692-889 |
3.88e-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: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 692 QVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEG 771
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 772 KepqdagERSRLQEFRRRVAAAQSQVQVLKEK------------------KQATERLVSLSAQSEKRLQELERNVQLMRQ 833
Cdd:COG4942 98 E------LEAQKEELAELLRALYRLGRQPPLAlllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 834 QQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQR 889
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
689-1063 |
4.64e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 689 QARQVPSATASEWRLAQAQQKIRElainIRMKEELigelvrTGKAAQALNRQHSQRIRELEQEAERVRAElSEGQRQLRE 768
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEE----KKKADEA------KKKAEEAKKADEAKKKAEEAKKAEEAKKK-AEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 769 LEGKepqdAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQ 848
Cdd:PTZ00121 1475 AKKK----AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 849 KRRLEaEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSV-------------------VSLEQQQKIE 909
Cdd:PTZ00121 1551 LKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeekkmkaeeakkaeeakIKAEELKKAE 1629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 910 EQKKWLDQEMEKVLQQRRALEELGEELH---------KREAILAKKEAlmQEKTGLESKRLRSSQALNEdivrvssrleh 980
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEenkikaaeeAKKAEEDKKKA--EEAKKAEEDEKKAAEALKK----------- 1696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 981 lEKELSEKNGQLRQGSAQSQ---QQIRREiDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:PTZ00121 1697 -EAEEAKKAEELKKKEAEEKkkaEELKKA-EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
....*.
gi 1622954647 1058 YKNEAI 1063
Cdd:PTZ00121 1775 KEKEAV 1780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
745-1081 |
4.72e-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: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 745 IRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRrrvaAAQSQVQVLKEKKQATERLVSLsaqseKRLQEL 824
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREYEGYELL-----KEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 825 ERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKEL--ELKHEQQQKILKIKtEEIAAFQRKRRSGSNGSVVSL 902
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkKIKDLGEEEQLRVK-EKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 903 EQQQKIEEQKKWLDQEMEKVLQQRRALE-ELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHL 981
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELErEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 982 EKELSEKNGQLRQGS--AQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYK 1059
Cdd:TIGR02169 395 EKLKREINELKRELDrlQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340
....*....|....*....|..
gi 1622954647 1060 NEAITCRQRVLRASASLLSQCE 1081
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAE 496
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
16-157 |
6.02e-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: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 16 VRVALRVRPLLPKELlhghqsclQVEPGLGRITLGRDRH----FGFHVVLAEDAGQEAVYQACVQpLLEAFFEGFNATVF 91
Cdd:pfam16796 22 IRVFARVRPELLSEA--------QIDYPDETSSDGKIGSknksFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVCIF 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622954647 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 ... |
685-951 |
6.38e-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: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 685 KARVQARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTgkaAQALNRQHSQRIR--ELEQEAERVRA-ELSE 761
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI---RQEERKRELERIRqeEIAMEISRMRElERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 762 GQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATE-RLVSLSAQSEKRLQELERNVQLMRQQQGQLQR 840
Cdd:pfam17380 385 MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREVRRLEEERAREMERVRLEEQERQQQVER 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 841 RLREETEQKRRlEAEMSKRQHRVKELElkhEQQQKILKIKTEE----IAAFQRKRR-----SGSNGSVVSLEQQQKIEEQ 911
Cdd:pfam17380 465 LRQQEEERKRK-KLELEKEKRDRKRAE---EQRRKILEKELEErkqaMIEEERKRKllekeMEERQKAIYEEERRREAEE 540
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622954647 912 KKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQ 951
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
698-1059 |
7.31e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 698 ASEWRLAQAQQKIREL--AINIRMKEEL-IGELVRtgKAAQALNRQHSQRIRELEQEAERvRAELSEGQRQLRELEGKEP 774
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAkkAEEKKKADELkKAEELK--KAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 775 QDAGERSRLQEFRRRVAAAQSQVQVLK--EKKQATERLVSLSAQSEKRLQELERnvQLMRQQQGQLQRRLREETEQKRRL 852
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKaeEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 853 EAEMSKRQHRVKELELKHEQQQK-----ILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRR 927
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 928 ALEELGEELHKREAILAKKEALMQEktGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREI 1007
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVA 1836
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622954647 1008 DS---LRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYK 1059
Cdd:PTZ00121 1837 DSknmQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
685-948 |
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 1622954647 685 KARVQARQVPSATAS-EWRLAQAQQKIRELAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIRELEQEAERVRAELSEG 762
Cdd:TIGR02169 234 ALERQKEAIERQLASlEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 763 QRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEkkQATERLVSLSAQSEK---RLQELERNVQLMRQQQGQLQ 839
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD--KLTEEYAELKEELEDlraELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 840 RRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgsNGSVVSlEQQQKIEEQKKWLDQEM 919
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED--KALEIK-KQEWKLEQLAADLSKYE 468
|
250 260
....*....|....*....|....*....
gi 1622954647 920 EKVLQQRRALEELGEELHKREAILAKKEA 948
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
703-1030 |
1.22e-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: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 703 LAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQE----AERVRAELSEGQRQLRELEGK---EPQ 775
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKideEEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 776 DAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 855
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 856 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKR---RSGSNGSVVSLEQQQKIEEQKKWLDQEME-KVLQQRRALEE 931
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEellQELLLKEEELEEQKLKDELESKEEKEKEEkKELEEESQKLN 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 932 LGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV--------RVSSRLEHLEKELSEKNGQLRQGSA---QSQ 1000
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEennkeeeeERNKRLLLAKEELGKVNLMAIEEFEekeERY 990
|
330 340 350
....*....|....*....|....*....|
gi 1622954647 1001 QQIRREIDSLRQEKDSLLKQRLEIDSKLRQ 1030
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
702-1014 |
1.53e-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: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGK--EPQDAGE 779
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlnDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 780 RSRLQEFRRRVAAAQSQVQ----VLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAE 855
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 856 MSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSgSNGSVVSLEQQQK-IEEQKKWLDQEMEKVLQQRRALEELGE 934
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRLSeLKAKLEALEEELSEIEDPKGEDEEIPE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 935 ELHKREAILAKKEALMQEKTGLESKRLRSSQalneDIVRVSSRLehleKELSEKNGQLrqgsAQSQQQIRREIDSLRQEK 1014
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQ----EYEEVLKRL----DELKEKRAKL----EEERKAILERIEEYEKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
744-1211 |
1.58e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 744 RIRELEQEAERVraelsegQRQLRELEGKEPQDAGERSRLQEFRRRVAAaqsqvqvLKEKKQATERLVSLSAQSEKRLQE 823
Cdd:PRK03918 194 LIKEKEKELEEV-------LREINEISSELPELREELEKLEKEVKELEE-------LKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 824 LERNVqlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsvvSLE 903
Cdd:PRK03918 260 KIREL--------------EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE------------------YLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 904 QQQKIEEqkkwldqEMEKVLQQRRALEELGEELHKREailAKKEALMQEKTGLESK--RLRSSQALNEDIVRVSSRLEHL 981
Cdd:PRK03918 308 ELREIEK-------RLSRLEEEINGIEERIKELEEKE---ERLEELKKKLKELEKRleELEERHELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 982 EKELSEKngqlrqgsaqSQQQIRREIDSLRQEKDSLLKQRLEIDSKLrqGSLLSPEEERtlfqlDEAIEALDAAieyKNE 1061
Cdd:PRK03918 378 KKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARI--GELKKEIKEL-----KKAIEELKKA---KGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1062 AITCRqrvlrasASLLSQCEMNLMAKLSyLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVA 1141
Cdd:PRK03918 438 CPVCG-------RELTEEHRKELLEEYT-AELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKELA 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1142 LERQRLEmdrqltlqQKEHEQNMQLLLQQSRDHlsEGLADSRRQYEARIQALEKDLGRYmwinQELKQKL 1211
Cdd:PRK03918 503 EQLKELE--------EKLKKYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKELEKL----EELKKKL 558
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
703-1173 |
3.88e-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: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 703 LAQAQQKIRELAINIRMKEELIGELVRTGkaaqalNRQHSQRIRELEQEAERVRAELSEGQR----QLRELEGKEPQDAG 778
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQ------NSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 779 E----RSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRL---------------QELE-RNVQLMRQQQGQL 838
Cdd:pfam15921 357 ElteaRTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrRELDdRNMEVQRLEALLK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 839 QRRLREETEQKRRLEAEMSKRQ--HRVKELELKHEQQQKILKIKTEEIAA----FQRKRRSGSNGSVVSLEQQQKIEEQK 912
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAkkmtLESSERTVSDLTASLQEKERAIEATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 913 KWLDQEMEKV---LQQRRALEELGEELHKREAILAKKEALMQEK--------------TGLESKRLRSSQALNEDIVRVS 975
Cdd:pfam15921 517 AEITKLRSRVdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvieilrqqienmTQLVGQHGRTAGAMQVEKAQLE 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 976 SRLEHLEKELSE-------KNGQLRQGSAQ-------------SQQQIRREIDSLRQEKDSLLKQ----RLEIDSKLRQG 1031
Cdd:pfam15921 597 KEINDRRLELQEfkilkdkKDAKIRELEARvsdlelekvklvnAGSERLRAVKDIKQERDQLLNEvktsRNELNSLSEDY 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1032 SLL-------SPEEERTLFQLDEAIEALDAAIEYKNEAITCRQ----RVLRASASLLSQCEMN------LMAKLSYLSSS 1094
Cdd:pfam15921 677 EVLkrnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEA 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1095 ETRALLCKYFdkvvtLREEQHQQQIAFS-----------ELEMQLEEQQRL---VYWLEVALERQRLEMDRQLTLQQKEH 1160
Cdd:pfam15921 757 MTNANKEKHF-----LKEEKNKLSQELStvateknkmagELEVLRSQERRLkekVANMEVALDKASLQFAECQDIIQRQE 831
|
570
....*....|...
gi 1622954647 1161 EQNMQLLLQQSRD 1173
Cdd:pfam15921 832 QESVRLKLQHTLD 844
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
698-1061 |
4.70e-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: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 698 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDA 777
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 778 GERSRLQEFRRRVAAAQSQ-----VQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 852
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAEleeeeEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 853 ---------------------------EAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAF------------QRKRRS 893
Cdd:COG1196 515 llaglrglagavavligveaayeaaleAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkiraraalAAALAR 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 894 GSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDivr 973
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL--- 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 974 vSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALD 1053
Cdd:COG1196 672 -AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
....*...
gi 1622954647 1054 AAIEYKNE 1061
Cdd:COG1196 751 EALEELPE 758
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
716-1043 |
4.72e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.99 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 716 NIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELegkepqdageRSRLQEFRRRVAAAQS 795
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKEL----------REEAQELREKRDELNE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 796 QVQVLKEKKQAT-ERLVSLSAQSEKRLQELernvqlmrqqqgqlqrrlrEETEQKRRLEAEMSKrqhRVKELELKheQQQ 874
Cdd:COG1340 72 KVKELKEERDELnEKLNELREELDELRKEL-------------------AELNKAGGSIDKLRK---EIERLEWR--QQT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 875 KILKIKtEEIAAFQRKRRSGSngsvvSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHK-REAILAKKEALMQEK 953
Cdd:COG1340 128 EVLSPE-EEKELVEKIKELEK-----ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 954 TGLESKRlRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRL-EIDSKLRQGS 1032
Cdd:COG1340 202 KEADELR-KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAeEIFEKLKKGE 280
|
330
....*....|.
gi 1622954647 1033 LLSPEEERTLF 1043
Cdd:COG1340 281 KLTTEELKLLQ 291
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
696-1197 |
5.38e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.98 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 696 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQR---IRELEQEAERVRAELSEGQRQL------ 766
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYleaLNKKLNEKESQLADAREVISCLknelse 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 767 --RELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLrE 844
Cdd:pfam05557 116 lrRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSK-S 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 845 ETEQKRRLEAEMSKRQHRVKELelkHEQQQKILKIKtEEIAAFQRK--RRSGSNGSVVSLE-----QQQKIEEQKKwLDQ 917
Cdd:pfam05557 195 ELARIPELEKELERLREHNKHL---NENIENKLLLK-EEVEDLKRKleREEKYREEAATLElekekLEQELQSWVK-LAQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 918 EMEKVLQQRRALEELGEELHKREAilakkeALMQEKTGLES--KRLRSSQALNEDIVRV-SSRLEHLEKELSEKNGQLRQ 994
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREI------VLKEENSSLTSsaRQLEKARRELEQELAQyLKKIEDLNKKLKRHKALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 995 gsaqsqqqIRREIDSLRQEKDsLLKQRLE-IDSKLRqgsllspEEERTLFQLDEAIEALDAAIEYKNEAITCRQRV---L 1070
Cdd:pfam05557 344 --------LQRRVLLLTKERD-GYRAILEsYDKELT-------MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLsvaE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1071 RASASLLSQCEMnLMAKLSYLSSSETRALLCKYFDKVVTLREEqhqqqiaFSELEMQLEEQQRLVYWLEVALERQRLEMD 1150
Cdd:pfam05557 408 EELGGYKQQAQT-LERELQALRQQESLADPSYSKEEVDSLRRK-------LETLELERQRLREQKNELEMELERRCLQGD 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622954647 1151 RQLTLQQK-EHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQALEKDL 1197
Cdd:pfam05557 480 YDPKKTKVlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDL 527
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
737-1228 |
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 1622954647 737 LNRQHS--QRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKekkqatERLVSLS 814
Cdd:TIGR00618 371 SCQQHTltQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ------RYAELCA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 815 AQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSG 894
Cdd:TIGR00618 445 AAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 895 SNGSVVsleqqQKIEEQKKWLDQEMEKVLQQrraleelGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRV 974
Cdd:TIGR00618 525 PLTRRM-----QRGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNI 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 975 SSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRqekdslLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDA 1054
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD------VRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1055 AIEYKNEAITCRQRVLRASASLLSQCEMN---LMAKLSYLSSSETrallckyfdKVVTLREEQHQQQIAFSELEMQLEEQ 1131
Cdd:TIGR00618 667 IRVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELET---------HIEEYDREFNEIENASSSLGSDLAAR 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1132 QRLVYWLEVALERQRLEMDRQLTL--QQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQALEKDLGRymwINQELKQ 1209
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEahFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE---IGQEIPS 814
|
490
....*....|....*....
gi 1622954647 1210 KLGGVNTVGHSRGGEKRSL 1228
Cdd:TIGR00618 815 DEDILNLQCETLVQEEEQF 833
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
690-1064 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 690 ARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKA-AQALNRQHSQRI----RELEQEAERVRAELSEG-- 762
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvLARLLELQEEPCplcgSCIHPNPARQDIDNPGPlt 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 763 ---QRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQA-TERLVSLSAQSEKRLQELERNVQLMRQQQGQL 838
Cdd:TIGR00618 528 rrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIlTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 839 QRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQ------------QQ 906
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqlalqkmQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 907 KIEEQKKWLD----------QEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQALNEDIVRVS 975
Cdd:TIGR00618 688 EKEQLTYWKEmlaqcqtllrELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKeLMHQARTVLKARTEAHFNNN 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 976 SR----------LEHLEKELSEKN-------GQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEE 1038
Cdd:TIGR00618 768 EEvtaalqtgaeLSHLAAEIQFFNrlreedtHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
410 420
....*....|....*....|....*.
gi 1622954647 1039 ERTLFQLDEAIEALDAAIEYKNEAIT 1064
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
711-1177 |
1.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 711 RELAINIRMKEELIGELvRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGERSRLQEFRRRV 790
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 791 AAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREET-EQKRRLEAEMSKRQHRVKELELK 869
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 870 HEQQQKILKIKTEEIAAFQRKRR-------SGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQ---------QRRALEELG 933
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERlkearllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfllLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 934 EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREI------ 1007
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagv 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1008 ---DSLR------QEKDSLLKQRLEIDSKLRQ--GSLLSPEEERTLFQLDEAIEALDAAIEYKNEAIT-CRQRVLRASAs 1075
Cdd:COG4717 382 edeEELRaaleqaEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEeLREELAELEA- 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1076 llsqcemnlmaKLSYLSSSETrallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVYwLEVALERqrlemdrqltL 1155
Cdd:COG4717 461 -----------ELEQLEEDGE-------------LAELLQELEELKAELRELAEEWAALKL-ALELLEE----------A 505
|
490 500
....*....|....*....|..
gi 1622954647 1156 QQKEHEQNMQLLLQQSRDHLSE 1177
Cdd:COG4717 506 REEYREERLPPVLERASEYFSR 527
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
739-1068 |
2.15e-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: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 739 RQHSQRIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEkkqaterlvslsaqSE 818
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAEAEQELEESKRE--------------TE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 819 KRLQELERNVQLMRQQQGQLQRRLREETEQ------KRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRR 892
Cdd:COG5185 336 TGIQNLTAEIEQGQESLTENLEAIKEEIENivgeveLSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 893 SgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKReailakkealmqEKTGLESKRLRSSQALNEDIV 972
Cdd:COG5185 416 K---------AADRQIEELQRQIEQATSSNEEVSKLLNELISELNKV------------MREADEESQSRLEEAYDEINR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 973 RVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEAL 1052
Cdd:COG5185 475 SVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
330
....*....|....*.
gi 1622954647 1053 DAAIEYKNEAITCRQR 1068
Cdd:COG5185 555 NAKTDGQAANLRTAVI 570
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1218 |
3.22e-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: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 844 EETEQK--------RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEiaafQRKRRSGSNGSVVSLEQqqKIEEQKKWL 915
Cdd:TIGR02168 175 KETERKlertrenlDRLEDILNELERQLKSLERQAEKAERYKELKAEL----RELELALLVLRLEELRE--ELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 916 DQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQA-LNEDIVRVSSRLEHLEKELSEKNGQLRQ 994
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK-ELYALANEISrLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 995 GSAQSQQQiRREIDSLRQEKDSLLKQRLEIDSKLrqgsllsPEEERTLFQLDEAIEALDAAIEYKNeaitcrqrvlrasa 1074
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAEL-------EELEAELEELESRLEELEEQLETLR-------------- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1075 sllsqcemnlmaklsylsssetrallckyfDKVVTLREEQHQQQIAFSELEMQLEEQQRlvywlevalERQRLEmDRQLT 1154
Cdd:TIGR02168 386 ------------------------------SKVAQLELQIASLNNEIERLEARLERLED---------RRERLQ-QEIEE 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954647 1155 LQQKEHEQNMQLLlQQSRDHLSEGLADSRRQYEARIQALEKDLGRYMWINQELKQKLGGVNTVG 1218
Cdd:TIGR02168 426 LLKKLEEAELKEL-QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
773-1030 |
7.80e-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: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 773 EPQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQK-R 850
Cdd:COG4913 219 EEPDTFEAaDALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAElE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 851 RLEAEMSKRQHRVKELELKHEQQQkilkiktEEIAAFQRKRRSgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE 930
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALR-------EELDELEAQIRG------NGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 931 ELGEELHkreailakkEALMQEKTGLESKRLRSSQALNEdivrvssrlehlEKELSEKNGQLRQGSAQSQQQIRREIDSL 1010
Cdd:COG4913 366 ALLAALG---------LPLPASAEEFAALRAEAAALLEA------------LEEELEALEEALAEAEAALRDLRRELREL 424
|
250 260
....*....|....*....|
gi 1622954647 1011 RQEKDSLLKQRLEIDSKLRQ 1030
Cdd:COG4913 425 EAEIASLERRKSNIPARLLA 444
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1197 |
9.65e-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: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 849 KRRLEAEMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQRR 927
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKrELSSLQSELRRIENRLDELSQELSDA-----------SRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 928 ALEELGEELhkrEAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSRLEHLEKELSEkngqlrqgsaQSQQQIRREI 1007
Cdd:TIGR02169 738 RLEELEEDL---SSLEQEIENVKSELKELEARI----EELEEDLHKLEEALNDLEARLSH----------SRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1008 DSLRQEKDSLLKQRLEIDSKLRQgslLSPEEErtlfQLDEAIEALDAAIEYKNEAITCRQRVLRasasllsqcemNLMAK 1087
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNR---LTLEKE----YLEKEIQELQEQRIDLKEQIKSIEKEIE-----------NLNGK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1088 LsylssSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLL 1167
Cdd:TIGR02169 863 K-----EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
330 340 350
....*....|....*....|....*....|
gi 1622954647 1168 LQQSRDHLSEGLADSRRQYEARIQALEKDL 1197
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 ... |
749-1195 |
9.68e-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: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 749 EQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEfrrrvaAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 828
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQE------QLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 829 qlmrqqqgqlqrrlREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 908
Cdd:pfam01576 85 --------------EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 909 EEQKKWLDQEMEKVLQQRRALEELGEEL----HKREAI-------LAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSR 977
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLsklkNKHEAMisdleerLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 978 LEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDsLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1058 YKNEAiTCRQRVLRasasllSQCEMNLmAKLSYLSSSETRAllckyFDKVVTLREEQHQQqiAFSELEMQLEEQQRLVYW 1137
Cdd:pfam01576 310 DTLDT-TAAQQELR------SKREQEV-TELKKALEEETRS-----HEAQLQEMRQKHTQ--ALEELTEQLEQAKRNKAN 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954647 1138 LE---VALERQRLEMDRQL-TLQQ--KEHEQNMQLLLQQSRDhLSEGLADSRRQYEARIQALEK 1195
Cdd:pfam01576 375 LEkakQALESENAELQAELrTLQQakQDSEHKRKKLEGQLQE-LQARLSESERQRAELAEKLSK 437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
730-1062 |
9.70e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 730 TGKAAQALNRQHSQRIRELEQEAERVRAelSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVlkEKKQATER 809
Cdd:PTZ00121 1108 TGKAEEARKAEEAKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA--KKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 810 LVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAemskrQHRVKELELKHEQQQKILKIKT-EEIAAFQ 888
Cdd:PTZ00121 1184 AEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA-----VKKAEEAKKDAEEAKKAEEERNnEEIRKFE 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 889 RKRRSgsngSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRAlEELGEELHKREAILAKKEAlMQEKTGLESKRLRSSQALN 968
Cdd:PTZ00121 1259 EARMA----HFARRQAAIKAEEARK--ADELKKAEEKKKA-DEAKKAEEKKKADEAKKKA-EEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 969 EDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQiRREIDSLRQE----KDSLLKQRLEIDSKLRQGSLLSPEEERTLFQ 1044
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEeakkKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
330
....*....|....*...
gi 1622954647 1045 LDEAIEALDAAIEYKNEA 1062
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKA 1427
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
742-1194 |
1.26e-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: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 742 SQRIRELEQEAERVRAELSEGQRQLRELEGkEPQDAGERsRLQEFRRRVAAAQSQVQV----LKEKKqATERLVSLSAQS 817
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKS-ESQNKIEL-LLQQHQDRIEQLISEHEVeitgLTEKA-SSARSQANSIQS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 818 EKRL-QELERNvqlmRQQQGQLQRRLREETEQKRRLEAEMSKRQHrvkelELKHEQQQKILKIKTEEIAAFQRKRRSGSN 896
Cdd:pfam15921 300 QLEIiQEQARN----QNSMYMRQLSDLESTVSQLRSELREAKRMY-----EDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 897 GSVVSLEQQQKI---------------EEQKKWLDQEMEKVL---QQRRALEELGEELHKREAILakkEALMQEKTGLES 958
Cdd:pfam15921 371 ESGNLDDQLQKLladlhkrekelslekEQNKRLWDRDTGNSItidHLRRELDDRNMEVQRLEALL---KAMKSECQGQME 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 959 KRLRSSQALNEDIVRVSSRLEHLEkelsekngqlrqgsaQSQQQIRREIDSLRQEKDSLlkqrleidsklrqgsllsPEE 1038
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQLE---------------STKEMLRKVVEELTAKKMTL------------------ESS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1039 ERTLFQLDEAIEALDAAIEYKNEAITcrqrVLRASASLLSQCEMNLMAKLSYLSSSETRallCKyfdkvvTLREEQHQQQ 1118
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEIT----KLRSRVDLKLQELQHLKNEGDHLRNVQTE---CE------ALKLQMAEKD 561
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 1119 IAFSELEMQLEEQQRLVYwlevalERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQALE 1194
Cdd:pfam15921 562 KVIEILRQQIENMTQLVG------QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
746-1026 |
1.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 746 RELEQE-----AERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKR 820
Cdd:PRK03918 443 RELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 821 LQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFQRKRRSGSNGSVV 900
Cdd:PRK03918 523 KAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE--------------EELAELLKELEELGFESVE 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 901 SLEQQ-QKIEE-QKKWL---DQEMEKVLQQRRaLEELGEELHKREAILAKKEALMQEKTG-LESKRLRSSQalnEDIVRV 974
Cdd:PRK03918 589 ELEERlKELEPfYNEYLelkDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKeLEELEKKYSE---EEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622954647 975 SSRLEHLEKELSEKNGQLrQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDS 1026
Cdd:PRK03918 665 REEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
693-1024 |
1.56e-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: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 693 VPSATASEWRLAQAQQKIRELainIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGK 772
Cdd:pfam07888 26 VPRAELLQNRLEECLQERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 773 EPQDAGERSRLQEFRRRVAAAQsqvqvlkekkqaterlvslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 852
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQR--------------------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 853 EAEMSKRQHRVKELELKHEQQQKILKIKTEEiaaFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL 932
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKE---FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 933 GEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEdivrvsSRLE--HLEKELSEKNGQLRQGSAQSQQQIRREIDSL 1010
Cdd:pfam07888 240 RSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ------ARLQaaQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330
....*....|....
gi 1622954647 1011 RQEKDSLLKQRLEI 1024
Cdd:pfam07888 314 EADKDRIEKLSAEL 327
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-939 |
1.70e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 696 ATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRE----LEG 771
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseLEA 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 772 KEPQDAGERSRLQEFRRRVAAAQSQVQVL----KEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE 847
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELeskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 848 QK-RRLEAEMSKRQHRVKELElkheqqqkilkiktEEIAAFqrkrrsgsnGSV--VSLEQQQKIEEQKKWLDQEMEKVLQ 924
Cdd:TIGR02168 958 ALeNKIEDDEEEARRRLKRLE--------------NKIKEL---------GPVnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
250
....*....|....*
gi 1622954647 925 QRRALEELGEELHKR 939
Cdd:TIGR02168 1015 AKETLEEAIEEIDRE 1029
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
917-1057 |
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 1622954647 917 QEMEKVLQQRRALE---ELGEELHKREAILAKKEALM--------QEKTGLESKRLRSSQA----LNEDIVRVSSRLEHL 981
Cdd:COG4913 242 EALEDAREQIELLEpirELAERYAAARERLAELEYLRaalrlwfaQRRLELLEAELEELRAelarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 982 EKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
934-1193 |
2.04e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 934 EELHKREAILAKKEALMQEKTGLeSKRLRSSQALNEDIVRVSSRLEHLEKELsekngqlrQGSAQSQQQIRREIDSLRQE 1013
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLV-QQDLEQTLALLDKIDRQKEETEQLKQQL--------AQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1014 KDSLLKQRLEIDSkLRQgslLSPEEERTLFQLDEAIEALDaaiEYKNEAITCRQRVLRASASllsqcemnlmaklsyLSS 1093
Cdd:PRK11281 110 NDEETRETLSTLS-LRQ---LESRLAQTLDQLQNAQNDLA---EYNSQLVSLQTQPERAQAA---------------LYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1094 SETRAllckyfdkvvtlreeqhqQQIAfSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQL--LLQQS 1171
Cdd:PRK11281 168 NSQRL------------------QQIR-NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdLLQKQ 228
|
250 260
....*....|....*....|..
gi 1622954647 1172 RDHLSEGLAdsrrQYEARIQAL 1193
Cdd:PRK11281 229 RDYLTARIQ----RLEHQLQLL 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
704-1190 |
2.22e-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: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 704 AQAQQKIRElaINIRMKEELIGELVRTGKAAQALNRQHSQRiRELEQEAERVR------AELSEGQRQLR-ELEGKEPQD 776
Cdd:TIGR00606 545 MDKDEQIRK--IKSRHSDELTSLLGYFPNKKQLEDWLHSKS-KEINQTRDRLAklnkelASLEQNKNHINnELESKEEQL 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 777 A-------------GERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSA--------------QSEKRLQELERNVQ 829
Cdd:TIGR00606 622 SsyedklfdvcgsqDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQ 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 830 LMRQQQgqlqrrlreETEQKRrLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVvslEQQQKIE 909
Cdd:TIGR00606 702 SKLRLA---------PDKLKS-TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ---RLKNDIE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 910 EQKKWL-----DQEMEKVLQQR-RALEELGEELHKREAILAKKEALMQEKTGleskrLRSSQALNEdivRVSSRLEHLEK 983
Cdd:TIGR00606 769 EQETLLgtimpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAAKLQGSDL-----DRTVQQVNQ---EKQEKQHELDT 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 984 ELSEknGQLRQGSAQSQQQirrEIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAI 1063
Cdd:TIGR00606 841 VVSK--IELNRKLIQDQQE---QIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLE 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1064 TCRQRVLRASASLLSQCEM-NLMAKLSYLSSSETRALLCKY----FDKVVTLREEQ-HQQQIAFSELEMQLEEQQRLVYW 1137
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETsNKKAQDKVNDIKEKVKNIHGYmkdiENKIQDGKDDYlKQKETELNTVNAQLEECEKHQEK 995
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1622954647 1138 LEVALERQRLEMDRQltlQQKEHEQNMQLLLQQSRDHLSEgLADSRRQYEARI 1190
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 ... |
702-1212 |
3.07e-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: 48.56 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINI----RMKEELIGElvrtgkaaqalNRQ--HSQR--IRELEQEAERVRAELSEG----------- 762
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIeaelKQKENKLQE-----------NRKiiEAQRkaIQELQFENEKVSLKLEEEiqenkdliken 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 763 --QRQLRELEGKEPQDAGERSRLQEFRR------------------------RVAAAQSQVQVLKEKKQATERLVSLSAQ 816
Cdd:pfam05483 151 naTRHLCNLLKETCARSAEKTKKYEYEReetrqvymdlnnniekmilafeelRVQAENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 817 SEKRLQELERNVQLMRQQQGQLQRRLREET-------------EQKRRLEAE-----MSKRQHRVKELE-LKHEQQQKI- 876
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTflleesrdkanqlEEKTKLQDEnlkelIEKKDHLTKELEdIKMSLQRSMs 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 877 --------LKIKTEEIAAFQRKRRSGS-----------------NGSVVSLE-----QQQKI---EEQKKWLDQEMEKvl 923
Cdd:pfam05483 311 tqkaleedLQIATKTICQLTEEKEAQMeelnkakaahsfvvtefEATTCSLEellrtEQQRLeknEDQLKIITMELQK-- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 924 qQRRALEELGE-------ELHKREAILAKKEALMQEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKNGQLrQGS 996
Cdd:pfam05483 389 -KSSELEEMTKfknnkevELEELKKILAEDEKLLDEKKQFE----KIAEELKGKEQELIFLLQAREKEIHDLEIQL-TAI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 997 AQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLlspeEERTLFQldeaiEALDAAIEYKNEA---ITCRQRVLRAS 1073
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL----ENKELTQ-----EASDMTLELKKHQediINCKKQEERML 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1074 ASL--LSQCEMNLMAKLSYlsssetrallckyfdkvvtLREEQHQQQiafSELEMQL---EEQQRLVYWLEVALERQRLE 1148
Cdd:pfam05483 534 KQIenLEEKEMNLRDELES-------------------VREEFIQKG---DEVKCKLdksEENARSIEYEVLKKEKQMKI 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622954647 1149 MDRQ---LTLQQKEHEQNMQLLLQQSRDHLSEGLADSRR--QYEARIQALEKDLgrymwinQELKQKLG 1212
Cdd:pfam05483 592 LENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQlnAYEIKVNKLELEL-------ASAKQKFE 653
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
963-1197 |
3.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 963 SSQALNEDIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRqgsllspEEERTL 1042
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1043 FQLDEAIEALDAAIEYKNEAItcrQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYF-DKVVTLREEQHQQQIAF 1121
Cdd:COG4942 86 AELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622954647 1122 SELEMQLEEQQRLVYWLEVALERQRlemdRQLTLQQKEHEQNMQLLLQQSRDHLSE--GLADSRRQYEARIQALEKDL 1197
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEER----AALEALKAERQKLLARLEKELAELAAElaELQQEAEELEALIARLEAEA 236
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
740-1054 |
5.59e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 740 QHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSR---LQEFRRRVAAAQSQVQ-VLKEKKQATERLVSLSA 815
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLStlsLRQLESRLAQTLDQLQnAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 816 QSE----------KRLQELERNVQLMRQQQGQLQRrlreetEQKRRLEAEMSKrqhrvkeLELKHEQQQKILKIKTEEIA 885
Cdd:PRK11281 157 QPEraqaalyansQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 886 AFQrKRRSGSNgsvvslEQQQKIEEQKkwldQEMEKVLQQRRAleELGEElHKREAILAKKEALMQEKTgLESKRLRSSQ 965
Cdd:PRK11281 224 LLQ-KQRDYLT------ARIQRLEHQL----QLLQEAINSKRL--TLSEK-TVQEAQSQDEAARIQANP-LVAQELEINL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 966 ALNEDIVRVSSRLehleKELSEKNGQLRQ---GSAQSQQQIRREIDSLR----------QEKDSL----LKQRL--EI-D 1025
Cdd:PRK11281 289 QLSQRLLKATEKL----NTLTQQNLRVKNwldRLTQSERNIKEQISVLKgslllsrilyQQQQALpsadLIEGLadRIaD 364
|
330 340 350
....*....|....*....|....*....|
gi 1622954647 1026 SKLRQGSLlspEEER-TLFQLDEAIEALDA 1054
Cdd:PRK11281 365 LRLEQFEI---NQQRdALFQPDAYIDKLEA 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
700-1161 |
6.04e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 700 EWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGE 779
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE-EEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 780 RSRLQEFRRRVAAAQSQvQVLKEKKQATERLVSLSA---QSEKRLQELERNVQL-------MRQQQGQLQRRLREETEQK 849
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLE-ELREERDELREREAELEAtlrTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 850 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTEeiaafqrkrrsgsngsVVSLEQQQKIEEQKkwLDQEMEKVLQQRRAL 929
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDR----------------IERLEERREDLEEL--IAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 930 EELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEK-----ELSEKNGQlRQGSAQSQQQIR 1004
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllAAIADAED-EIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1005 REIDSLRQEKDSLLKQRL-EIDSKLRQGSLLSPEEERTlfQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCE-- 1081
Cdd:PRK02224 619 AELNDERRERLAEKRERKrELEAEFDEARIEEAREDKE--RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEel 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1082 ----MNLMAKLSYLSS--SETRALLCKYFDkvvtLREEQHQQQIafSELEMQLEEQQRLVYWLEvALERQRLEMDRQLTL 1155
Cdd:PRK02224 697 rerrEALENRVEALEAlyDEAEELESMYGD----LRAELRQRNV--ETLERMLNETFDLVYQND-AYSHIELDGEYELTV 769
|
....*.
gi 1622954647 1156 QQKEHE 1161
Cdd:PRK02224 770 YQKDGE 775
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
702-828 |
6.65e-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: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIGELVRTGkAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERS 781
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622954647 782 R-LQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNV 828
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 ... |
803-1153 |
9.90e-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: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 803 KKQATERLVSLSAQSEKRLQELERNVQL--MRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIK 880
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 881 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwlDQEMEKVLQQRRALEELGEELHKREAILAKKEAlmQEKTGLESKR 960
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE--ELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 961 LRSS------QALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLL 1034
Cdd:pfam02463 307 RRKVddeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1035 SPEEERTLFQLDEAIEALDAAieykNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQ 1114
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEA----QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622954647 1115 HQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQL 1153
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
784-1029 |
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 1622954647 784 QEFRRRVAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHR 862
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKqAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 863 VKELELKHEQQQKILKIKTEeiAAFQRKRRSGSNGSVVSLEQQQKIEEQKK----WLDQEMEKVLQQRRA---------- 928
Cdd:pfam12128 680 ANERLNSLEAQLKQLDKKHQ--AWLEEQKEQKREARTEKQAYWQVVEGALDaqlaLLKAAIAARRSGAKAelkaletwyk 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 929 --LEELG---EELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIV----RVSSRLEHLEKELSEKNGQLrqgsAQS 999
Cdd:pfam12128 758 rdLASLGvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQL----ARL 833
|
250 260 270
....*....|....*....|....*....|
gi 1622954647 1000 QQQIRREIDSLRQEKDSLLKQRLEIDSKLR 1029
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 ... |
702-1051 |
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 1622954647 702 RLAQAQQKIRELAINIRMKEEligELvrtgKAAQAlnrqhsqrirELEQEAervrAELSEGQRQLRELEgkepqdaGERS 781
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEE---EL----QAALA----------RLEEET----AQKNNALKKIRELE-------AQIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 782 RLQEFRRRVAAAQSQVQvlKEKKQATERLVSLSAqsekrlqELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 861
Cdd:pfam01576 275 ELQEDLESERAARNKAE--KQRRDLGEELEALKT-------ELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 862 RVKELELKHEQQQKILkikTEEIAAFQRKRrsgsngsvVSLEQ-QQKIEEQKKWLDQEMeKVLQQRRALEElgeelHKRE 940
Cdd:pfam01576 346 QLQEMRQKHTQALEEL---TEQLEQAKRNK--------ANLEKaKQALESENAELQAEL-RTLQQAKQDSE-----HKRK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 941 ailaKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQ-----GSAQSQQQirrEIDSLRQEKD 1015
Cdd:pfam01576 409 ----KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvSSLESQLQ---DTQELLQEET 481
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622954647 1016 sllKQRLEIDSKLRQgsllsPEEERT--LFQLDEAIEA 1051
Cdd:pfam01576 482 ---RQKLNLSTRLRQ-----LEDERNslQEQLEEEEEA 511
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
727-859 |
2.00e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 727 LVRTGKAAQALNRQHSQ----------RIRELEQEAERVRAELSEGQRQLRELEgKEPQDAGERSRLQEFRRRVAAAQsQ 796
Cdd:PRK09510 54 MVDPGAVVEQYNRQQQQqksakraeeqRKKKEQQQAEELQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALK-Q 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954647 797 VQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKR 859
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 ... |
744-1195 |
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 1622954647 744 RIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQ-----------EFRRRVAAAQSQVQVL-KEKKQATERLV 811
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvtteakikKLEEDILLLEDQNSKLsKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 812 SLSAQ------SEKRLQELeRNVQLMRQQQGQLQRRLREETEQ-----KRRLEAEMSKRQHRVKELELKHEQQQKILKIK 880
Cdd:pfam01576 163 EFTSNlaeeeeKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQelekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 881 TEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALE----ELGEELH------------------- 937
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEkqrrDLGEELEalkteledtldttaaqqel 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 938 --KREAILAK-KEALMQEKTGLESK----RLRSSQALNEdivrVSSRLEHLE--KELSEKNgqlRQGSAQSQQQIRREID 1008
Cdd:pfam01576 322 rsKREQEVTElKKALEEETRSHEAQlqemRQKHTQALEE----LTEQLEQAKrnKANLEKA---KQALESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1009 SLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKL 1088
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1089 SYLsSSETRALLcKYFDKVVTLREEQhqqqiafSELEMQLEEQQRlvywLEVALERQRLEMDRQLTLQQKEHEQNMQLL- 1167
Cdd:pfam01576 475 ELL-QEETRQKL-NLSTRLRQLEDER-------NSLQEQLEEEEE----AKRNVERQLSTLQAQLSDMKKKLEEDAGTLe 541
|
490 500
....*....|....*....|....*....
gi 1622954647 1168 -LQQSRDHLSEGLADSRRQYEARIQALEK 1195
Cdd:pfam01576 542 aLEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
794-1062 |
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 1622954647 794 QSQVQVLKEKKqatERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 873
Cdd:COG1340 7 SSSLEELEEKI---EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 874 QKILKIKTEEIAAFQRKR--RSGSNGSVVSLEQQ-QKIEE--QKKWLDQEMEKVLQQRraLEELGEELHKREAILAKKEA 948
Cdd:COG1340 84 NEKLNELREELDELRKELaeLNKAGGSIDKLRKEiERLEWrqQTEVLSPEEEKELVEK--IKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 949 LMQEKTGLESKRLRSSQaLNEDIvrvssrlehleKELSEKNGQLRqgsaQSQQQIRREIDSLRQEKDSLLKQRLEIDSKL 1028
Cdd:COG1340 162 LKELRAELKELRKEAEE-IHKKI-----------KELAEEAQELH----EEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270
....*....|....*....|....*....|....
gi 1622954647 1029 RQgslLSPEEERTLFQLDEAIEALDAAIEYKNEA 1062
Cdd:COG1340 226 DE---LHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
845-987 |
3.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 845 ETEQKRRLEAEMSKRQHRVKELELkhEQQQKILKIKTEEIAAFQRKRRSgsngsvvsLEQQQKIEEQKK-WLDQEMEKVL 923
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNE--------LQKLEKRLLQKEeNLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622954647 924 QQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRvSSRLEHLEKELSE 987
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAK-EILLEKVEEEARH 169
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
719-1233 |
3.52e-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: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 719 MKEELIGELVRTGKAAQALNR---QHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQS 795
Cdd:pfam15921 438 MKSECQGQMERQMAAIQGKNEsleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 796 QV-----------QVLKEKKQATERLVSLSAQSE----------KRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEA 854
Cdd:pfam15921 518 EItklrsrvdlklQELQHLKNEGDHLRNVQTECEalklqmaekdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEK 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 855 EMSKRQHRVKELE-LKHEQQQKILKIKTEEIAAFQRKRRSGSNGSvvslEQQQKIEEQKKWLDQEMEKVLQQRRALEELG 933
Cdd:pfam15921 598 EINDRRLELQEFKiLKDKKDAKIRELEARVSDLELEKVKLVNAGS----ERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 934 EELHKREAILAKKEALMQEKTGLESKRLRSSQalnedivrvsSRLEHLEKELSEKNGQlrQGSAQsqqqirreidslrqe 1013
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ----------SELEQTRNTLKSMEGS--DGHAM--------------- 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1014 KDSLLKQRlEIDSKLRQgsllspeeertlfqldeaIEALDAAIEYKNEAITC---RQRVLRASASLLSQ------CEMNL 1084
Cdd:pfam15921 727 KVAMGMQK-QITAKRGQ------------------IDALQSKIQFLEEAMTNankEKHFLKEEKNKLSQelstvaTEKNK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1085 MA-KLSYLSSSETRallckyfdkvvtLREEQHQQQIAFSELEMQLEEQQRLVYWLEvaLERQRLEMDRQL---TLQQKEH 1160
Cdd:pfam15921 788 MAgELEVLRSQERR------------LKEKVANMEVALDKASLQFAECQDIIQRQE--QESVRLKLQHTLdvkELQGPGY 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1161 EQNMQL---LLQQS---RDH----LSEGLADSRRQYEARIQALEKDLGRYM-WINQELKQKLGGVNTVGHSRGGEKRSLC 1229
Cdd:pfam15921 854 TSNSSMkprLLQPAsftRTHsnvpSSQSTASFLSHHSRKTNALKEDPTRDLkQLLQELRSVINEEPTVQLSKAEDKGRAP 933
|
....
gi 1622954647 1230 SEGR 1233
Cdd:pfam15921 934 SLGA 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-1201 |
3.73e-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: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIgELVRTGKAAQALNRQHsQRIRELEQEAERVRAELSEGQRQLRELEGKEpqDAGERS 781
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLR-AALRLWFAQRRLELLE-AELEELRAELARLEAELERLEARLDALREEL--DELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 782 RLQEFRRRVAAAQSQVQVLKEKKQATERLvslSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQH 861
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 862 rvkELELKHEQQQKILKIKTEEIAAFQRkRRSGSNGSVVS----LEQQQKI---------------EEQKKWLDQeMEKV 922
Cdd:COG4913 409 ---EAEAALRDLRRELRELEAEIASLER-RKSNIPARLLAlrdaLAEALGLdeaelpfvgelievrPEEERWRGA-IERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 923 L---------------QQRRALEE--LGEELHKREAILAKKEALMQE------------KTGLESKRLRSSQALNEDIVR 973
Cdd:COG4913 484 LggfaltllvppehyaAALRWVNRlhLRGRLVYERVRTGLPDPERPRldpdslagkldfKPHPFRAWLEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 974 VSS--RLEHLEKELSeKNGQLRQGSAQSQQQIRREIDSLR------QEKDSLLKQRLEidsklrqgsllspEEERTLFQL 1045
Cdd:COG4913 564 VDSpeELRRHPRAIT-RAGQVKGNGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELA-------------ELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1046 DEAIEALDAAIEYKNEAITCRQRVLRAS------ASLLSQCEmNLMAKLSYLSSSEtrallckyfDKVVTLREEQHQQQI 1119
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIA-ELEAELERLDASS---------DDLAALEEQLEELEA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1120 AFSELEMQLE-----------EQQRLVYWLEVALER-QRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYE 1187
Cdd:COG4913 700 ELEELEEELDelkgeigrlekELEQAEEELDELQDRlEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR 779
|
570
....*....|....
gi 1622954647 1188 ARIQALEKDLGRYM 1201
Cdd:COG4913 780 ARLNRAEEELERAM 793
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
743-931 |
4.27e-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: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 743 QRIRELEQEAERVRAELSEGQRQLRELEGKEpqdAGERSRLQEFRRRVAAAQSQVQVLKEK-KQATERLvsLSAQSEKRL 821
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARL---EAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQL--GNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 822 QELERnvqlmrqqqgqlqrrlrEETEQKRRLeaemSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRsgsngsvvs 901
Cdd:COG1579 92 EALQK-----------------EIESLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELE--------- 141
|
170 180 190
....*....|....*....|....*....|
gi 1622954647 902 lEQQQKIEEQKKWLDQEMEKVLQQRRALEE 931
Cdd:COG1579 142 -EKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
702-987 |
5.09e-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: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKAAQAL---------NRQHSQRIRELEQEaervRAELSEGQRQLRELEGk 772
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAE----LERLDASSDDLAALEE- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 773 epQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRL 852
Cdd:COG4913 693 --QLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 853 EAEMSKRQHRVKelELKHEQQQKILKIkteeIAAFQRKRRSGSNGSVVSLEqqqkieeqkkwldqEMEKVLQQRRALEEL 932
Cdd:COG4913 768 RENLEERIDALR--ARLNRAEEELERA----MRAFNREWPAETADLDADLE--------------SLPEYLALLDRLEED 827
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622954647 933 GEELHKREAILAKKEALMQEKTGLeskrlrsSQALNEDIVRVSSRLEHLEKELSE 987
Cdd:COG4913 828 GLPEYEERFKELLNENSIEFVADL-------LSKLRRAIREIKERIDPLNDSLKR 875
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
710-960 |
5.59e-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: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 710 IRELAINIRMKEELIGELVRTGKAAQALnrqhSQRIRELEQEAERVRAElsEGQRQLRELEGKEPQDAGERSRLQEfrrR 789
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEA---E 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 790 VAAAQSQVQVLKEKKQATERlvSLSAQSEKRLQELERnvqlmrqqqgqlqrrlreeteQKRRLEAEMSKRQHRVKELelk 869
Cdd:COG4913 311 LERLEARLDALREELDELEA--QIRGNGGDRLEQLER---------------------EIERLERELEERERRRARL--- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 870 hEQQQKILKIKT-EEIAAFQRKRRsgsngsvVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEElgeelhkreailaKKEA 948
Cdd:COG4913 365 -EALLAALGLPLpASAEEFAALRA-------EAAALLEALEEELEALEEALAEAEAALRDLRR-------------ELRE 423
|
250
....*....|..
gi 1622954647 949 LMQEKTGLESKR 960
Cdd:COG4913 424 LEAEIASLERRK 435
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
748-1025 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 748 LEQEAERVRAELSEGQRQLRElegkepqdagersRLQEFRRRVAAAQSQVQVLKEKKQaterLVSLSAQSEKRLQELERn 827
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE-------------QLPELRKELEEAEAALEEFRQKNG----LVDLSEEAKLLLQQLSE- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 828 vqlmrqqqgqlqrrlreeteqkrrLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQrkrrsgSNGSVVSLEQQQk 907
Cdd:COG3206 224 ------------------------LESQLAEARAELAEAEARLAALRAQLGSGPDALPELL------QSPVIQQLRAQL- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 908 ieeqkkwldQEMEkvLQQRRALEELGEELHKREAILAKKEALMQEktgLESKRLRSSQALNEDIVRVSSRLEHLEKELSE 987
Cdd:COG3206 273 ---------AELE--AELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622954647 988 KNGQLRQGSAQSQQ--QIRREIDSLRQEKDSLLKQRLEID 1025
Cdd:COG3206 339 LEARLAELPELEAElrRLEREVEVARELYESLLQRLEEAR 378
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
698-951 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 698 ASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEGKEPQDA 777
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 778 GERSRLqefrrrVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETE----QKRRLE 853
Cdd:pfam15921 632 LEKVKL------VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmQLKSAQ 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 854 AEMSKRQHRVKELELK--HEQQ-----QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQR 926
Cdd:pfam15921 706 SELEQTRNTLKSMEGSdgHAMKvamgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
250 260
....*....|....*....|....*
gi 1622954647 927 RALEELGEELHKREAILAKKEALMQ 951
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANME 810
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
698-1048 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 698 ASEWrLAQAQQKIReLAINIRMKEELIGEL-VRTGKAAQALNRQHSQRIrELEQEAERVRAELSEGQRQLRELegkepQD 776
Cdd:COG3096 332 ASDH-LNLVQTALR-QQEKIERYQEDLEELtERLEEQEEVVEEAAEQLA-EAEARLEAAEEEVDSLKSQLADY-----QQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 777 AgersrLQEFRRRVAAAQSQVQVLKEKKQAT-------ERLVSLSAQSEKRLQELERNVQlmrqqqgqlqrrlreETEQK 849
Cdd:COG3096 404 A-----LDVQQTRAIQYQQAVQALEKARALCglpdltpENAEDYLAAFRAKEQQATEEVL---------------ELEQK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 850 RRLeAEMSKRQHRvKELEL------------KHEQQQKILKIKTEEIAAFQRkrRSGSNGSVVSLEQ----QQKIEEQKK 913
Cdd:COG3096 464 LSV-ADAARRQFE-KAYELvckiageversqAWQTARELLRRYRSQQALAQR--LQQLRAQLAELEQrlrqQQNAERLLE 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 914 WLDQEMEKVLQQRRALEELGEELH-KREAILAKKEALMQEKTGLESKRlrssQALNEDIVRVSSR----------LEHLE 982
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEaQLEELEEQAAEAVEQRSELRQQL----EQLRARIKELAARapawlaaqdaLERLR 615
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 983 KELSEKNGQLRQGSAQSQQQIRREIDsLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEA 1048
Cdd:COG3096 616 EQSGEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIERLSQPGGAEDPRLLALAER 680
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
744-934 |
2.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 744 RIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGER-SRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQ 822
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 823 ELERNVQLMRQQQGQLQRRLREET-----EQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRrsgsng 897
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK------ 710
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622954647 898 svvslEQQQKIEEQKKWLDQEMEKV-----LQQRRALEELGE 934
Cdd:PRK03918 711 -----KELEKLEKALERVEELREKVkkykaLLKERALSKVGE 747
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
898-1185 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 898 SVVSLEQQQKIEE-QKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALnedivrvss 976
Cdd:pfam17380 283 AVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--------- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 977 RLEHLEKELSekngQLRQGSAQSQQQIRREIDSL---RQEKDSLLKQRLEIDSKLRqgsLLSPEEERTLFQLDEAIEALD 1053
Cdd:pfam17380 354 RQEERKRELE----RIRQEEIAMEISRMRELERLqmeRQQKNERVRQELEAARKVK---ILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1054 AAIEykneaiTCRQRVLRAsasllsqcemnlmaklsyLSSSETRALlckyfdKVVTLREEQHQQQIafsELEMQLEEQQR 1133
Cdd:pfam17380 427 AEQE------EARQREVRR------------------LEEERAREM------ERVRLEEQERQQQV---ERLRQQEEERK 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622954647 1134 lvywlevaleRQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQ 1185
Cdd:pfam17380 474 ----------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR 515
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
902-1195 |
3.01e-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: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 902 LEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILakkealmqEKTGLESKRLRS-----SQALNEDIVR--- 973
Cdd:COG3096 343 LRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL--------EAAEEEVDSLKSqladyQQALDVQQTRaiq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 974 ---VSSRLEHLEK-----ELSEKNGQLRQGSAQSQQQirrEIDSLRQEkdslLKQRLEIDSKLRQgsllspeeertlfQL 1045
Cdd:COG3096 415 yqqAVQALEKARAlcglpDLTPENAEDYLAAFRAKEQ---QATEEVLE----LEQKLSVADAARR-------------QF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1046 DEAIEAL---------DAAIEYKNEAItCRQRVLRASASLLSQCEMNLmAKLSYLSSSETRAL-----LCKYFDKVVT-- 1109
Cdd:COG3096 475 EKAYELVckiageverSQAWQTARELL-RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAErlleeFCQRIGQQLDaa 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1110 --LREEQHQQQIAFSELEMQLEEQQrlvywlEVALE-RQRLEmdrQLTLQQKEHEQ------NMQLLLQQSRDHLSEGLA 1180
Cdd:COG3096 553 eeLEELLAELEAQLEELEEQAAEAV------EQRSElRQQLE---QLRARIKELAArapawlAAQDALERLREQSGEALA 623
|
330
....*....|....*
gi 1622954647 1181 DSRRQYEARIQALEK 1195
Cdd:COG3096 624 DSQEVTAAMQQLLER 638
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
687-1021 |
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 1622954647 687 RVQARQVPSATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNrqhsQRIRELEQEAERVRAELsegQRQL 766
Cdd:pfam05557 59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLK----NELSELRRQIQRAELEL---QSTN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 767 RELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEK------------KQATERLVSLSAQSE-KRLQELERNVQLMRQ 833
Cdd:pfam05557 132 SELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAeqrikelefeiqSQEQDSEIVKNSKSElARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 834 QQGQLQRRLR------EETEQ-KRRLEAEMSKRQHRVK-ELELKHEQQQ-----------------------KILKIKTE 882
Cdd:pfam05557 212 HNKHLNENIEnklllkEEVEDlKRKLEREEKYREEAATlELEKEKLEQElqswvklaqdtglnlrspedlsrRIEQLQQR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 883 EIAAFQRKrrSGSNGSVVSLEQQQKIEEQKkwLDQEMEKVLQQRRALEE---LGEELHKREAILAK-------------K 946
Cdd:pfam05557 292 EIVLKEEN--SSLTSSARQLEKARRELEQE--LAQYLKKIEDLNKKLKRhkaLVRRLQRRVLLLTKerdgyrailesydK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 947 EALMQEKTGLESKRLRSSQALNEDI----VRVSSRLEHLEKELSEKNGQL-----------RQGSAQSQQQIRREIDSLR 1011
Cdd:pfam05557 368 ELTMSNYSPQLLERIEEAEDMTQKMqahnEEMEAQLSVAEEELGGYKQQAqtlerelqalrQQESLADPSYSKEEVDSLR 447
|
410
....*....|
gi 1622954647 1012 QEKDSLLKQR 1021
Cdd:pfam05557 448 RKLETLELER 457
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
903-1075 |
3.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 903 EQQQKIEEQKKWLDQEMEKVLQQ----RRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQ------------A 966
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEynelQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldvlL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 967 LNEDIVRVSSRLEHLEKeLSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLD 1046
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180
....*....|....*....|....*....
gi 1622954647 1047 EAIEALDAAIEYKNEAITCRQRVLRASAS 1075
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
735-1020 |
3.67e-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: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 735 QALNRQHSQRIRELEQEAERVRAELSEGQRQL----RELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLK-EKKQATER 809
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVsalqPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEiAVEQKKEE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 810 LVSLSAQSEK----------------RLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQ 873
Cdd:pfam10174 533 CSKLENQLKKahnaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 874 QKILKIKTEEIAAFQRKRRSGSngsvvsleqQQKIEEQKKWLDQEMEKVLQQR-----RALEELGEELHKREAILAKKEA 948
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKG---------AQLLEEARRREDNLADNSQQLQleelmGALEKTRQELDATKARLSSTQQ 683
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622954647 949 LMQEKTG-LESKRLRSSQALNEdivRVSSRLEHLEKELSEK--NGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQ 1020
Cdd:pfam10174 684 SLAEKDGhLTNLRAERRKQLEE---ILEMKQEALLAAISEKdaNIALLELSSSKKKKTQEEVMALKREKDRLVHQ 755
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
782-1057 |
4.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 782 RLQEFRRRVAAAQSQVQVLKEKKQatERLVSLSAQSE--------KRLQELErnvqlmrqqqgqlqRRLREETEQKRRLE 853
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQR--GSLDQLKAQIEekeekdlhERLNGLE--------------SELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 854 AEMSKRQHRVKELEL---KHEQQQKILKIKTEEIAafqrkrrsgsngsvvslEQQQKIEEQKKWLDQEMEKVLQQRRALE 930
Cdd:PRK02224 227 EQREQARETRDEADEvleEHEERREELETLEAEIE-----------------DLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 931 ELGEElhkREAILAkkealmqeKTGLESKrlrssqalneDIVRVSSRLEHLEKELSEKNGQLRQgSAQSQQQIRREIDSL 1010
Cdd:PRK02224 290 ELEEE---RDDLLA--------EAGLDDA----------DAEAVEARREELEDRDEELRDRLEE-CRVAAQAHNEEAESL 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622954647 1011 RQEKDSLLKQRLEIDSKLRQGSLLSPEEERTLFQLDEAIEALDAAIE 1057
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
920-1194 |
4.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 920 EKVLQQRRAL----EELGEELHKREAILAKKEALMQEKTGLE------SKRLRSSQA---LNEDIVRVSSRLEHLEKELS 986
Cdd:PRK04863 286 EEALELRRELytsrRQLAAEQYRLVEMARELAELNEAESDLEqdyqaaSDHLNLVQTalrQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 987 EKNgQLRQGSAQSQQQIRREIDSLRQEKDSLLKQ------RLEIDSK-----------LRQGSLLSPEEERTLFQLDEAI 1049
Cdd:PRK04863 366 EQN-EVVEEADEQQEENEARAEAAEEEVDELKSQladyqqALDVQQTraiqyqqavqaLERAKQLCGLPDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1050 EALDAAIEYKNEAITCRQRVLRASASLLSQCE--MNLMAKL----SYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSE 1123
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqaYQLVRKIagevSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSE 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622954647 1124 LEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLllqqsrDHLSEGLADSRRQYEARIQALE 1194
Cdd:PRK04863 525 LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL------ESLSESVSEARERRMALRQQLE 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
902-1063 |
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 1622954647 902 LEQQQKIEEQKKWLDQEMEKVLQQ----RRALEELGEELHKREAILAKKEALMQEKTGLE---SKRLRSSQALNEDIVRV 974
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREineiSSELPELREELEKLEKEVKELEELKEEIEELEkelESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 975 SSRLEHLEKELSEkngqlrqgsaqsQQQIRREIDSLRQEKDS---LLKQRLEIDSKLRQGSllspEEERTLFQLDEAIEA 1051
Cdd:PRK03918 265 EERIEELKKEIEE------------LEEKVKELKELKEKAEEyikLSEFYEEYLDELREIE----KRLSRLEEEINGIEE 328
|
170
....*....|..
gi 1622954647 1052 LDAAIEYKNEAI 1063
Cdd:PRK03918 329 RIKELEEKEERL 340
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
790-922 |
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 1622954647 790 VAAAQSQVQVLKEK-KQATERLVSLSAQSEKRLQELERnvqlmrqqqgqlqrrLREETEQ-KRRLEAEMSKRQHRVKELE 867
Cdd:PRK00409 504 IEEAKKLIGEDKEKlNELIASLEELERELEQKAEEAEA---------------LLKEAEKlKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 868 LKHEQQ-QKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKwLDQEMEKV 922
Cdd:PRK00409 569 EEAEKEaQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKK 623
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
792-1206 |
5.13e-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: 41.25 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 792 AAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKEL-ELKH 870
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMtKFKN 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 871 EQQQKILKIKT----EEIAAFQRKrrsgsngsvvsleQQQKIEEQKKWLDQEMEKVLQQRRaleelgEELHKRE----AI 942
Cdd:pfam05483 402 NKEVELEELKKilaeDEKLLDEKK-------------QFEKIAEELKGKEQELIFLLQARE------KEIHDLEiqltAI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 943 LAKKEALMQE----KTGLESKRLRSSQAL---------NEDIVRVSSRL-----EHLEKELSEKNGQLR-----QGSAQS 999
Cdd:pfam05483 463 KTSEEHYLKEvedlKTELEKEKLKNIELTahcdkllleNKELTQEASDMtlelkKHQEDIINCKKQEERmlkqiENLEEK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1000 QQQIRREIDSLRQEkdsLLKQRLEIDSKL-------RQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRA 1072
Cdd:pfam05483 543 EMNLRDELESVREE---FIQKGDEVKCKLdkseenaRSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1073 sasllsqcemnlmakLSYLSSSETRALLCkYFDKVVTLREEQHQQQIAFSEL----EMQLEEQQRLVYWLEVALERQRLE 1148
Cdd:pfam05483 620 ---------------LKKKGSAENKQLNA-YEIKVNKLELELASAKQKFEEIidnyQKEIEDKKISEEKLLEEVEKAKAI 683
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622954647 1149 MDRQLTLQQKeheqnMQLLLQQSRDHLSEGLADSRRQYEARIQALEKDLGRYMWINQE 1206
Cdd:pfam05483 684 ADEAVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-969 |
6.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 702 RLAQAQQKIRELAINIRMKEELIGELVRTGKaaqalNRQHSQRIRELE--------QEAERVRAELSEGQRQLRELEGKE 773
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEeklkkynlEELEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 774 PQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATER-LVSLSAQS----EKRLQELE---------RNVQLMRQQQGQLQ 839
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKeLEELGFESveelEERLKELEpfyneylelKDAEKELEREEKEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 840 RRLREETEQKRrleAEMSKRQHRVKELELKHEQQQKilKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEM 919
Cdd:PRK03918 622 KKLEEELDKAF---EELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622954647 920 EKVLQQRRALEELGEELHKREAILAKKEALmQEKTgLESKRLRSSQALNE 969
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEEL-REKV-KKYKALLKERALSK 744
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
739-1023 |
6.51e-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: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 739 RQHSQRIRELEQEAERVRAELSEGQRQLRELE---GKEPQDAGERSRLQE----FRRRVAAAQSQVQVLKEK-KQA---- 806
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWKHCQQKIRELElevLKQAQSIKSQNSLQEklaqEKSRVADAEEKILELQQKlEHAhkvc 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 807 -TERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRL------REETEQKRR--------LEAEMSKRQHRVKELELKHE 871
Cdd:pfam15742 145 lTDTCILEKKQLEERIKEASENEAKLKQQYQEEQQKRklldqnVNELQQQVRslqdkeaqLEMTNSQQQLRIQQQEAQLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 872 QQQKILKIKTEEIAAfqrkrrsgsngsvvsleqQQKIEEQKKWLDQEMEKVLQQ-RRALEELGEELHKReailakKEALM 950
Cdd:pfam15742 225 QLENEKRKSDEHLKS------------------NQELSEKLSSLQQEKEALQEElQQVLKQLDVHVRKY------NEKHH 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954647 951 QEKTGLEskrlRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQsQQQIRREIDSLRQEKDSLLKQRLE 1023
Cdd:pfam15742 281 HHKAKLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAF-QKQVTAQNEILLLEKRKLLEQLTE 348
|
|
| COG5223 |
COG5223 |
Uncharacterized conserved protein [Function unknown]; |
850-1028 |
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 1622954647 850 RRLEAEMSKRQHRVKELELKHEQQQKILKIKTE-------EIAAFQRKRRSGSNGSVVSLEQQQKIEEQ---KKWLDQEM 919
Cdd:COG5223 23 RRKYGKLEKKKDYVKRAQDINKKQDELKKLREKarernpdEYYHGMHSVKTDGGVSSIYREDEPTIMDLakmLKTQDNEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 920 EKVLQQ--RRALEELGEELHKREAILAKKEALMQEKTGlESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSA 997
Cdd:COG5223 103 QRCRRKleRYKPMPCGTQIKFEESSLHTIFVDMRFGQK-EFIPEEFFRTTEELVVRRENRLEKDQIENNELEDSVFSGKL 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1622954647 998 QSQQQIRREID-SLRQEKDSLLK---QRLEIDSKL 1028
Cdd:COG5223 182 HSKLKEKAATElLLRQKRDKKLAaaeERVELDRLL 216
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
818-1193 |
6.99e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 818 EKRLQELERNvqlmrqqqgqlqrrLREETEQKRRLEAEMSKRQHRVKELELKHEQ----QQKILKIKTEEIAAFQrkrrs 893
Cdd:pfam03528 7 QQRVAELEKE--------------NAEFYRLKQQLEAEFNQKRAKFKELYLAKEEdlkrQNAVLQEAQVELDALQ----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 894 gsngsvVSLEQQQkieeqkkwldQEMEKVlqqrRALEELGEELhKREAILAKKEALMQEKTGLeskrlrssQALNEDIVR 973
Cdd:pfam03528 68 ------NQLALAR----------AEMENI----KAVATVSENT-KQEAIDEVKSQWQEEVASL--------QAIMKETVR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 974 VSSRLEH--LEKELSEKNgQLRQGSAQSQQQIRREIDSLRQEK--DSLLKQRLEIDSKLRqgSLLSPEEERTLFQLDEAI 1049
Cdd:pfam03528 119 EYEVQFHrrLEQERAQWN-QYRESAEREIADLRRRLSEGQEEEnlEDEMKKAQEDAEKLR--SVVMPMEKEIAALKAKLT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1050 EALDAAIEYKNEAITCRQRVLRASASLLSQCEMnLMAKLSYLSS--SETRALLCKYFDKVVTLREEQHQQQI----AFSE 1123
Cdd:pfam03528 196 EAEDKIKELEASKMKELNHYLEAEKSCRTDLEM-YVAVLNTQKSvlQEDAEKLRKELHEVCHLLEQERQQHNqlkhTWQK 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1124 LEMQLEEQQRLvywLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLSEGLADSRRQYEARIQAL 1193
Cdd:pfam03528 275 ANDQFLESQRL---LMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAV 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
858-1020 |
7.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 858 KRQHRVKELELKhEQQQKILKIKTEEIAAFQRKRRsgsngsvvsLEQQQKIEEQKkwldQEMEKVLQQRRA-LEELGEEL 936
Cdd:PRK12704 26 KKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL---------LEAKEEIHKLR----NEFEKELRERRNeLQKLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 937 HKREAILAKK-EALMQEKTGLESKRlrssqalnedivrvsSRLEHLEKELSEKNGQLrQGSAQSQQQIRREIDSLRQE-- 1013
Cdd:PRK12704 92 LQKEENLDRKlELLEKREEELEKKE---------------KELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEea 155
|
....*..
gi 1622954647 1014 KDSLLKQ 1020
Cdd:PRK12704 156 KEILLEK 162
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
724-1170 |
7.65e-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: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 724 IGELVRTGKAAQALNRQHSQRIRELEQEAERVRA--------ELSEGQRQLRELEGKEPQDAgersrLQEFRRRVAAAQS 795
Cdd:pfam07111 189 AKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESlrkyvgeqVPPEVHSQTWELERQELLDT-----MQHLQEDRADLQA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 796 QVQVLKEKKQATERLVSLSAQS-EKRLQELERNVQLMRQQQGQLQRRLREET------EQKRRLEAEMSKRQHRVKELEL 868
Cdd:pfam07111 264 TVELLQVRVQSLTHMLALQEEElTRKIQPSDSLEPEFPKKCRSLLNRWREKVfalmvqLKAQDLEHRDSVKQLRGQVAEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 869 KHE-----QQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQK-----------IEEQKK-----------WLDQEMEK 921
Cdd:pfam07111 344 QEQvtsqsQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEarrrqqqqtasAEEQLKfvvnamsstqiWLETTMTR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 922 VLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRS---SQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQ 998
Cdd:pfam07111 424 VEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQEScppPPPAPPVDADLSLELEQLREERNRLDAELQLSAHL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 999 SQQQIRREIDSLRQEKDSLLK--QRLEIDSKLRQGSLLSPEEertlfQLDEAI----EALDAAIEYKNEAITCRQRVLRA 1072
Cdd:pfam07111 504 IQQEVGRAREQGEAERQQLSEvaQQLEQELQRAQESLASVGQ-----QLEVARqgqqESTEEAASLRQELTQQQEIYGQA 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1073 SASLLSQCEMNLMAKLSYLSS--SETRALLCKyfdKVVTLREEQHQ--QQIAFSELEMQLEEQQRLVYWLEVALERQRLE 1148
Cdd:pfam07111 579 LQEKVAEVETRLREQLSDTKRrlNEARREQAK---AVVSLRQIQHRatQEKERNQELRRLQDEARKEEGQRLARRVQELE 655
|
490 500
....*....|....*....|..
gi 1622954647 1149 MDRQLTLQQKEHEQNMQLLLQQ 1170
Cdd:pfam07111 656 RDKNLMLATLQQEGLLSRYKQQ 677
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
693-898 |
8.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 693 VPSATASEWRLAQAQQKIRELAINIrmkEELIGELVRTGKAAQALNRQHSQ---RIRELEQEAERVRAELSEGQRQLREL 769
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAEL---EAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 770 EgkepQDAGERSR--------------------LQEFRRRVAA----AQSQVQVLKEKKQATERLVSLSAQSEKRLQELE 825
Cdd:COG3883 85 R----EELGERARalyrsggsvsyldvllgsesFSDFLDRLSAlskiADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622954647 826 RNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGS 898
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
744-828 |
8.57e-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: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 744 RIRELEQEAERVRAELSEGQRQLRELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQE 823
Cdd:pfam00529 66 QLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVT 145
|
....*
gi 1622954647 824 LERNV 828
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 ... |
750-1055 |
8.92e-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: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 750 QEAERVRAELSEGQRQLR-ELEGKEPQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERlVSLSAQSEKRLQELERNv 828
Cdd:pfam01576 422 SESERQRAELAEKLSKLQsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR-QKLNLSTRLRQLEDERN- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 829 qlmrqqqgQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKI 908
Cdd:pfam01576 500 --------SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 909 EEQKKWLDQEMEKVL----QQRRALEELGEELHKREAILAKKEALmqeKTGLESKRLRSSQALNEDIVRVSSRLEHLEKE 984
Cdd:pfam01576 572 EKTKNRLQQELDDLLvdldHQRQLVSNLEKKQKKFDQMLAEEKAI---SARYAEERDRAEAEAREKETRALSLARALEEA 648
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622954647 985 LSEKNGQLRQgsaqsQQQIRREIDSLRQEKDSLLKQRLEIDsKLRQGSLLSPEEERTlfQLDEAIEALDAA 1055
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 ... |
754-1176 |
8.95e-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: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 754 RVRAELSEgqRQLRELegkepqdageRSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSE---KRLQ---ELERN 827
Cdd:pfam05622 86 RIKCEELE--KEVLEL----------QHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVEtykKKLEdlgDLRRQ 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 828 VQLMRQQQGQLQRRLREETEQKRRLEA-----EMSKRQhrVKELELKHEQQQKilkiKTEEiAAFQRKrrsgsngsvvsl 902
Cdd:pfam05622 154 VKLLEERNAEYMQRTLQLEEELKKANAlrgqlETYKRQ--VQELHGKLSEESK----KADK-LEFEYK------------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 903 eqqqKIEEQKKWLDQEMEKVLQQRRALEELGEELH---------KREAILAKKEALMQEKTG----------------LE 957
Cdd:pfam05622 215 ----KLEEKLEALQKEKERLIIERDTLRETNEELRcaqlqqaelSQADALLSPSSDPGDNLAaeimpaeireklirlqHE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 958 SKRLRSSQ--ALNEDIVRVSSRLEHLEKELSEKNGQLRQgsaqSQQQIRreidSLRQEKDSLLKQRLEIDSKLRQGSLLS 1035
Cdd:pfam05622 291 NKMLRLGQegSYRERLTELQQLLEDANRRKNELETQNRL----ANQRIL----ELQQQVEELQKALQEQGSKAEDSSLLK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 1036 PEEERTLFQLDEAIEALDAAIEYKNEAitcRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQH 1115
Cdd:pfam05622 363 QKLEEHLEKLHEAQSELQKKKEQIEEL---EPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPK 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622954647 1116 QQQIAFSE---LEMQLEEQQRLVYWLEVALERQRL--EMDRQL----------TLQQKEHEQNMQLLLQQSRDHLS 1176
Cdd:pfam05622 440 QNPASPPEiqaLKNQLLEKDKKIEHLERDFEKSKLqrEQEEKLivtawynmgmALHRKAIEERLAGLSSPGQSFLA 515
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
710-1062 |
9.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 710 IRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAERVRAELSEGQRQLRELEgkepqdagerSRLQEFRRR 789
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN----------EQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 790 VAAAQSQVQVLKEKKQATERLVslsAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELE-- 867
Cdd:COG4372 96 LAQAQEELESLQEEAEELQEEL---EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 868 -LKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEEL-GEELHKREAILAK 945
Cdd:COG4372 173 lQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALlDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622954647 946 KEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKNGQLRQGSAQSQQQIRREIDSLRQEKDSLLKQRLEID 1025
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622954647 1026 SKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEA 1062
Cdd:COG4372 333 AILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| |
