|
Name |
Accession |
Description |
Interval |
E-value |
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
1-346 |
6.24e-29 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 114.37 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 1 MIKEISLKNFKCF-NELYL------KQLKTLNIIAGKNNYGKTSILDAIFCFYDVKNPAVLLN---IQAFRKEMAEINKN 70
Cdd:COG1106 1 MLISFSIENFRSFkDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGdklVEPFLLDSESKNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 71 KPFWVSYFHDmdtsqkmsivirdersEVTQTYETETNQRLESSLSLNVDTVLSNQNIPRqtigSQATVNSLKINVTETPN 150
Cdd:COG1106 81 SEFEILFLLD----------------GVRYEYGFELDKERIISEWLYFLSTAAQLNVPL----LSPLYDWFDNNISLDTS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 151 AKNrvsnklFSMQLKEDgveikseiknerdginykfktatiittsrkinkeatitnvsslltQKRKKDILENLKKIDDRI 230
Cdd:COG1106 141 SDG------LTLLLKED---------------------------------------------ESLKEELLELLKIADPGI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 231 VDIAI-----SAIGNNKEIYLDIGFSELNEISMLGEGISRALSFISSVL--VQENSIILIDEIENGIHYSVIKDIIKSLI 303
Cdd:COG1106 170 EDIEVeeeeiEDLVERKLIFKHKGGNVPLPLSEESDGTKRLLALAGALLdaLAKGGVLLIDEIEASLHPSLLRKLLKLFL 249
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2244495206 304 SSAKQNNNQIFATTHSQDVIRAINEIDSKNEdiaYIRLGREKN 346
Cdd:COG1106 250 DLANKNNAQLIFTTHSTELLDAFLELLRRDQ---IWFVEKDKD 289
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
24-324 |
1.35e-17 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 82.44 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 24 LNIIAGKNNYGKTSILDAIFCFYDVKNPAVLLNIQAFRKEMAEINKNKP----------FWVSYFHDMDTSQKMSIVIRD 93
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLngidpkepieFEISEFLEDGVRYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 94 ERSEvtqTYETETNQRLESSLSLNVDTVLSNQNIPRQTIGSQATVNSLKINVTETPNAKNRVSNKLFSmqlkEDGVEIKS 173
Cdd:pfam13304 81 EDVE---EKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLL----SIISPLSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 174 EIKNERDGINYKFKTATIITTSRKINKEATItnVSSLLTQKRKKDILENLKKIDDRIVDIAISAIGNNKEIYLDIGFSEL 253
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKEL--LQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244495206 254 NEISMLGEGISRALSFISSVL--VQENSIILIDEIENGIHYSVIKDIIKsLISSAKQNNNQIFATTHSQDVIR 324
Cdd:pfam13304 232 LPAFELSDGTKRLLALLAALLsaLPKGGLLLIDEPESGLHPKLLRRLLE-LLKELSRNGAQLILTTHSPLLLD 303
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
2-43 |
1.45e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 40.14 E-value: 1.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAIF 43
Cdd:PRK00064 3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIY 44
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
2-42 |
2.03e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 39.12 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAI 42
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTAL 41
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
1-346 |
6.24e-29 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 114.37 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 1 MIKEISLKNFKCF-NELYL------KQLKTLNIIAGKNNYGKTSILDAIFCFYDVKNPAVLLN---IQAFRKEMAEINKN 70
Cdd:COG1106 1 MLISFSIENFRSFkDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGdklVEPFLLDSESKNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 71 KPFWVSYFHDmdtsqkmsivirdersEVTQTYETETNQRLESSLSLNVDTVLSNQNIPRqtigSQATVNSLKINVTETPN 150
Cdd:COG1106 81 SEFEILFLLD----------------GVRYEYGFELDKERIISEWLYFLSTAAQLNVPL----LSPLYDWFDNNISLDTS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 151 AKNrvsnklFSMQLKEDgveikseiknerdginykfktatiittsrkinkeatitnvsslltQKRKKDILENLKKIDDRI 230
Cdd:COG1106 141 SDG------LTLLLKED---------------------------------------------ESLKEELLELLKIADPGI 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 231 VDIAI-----SAIGNNKEIYLDIGFSELNEISMLGEGISRALSFISSVL--VQENSIILIDEIENGIHYSVIKDIIKSLI 303
Cdd:COG1106 170 EDIEVeeeeiEDLVERKLIFKHKGGNVPLPLSEESDGTKRLLALAGALLdaLAKGGVLLIDEIEASLHPSLLRKLLKLFL 249
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2244495206 304 SSAKQNNNQIFATTHSQDVIRAINEIDSKNEdiaYIRLGREKN 346
Cdd:COG1106 250 DLANKNNAQLIFTTHSTELLDAFLELLRRDQ---IWFVEKDKD 289
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
24-324 |
1.35e-17 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 82.44 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 24 LNIIAGKNNYGKTSILDAIFCFYDVKNPAVLLNIQAFRKEMAEINKNKP----------FWVSYFHDMDTSQKMSIVIRD 93
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLngidpkepieFEISEFLEDGVRYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 94 ERSEvtqTYETETNQRLESSLSLNVDTVLSNQNIPRQTIGSQATVNSLKINVTETPNAKNRVSNKLFSmqlkEDGVEIKS 173
Cdd:pfam13304 81 EDVE---EKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLL----SIISPLSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 174 EIKNERDGINYKFKTATIITTSRKINKEATItnVSSLLTQKRKKDILENLKKIDDRIVDIAISAIGNNKEIYLDIGFSEL 253
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKEL--LQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2244495206 254 NEISMLGEGISRALSFISSVL--VQENSIILIDEIENGIHYSVIKDIIKsLISSAKQNNNQIFATTHSQDVIR 324
Cdd:pfam13304 232 LPAFELSDGTKRLLALLAALLsaLPKGGLLLIDEPESGLHPKLLRRLLE-LLKELSRNGAQLILTTHSPLLLD 303
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-328 |
3.12e-14 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 73.04 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 1 MIKEISLKNFKCFNELYLKqLKTLNIIAGKNNYGKTSILDAIfcfydvknpAVLLNI------QAFRKE--MAEInknkp 72
Cdd:COG4637 1 MITRIRIKNFKSLRDLELP-LGPLTVLIGANGSGKSNLLDAL---------RFLSDAargglqDALARRggLEEL----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 73 FWvsyFHDMDTSQKMSIVIR-DERSEVTQTYE-----TETNQR-------LESSLSLNVDTVLSNQNIPRQTIGSQATVN 139
Cdd:COG4637 66 LW---RGPRTITEPIRLELEfAEEDERDLRYElelglPEPGGRpevkeerLWLKRGSGGRPFLDFRPKGRAVGGEPERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 140 SLKINVTETPNAKNRvsnklfsmqlkEDGVEIKSEIKNER--DGINYKFKTATIITTSRKINKEATitNVSSLL------ 211
Cdd:COG4637 143 SPESLLSQLGDPERF-----------PELRALREALRSWRfyDFHPAPLRQPQPAGRTPVLAPDGS--NLAAVLatlret 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 212 TQKRKKDILENLKKIDDRIVDIAISAIGNNKeIYL---DIGFSELNEISMLGEGISRALSFISSVL-VQENSIILIDEIE 287
Cdd:COG4637 210 HPERFERILEALRDAFPGFEDIEVEPDEDGR-VLLefrEKGLDRPFPARELSDGTLRFLALLAALLsPRPPPLLCIEEPE 288
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2244495206 288 NGIHYSVIKDIIKSLISSAKQnnNQIFATTHSQDVIRAINE 328
Cdd:COG4637 289 NGLHPDLLPALAELLREASER--TQVIVTTHSPALLDALEP 327
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-359 |
4.56e-13 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 69.65 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAIFCFYDVknpavllniqafrkemaeiNKNKPFWVSYFHDM 81
Cdd:COG3593 3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGP-------------------SSSRKFDEEDFYLG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 82 DTSQKMSIVIrdersevtqtyetetnqrlesslSLNVDTVLSnqniprqtigsqatvnslkinvtetpnaknRVSNKLFS 161
Cdd:COG3593 64 DDPDLPEIEI-----------------------ELTFGSLLS------------------------------RLLRLLLK 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 162 mqlKEDGVEIKSEIKNERDGINYKFKTATiittsrkinkeATITNVSSLLTQKRKKDILENLKKIDDRIVDIAISaIGNN 241
Cdd:COG3593 91 ---EEDKEELEEALEELNEELKEALKALN-----------ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLR-IEDG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 242 KEIyldigfselnEISMLGEGISRALSFISSVLVQE------NSIILIDEIENGIHYSVIKDIIKSLISSAKqNNNQIFA 315
Cdd:COG3593 156 KEL----------PLDRLGSGFQRLILLALLSALAElkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSE-KPNQVII 224
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2244495206 316 TTHSQDVIRAINeidskNEDIayIRLGREKNSLKPTAVQFNMDD 359
Cdd:COG3593 225 TTHSPHLLSEVP-----LENI--RRLRRDSGGTTSTKLIDLDDE 261
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
2-323 |
6.51e-12 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 66.08 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAIFCFYDVKNP------------AVLLNIQAFRKEMAEINK 69
Cdd:pfam13175 3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIFLNNKEKffeddflvlylkDVIKIDKEDLNIFENISF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 70 NKPFWVSYFHDMDTSQKMSIVIRDERSEVTQTYET------ETNQRLESSLSLNVDTVLSNQNIPRQTIGSQATVNSLKI 143
Cdd:pfam13175 83 SIDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKEyektlhPKGANKADLLLELKISDLKKYLKQFKIYIYNNYYLDEKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 144 NVTETPNAKNRVSNKLFSMQLKEDGVEIKSE-----------IKNERDGINYKFKTATIITTSRKINKEATITNVSSLLT 212
Cdd:pfam13175 163 NVFDKKSKYELPSLKEEFLNSEKEEIKVDKEdlkklinelekSINYHENVLENLQIKKLLISADRNASDEDSEKINSLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 213 Q----------KRKKDILENLKKIDDRIVDIAISAIGNNKEIYLDIGFSELN--------------------EISMLGEG 262
Cdd:pfam13175 243 AlkqrifeealQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKIDKLKDfgyppflnpeieikkddedlPLNKNGSG 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 263 ISRALSFI---------SSVLVQENSIILIDEIENGIHYSVIKDIIKSLISSAKQNNNQIFATTHSQDVI 323
Cdd:pfam13175 323 VQRLILLIffiaeaerkEDEIEEKNVILAIEEPEAHLHPQAQRVLIKLLKELANDNKTQVIITTHSPHII 392
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-328 |
1.97e-10 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 60.78 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 1 MIKEISLKNFKCFN--ELYLKQLKTLNIIAGKNNYGKTSILDAIF-CFYDVKNPAVLLNIQAFRKEMAEINKNKPFWVSY 77
Cdd:COG3950 2 RIKSLTIENFRGFEdlEIDFDNPPRLTVLVGENGSGKTTLLEAIAlALSGLLSRLDDVKFRKLLIRNGEFGDSAKLILYY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 78 fhdmDTSQKMSIVIRDERSEVTQTYETETnQRLESSLSlnvdtvlsnqniprqtigsqatvnslkinvtetpnakNRVSN 157
Cdd:COG3950 82 ----GTSRLLLDGPLKKLERLKEEYFSRL-DGYDSLLD-------------------------------------EDSNL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 158 KLFSMQLKEDGVEIKSEIKNErdginykfktatiittsrkinKEATITNVSSLLtqkrkKDILENLKKIDDRIVDIAISA 237
Cdd:COG3950 120 REFLEWLREYLEDLENKLSDE---------------------LDEKLEAVREAL-----NKLLPDFKDIRIDRDPGRLVI 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 238 IGNNKEiylDIGFSEL-----NEISMLGEGISRA--LSFISSVLVQENSIILIDEIENGIHYSVIKDIIKSLISSAKqnN 310
Cdd:COG3950 174 LDKNGE---ELPLNQLsdgerSLLALVGDLARRLaeLNPALENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKIFP--N 248
|
330
....*....|....*...
gi 2244495206 311 NQIFATTHSQDVIRAINE 328
Cdd:COG3950 249 IQFIVTTHSPLILSSLED 266
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
2-47 |
1.64e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 51.89 E-value: 1.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2244495206 2 IKEISLKNFKCFNELYLkQLKTLNIIAGKNNYGKTSILDAIFCFYD 47
Cdd:COG4938 1 IKSISIKNFGPFKEAEL-ELKPLTLLIGPNGSGKSTLIQALLLLLQ 45
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1-46 |
2.14e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 2.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2244495206 1 MIKEISLKNFKCFNELYLKQL-KTLNIIAGKNNYGKTSILDAI-FCFY 46
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFdDGLNLIVGPNGAGKSTILEAIrYALY 48
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-43 |
3.20e-05 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 45.53 E-value: 3.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAIF 43
Cdd:COG1195 2 LKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAIY 43
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-217 |
1.52e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 42.10 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 5 ISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAI-FCFYDVKNPAVLLNIQAFRKEMAEINKNKpfwvsyfhdmDT 83
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIkLALYGKTSRLKRKSGGGFVKGDIRIGLEG----------KG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2244495206 84 SQKMSIVIRDERSEVTQTYETETNQRLESSLSLnvdtvlsnqnipRQTIGSQATVNSLKINVTETPNAKNRVSNKLFSMQ 163
Cdd:pfam13476 71 KAYVEITFENNDGRYTYAIERSRELSKKKGKTK------------KKEILEILEIDELQQFISELLKSDKIILPLLVFLG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2244495206 164 LKEDGVEIKSEIKNERDGINYKFKTATIIttSRKINKEATITNVSSLLTQKRKK 217
Cdd:pfam13476 139 QEREEEFERKEKKERLEELEKALEEKEDE--KKLLEKLLQLKEKKKELEELKEE 190
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
2-43 |
1.45e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 40.14 E-value: 1.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAIF 43
Cdd:PRK00064 3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIY 44
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| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
2-42 |
2.03e-03 |
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ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 39.12 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAI 42
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTAL 41
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| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
2-45 |
2.83e-03 |
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The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.44 E-value: 2.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2244495206 2 IKEISLKNFKCFNELYLKQL-KTLNIIAGKNNYGKTSILDAIfCF 45
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGsNSFNAIVGPNGSGKSNIVDAI-CF 44
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| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-43 |
3.71e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.36 E-value: 3.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKT-LNIIAGKNNYGKTSILDAIF 43
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSpLTLIVGQNGAGKTTIIEALK 43
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| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
2-43 |
5.16e-03 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 38.05 E-value: 5.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAIF 43
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAIS 42
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| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
2-42 |
6.71e-03 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 37.58 E-value: 6.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2244495206 2 IKEISLKNFKCFNELYLKQLKTLNIIAGKNNYGKTSILDAI 42
Cdd:cd03277 3 IVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAI 43
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