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Conserved domains on  [gi|496418241|ref|WP_009127088|]
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MULTISPECIES: AAA family ATPase [Bacteroidaceae]

Protein Classification

COG3950 family protein( domain architecture ID 11467691)

COG3950 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-356 2.56e-58

Predicted ATP-binding protein involved in virulence [General function prediction only];


:

Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 192.91  E-value: 2.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFN--GNLTVVIGNNTAGKTTLLKALQVGLGAYLQSLktlpggtsyrrnfssldkfmrfdq 78
Cdd:COG3950    1 MRIKSLTIENFRGFEDLEIDFDnpPRLTVLVGENGSGKTTLLEAIALALSGLLSRL------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  79 elrdyvpntekpritihadfpittssdghcPEVSFIPIRwyreyagnytthtrvsagelidavhhmehLRNEEKENSiYP 158
Cdd:COG3950   57 ------------------------------DDVKFRKLL-----------------------------IRNGEFGDS-AK 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 159 LVLSFGAKRT-SDAQAKSKSTVKERASRIEKAYKFALHDKVDFEGAMEWLKHYDKNI--KDRKEFEGTREAFFEALQQAI 235
Cdd:COG3950   77 LILYYGTSRLlLDGPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLenKLSDELDEKLEAVREALNKLL 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 236 PALSEIDFDNGEIEAVVSVTGHTPSRhhFSYMSDGLQSMINIVAEIAHRCIELNGFLGqhAIKMTPGIVMIDEIDLYLHP 315
Cdd:COG3950  157 PDFKDIRIDRDPGRLVILDKNGEELP--LNQLSDGERSLLALVGDLARRLAELNPALE--NPLEGEGIVLIDEIDLHLHP 232
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 496418241 316 HWQKHVLQDLTNAFPMIQFIVSTHSPFIVQSLQEGQLVSFD 356
Cdd:COG3950  233 KWQRRILPDLRKIFPNIQFIVTTHSPLILSSLEDEEVIVLE 273
 
Name Accession Description Interval E-value
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-356 2.56e-58

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 192.91  E-value: 2.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFN--GNLTVVIGNNTAGKTTLLKALQVGLGAYLQSLktlpggtsyrrnfssldkfmrfdq 78
Cdd:COG3950    1 MRIKSLTIENFRGFEDLEIDFDnpPRLTVLVGENGSGKTTLLEAIALALSGLLSRL------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  79 elrdyvpntekpritihadfpittssdghcPEVSFIPIRwyreyagnytthtrvsagelidavhhmehLRNEEKENSiYP 158
Cdd:COG3950   57 ------------------------------DDVKFRKLL-----------------------------IRNGEFGDS-AK 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 159 LVLSFGAKRT-SDAQAKSKSTVKERASRIEKAYKFALHDKVDFEGAMEWLKHYDKNI--KDRKEFEGTREAFFEALQQAI 235
Cdd:COG3950   77 LILYYGTSRLlLDGPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLenKLSDELDEKLEAVREALNKLL 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 236 PALSEIDFDNGEIEAVVSVTGHTPSRhhFSYMSDGLQSMINIVAEIAHRCIELNGFLGqhAIKMTPGIVMIDEIDLYLHP 315
Cdd:COG3950  157 PDFKDIRIDRDPGRLVILDKNGEELP--LNQLSDGERSLLALVGDLARRLAELNPALE--NPLEGEGIVLIDEIDLHLHP 232
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 496418241 316 HWQKHVLQDLTNAFPMIQFIVSTHSPFIVQSLQEGQLVSFD 356
Cdd:COG3950  233 KWQRRILPDLRKIFPNIQFIVTTHSPLILSSLEDEEVIVLE 273
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
25-344 7.09e-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: 80.90  E-value: 7.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   25 LTVVIGNNTAGKTTLLKALQVGLG--AYLQSLKTLPGGTS----YRRNFSSLDKFMRFDQELRDYVPNTEKPRITIHADF 98
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADfdALVIGLTDERSRNGgiggIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   99 PITTSSDGHCPEV--SFIPIRWYREYAGNYTTHTRVSAGELIDAVHHMEHLRNEEKENSIYPLVLSFGAkrtsdaqAKSK 176
Cdd:pfam13304  81 EDVEEKLSSKPTLleKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIIS-------PLSF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  177 STVKERASRIEKAYKFALHDKvdfegamewLKHYDKNIKDRKEFEGTREAFFEALQQAIPALSEIDFDNGEIEAVVSVTG 256
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAAD---------LALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  257 HTPSRHHFSY--MSDGLQSMINIVAEIahrcielngflgqHAIKMTPGIVMIDEIDLYLHPHWQKHVLQDLTN-AFPMIQ 333
Cdd:pfam13304 225 ENGGGGELPAfeLSDGTKRLLALLAAL-------------LSALPKGGLLLIDEPESGLHPKLLRRLLELLKElSRNGAQ 291
                         330
                  ....*....|.
gi 496418241  334 FIVSTHSPFIV 344
Cdd:pfam13304 292 LILTTHSPLLL 302
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-47 6.94e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 6.94e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGL 47
Cdd:PRK03918   1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGL 47
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
3-56 1.82e-05

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: 46.14  E-value: 1.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496418241   3 IKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKAlqVGLGAYLQSLKT 56
Cdd:cd03242    1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEA--ISLLATGKSHRT 52
retron_eff_Eco8 NF038234
retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner ...
266-347 3.16e-03

retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner next to a reverse transcriptase in Eco8 type retron systems, is a predicted OLD family endonuclease.


Pssm-ID: 468422 [Multi-domain]  Cd Length: 679  Bit Score: 40.01  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 266 YMSDGLQS------MINIVAEIAHRCIelngflgqhaikMTPgIVMIDEIDLYLHPH---------WQKHVLQDLTNAFP 330
Cdd:NF038234 245 TQSDGTNSfnfiklFLNLLITLSRREY------------ITP-FIFIDEPELGLHPKlneqlineiYESYSFKKKDNKTP 311
                         90
                 ....*....|....*..
gi 496418241 331 MIQFIVSTHSPFIVQSL 347
Cdd:NF038234 312 YPKIILATHSPRIIKNI 328
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
1-79 4.28e-03

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 39.26  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241    1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQvglgaylqslkTLPGGTSYRrnfSSLDK-FMRFDQE 79
Cdd:TIGR00611   1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIY-----------YLALGRSHR---TSRDKpLIRFGAE 66
 
Name Accession Description Interval E-value
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
1-356 2.56e-58

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 192.91  E-value: 2.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFN--GNLTVVIGNNTAGKTTLLKALQVGLGAYLQSLktlpggtsyrrnfssldkfmrfdq 78
Cdd:COG3950    1 MRIKSLTIENFRGFEDLEIDFDnpPRLTVLVGENGSGKTTLLEAIALALSGLLSRL------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  79 elrdyvpntekpritihadfpittssdghcPEVSFIPIRwyreyagnytthtrvsagelidavhhmehLRNEEKENSiYP 158
Cdd:COG3950   57 ------------------------------DDVKFRKLL-----------------------------IRNGEFGDS-AK 76
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 159 LVLSFGAKRT-SDAQAKSKSTVKERASRIEKAYKFALHDKVDFEGAMEWLKHYDKNI--KDRKEFEGTREAFFEALQQAI 235
Cdd:COG3950   77 LILYYGTSRLlLDGPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLEWLREYLEDLenKLSDELDEKLEAVREALNKLL 156
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 236 PALSEIDFDNGEIEAVVSVTGHTPSRhhFSYMSDGLQSMINIVAEIAHRCIELNGFLGqhAIKMTPGIVMIDEIDLYLHP 315
Cdd:COG3950  157 PDFKDIRIDRDPGRLVILDKNGEELP--LNQLSDGERSLLALVGDLARRLAELNPALE--NPLEGEGIVLIDEIDLHLHP 232
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 496418241 316 HWQKHVLQDLTNAFPMIQFIVSTHSPFIVQSLQEGQLVSFD 356
Cdd:COG3950  233 KWQRRILPDLRKIFPNIQFIVTTHSPLILSSLEDEEVIVLE 273
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
1-344 2.04e-21

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: 95.07  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGLGaylqslktlpggTSYRRNFSSLDkFMRFDqel 80
Cdd:COG3593    1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLG------------PSSSRKFDEED-FYLGD--- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  81 rdyvpNTEKPRITIHADFpittssdghcpevsfipirwyreyagnytthtrvsaGELIDAVhhMEHLRNEEKENSIyplv 160
Cdd:COG3593   65 -----DPDLPEIEIELTF------------------------------------GSLLSRL--LRLLLKEEDKEEL---- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 161 lsfgakrtsdaqakskstvKERASRIEKAYKFALHDkvdfegAMEWLKHYDKNIKDRKEFEgtreaffealqqaipaLSE 240
Cdd:COG3593   98 -------------------EEALEELNEELKEALKA------LNELLSEYLKELLDGLDLE----------------LEL 136
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 241 IDFDNGEIEAVVSVTGHTPSRHHFSYMSDGLQSMInivaeiahrCIELNGFLGQHAIKMTPGIVMIDEIDLYLHPHWQKH 320
Cdd:COG3593  137 SLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLI---------LLALLSALAELKRAPANPILLIEEPEAHLHPQAQRR 207
                        330       340
                 ....*....|....*....|....*
gi 496418241 321 VLQDLTN-AFPMIQFIVSTHSPFIV 344
Cdd:COG3593  208 LLKLLKElSEKPNQVIITTHSPHLL 232
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
25-344 7.09e-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: 80.90  E-value: 7.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   25 LTVVIGNNTAGKTTLLKALQVGLG--AYLQSLKTLPGGTS----YRRNFSSLDKFMRFDQELRDYVPNTEKPRITIHADF 98
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADfdALVIGLTDERSRNGgiggIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   99 PITTSSDGHCPEV--SFIPIRWYREYAGNYTTHTRVSAGELIDAVHHMEHLRNEEKENSIYPLVLSFGAkrtsdaqAKSK 176
Cdd:pfam13304  81 EDVEEKLSSKPTLleKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIIS-------PLSF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  177 STVKERASRIEKAYKFALHDKvdfegamewLKHYDKNIKDRKEFEGTREAFFEALQQAIPALSEIDFDNGEIEAVVSVTG 256
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAAD---------LALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  257 HTPSRHHFSY--MSDGLQSMINIVAEIahrcielngflgqHAIKMTPGIVMIDEIDLYLHPHWQKHVLQDLTN-AFPMIQ 333
Cdd:pfam13304 225 ENGGGGELPAfeLSDGTKRLLALLAAL-------------LSALPKGGLLLIDEPESGLHPKLLRRLLELLKElSRNGAQ 291
                         330
                  ....*....|.
gi 496418241  334 FIVSTHSPFIV 344
Cdd:pfam13304 292 LILTTHSPLLL 302
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
1-344 3.53e-14

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: 73.79  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241    1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQV------------GLGAYLQSLKT------------ 56
Cdd:pfam13175   1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEALDIflnnkekffeddFLVLYLKDVIKidkedlnifeni 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   57 ------------LPGGTSYRRNFSSLDKFMRFDQELRDYVPNTEKPRITIHADFPITTSSDGHCPEVSFIPIRWYREYAG 124
Cdd:pfam13175  81 sfsidieidvefLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFKIYIYNNYYLDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  125 NYTTHTRVSAGELIDAVHHMEHLRNEEKE------------------------NSIYPLVLSFGAKR-----TSDAQAKS 175
Cdd:pfam13175 161 KKNVFDKKSKYELPSLKEEFLNSEKEEIKvdkedlkklineleksinyhenvlENLQIKKLLISADRnasdeDSEKINSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  176 KSTVKERASR---------IEKAYKF-ALHDKVDFEGAMEWLKHYDKNIKDRKEFEGTREAFFEalqqaipalSEIDFDN 245
Cdd:pfam13175 241 LGALKQRIFEealqeelelTEKLKETqNKLKEIDKTLAEELKNILFKKIDKLKDFGYPPFLNPE---------IEIKKDD 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  246 GEIEAvvsvtghtpsrhhfSYMSDGLQSMINIVAEIAHRcielngFLGQHAIKMTPGIVMIDEIDLYLHPHWQKHV---L 322
Cdd:pfam13175 312 EDLPL--------------NKNGSGVQRLILLIFFIAEA------ERKEDEIEEKNVILAIEEPEAHLHPQAQRVLiklL 371
                         410       420
                  ....*....|....*....|..
gi 496418241  323 QDLTNAFPMiQFIVSTHSPFIV 344
Cdd:pfam13175 372 KELANDNKT-QVIITTHSPHII 392
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
3-349 4.56e-14

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 72.77  E-value: 4.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   3 IKEVNIVNFKGFQNEtVTFN--------GNLTVVIGNNTAGKTTLLKALQVGLGAYLQSLKtlpggtsyrrNFSSLDKFM 74
Cdd:COG1106    2 LISFSIENFRSFKDE-LTLSmvasglrlLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQ----------PGDKLVEPF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  75 RFDQELRDyvpnteKPritihADFpittssdghcpEVSFIPIRWYREYagnytthtRVSAGEliDAVHHmEHLRneeken 154
Cdd:COG1106   71 LLDSESKN------EP-----SEF-----------EILFLLDGVRYEY--------GFELDK--ERIIS-EWLY------ 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 155 siyplVLSFGAKRTSDAqakskstvkerasrIEKAYKFaLHDKVDFEGAMEwlkHYDKNIKDRKEFEgtrEAFFEALQQA 234
Cdd:COG1106  112 -----FLSTAAQLNVPL--------------LSPLYDW-FDNNISLDTSSD---GLTLLLKEDESLK---EELLELLKIA 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 235 IPALSEIDFDNGEIEAVVS---VTGHTPSRHHFSY--MSDGLQSMINIVAEIAHrcielngflgqhaIKMTPGIVMIDEI 309
Cdd:COG1106  166 DPGIEDIEVEEEEIEDLVErklIFKHKGGNVPLPLseESDGTKRLLALAGALLD-------------ALAKGGVLLIDEI 232
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 496418241 310 DLYLHPHWQKHVLQ---DLTNAFPmIQFIVSTHSPFIVQSLQE 349
Cdd:COG1106  233 EASLHPSLLRKLLKlflDLANKNN-AQLIFTTHSTELLDAFLE 274
COG4637 COG4637
Predicted ATPase [General function prediction only];
2-358 5.58e-13

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 69.96  E-value: 5.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   2 RIKEVNIVNFKGFQNETVTFnGNLTVVIGNNTAGKTTLLKALQV-------GLGAYLQSLktlpGGTSYRRNFSSLDKFM 74
Cdd:COG4637    1 MITRIRIKNFKSLRDLELPL-GPLTVLIGANGSGKSNLLDALRFlsdaargGLQDALARR----GGLEELLWRGPRTITE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241  75 RFdqELRDYVPNTEKPRITIHADFPITTSSDGhcPEVSfipirwyREYAgnyTTHTRVSAGELIDAVHHMEHLRNEEKEN 154
Cdd:COG4637   76 PI--RLELEFAEEDERDLRYELELGLPEPGGR--PEVK-------EERL---WLKRGSGGRPFLDFRPKGRAVGGEPERL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 155 SIYPLVLSfgaKRTSDAQAKSKSTVKERasrIEKAYKFALHD----KVDFEGAMEWLKHYDKNIKD-----RKEFEGTRE 225
Cdd:COG4637  142 DSPESLLS---QLGDPERFPELRALREA---LRSWRFYDFHPaplrQPQPAGRTPVLAPDGSNLAAvlatlRETHPERFE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 226 AFFEALQQAIPALSEIDF---DNGEIEAVVSvtgHTPSRHHFS--YMSDGLQSMINIVAEIAHRcielngflgqhaikMT 300
Cdd:COG4637  216 RILEALRDAFPGFEDIEVepdEDGRVLLEFR---EKGLDRPFParELSDGTLRFLALLAALLSP--------------RP 278
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496418241 301 PGIVMIDEIDLYLHPHWQKHVLQDLTNAFPMIQFIVSTHSPFIVQSLQEGQLVSFDPN 358
Cdd:COG4637  279 PPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDALEPEEVLVLERE 336
AAA_23 pfam13476
AAA domain;
6-219 1.90e-10

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 59.82  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241    6 VNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGLGAYLQSLKTLPGGTSyrrnfssldkfmrFDQELRDYVP 85
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGF-------------VKGDIRIGLE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   86 NTEKPRITIHadfpITTSSDGHCPEvsfipIRWYREYAGNYTTHTRVSAGELIDAVHHMEHLRNE-EKENSIYPLVLSFG 164
Cdd:pfam13476  68 GKGKAYVEIT----FENNDGRYTYA-----IERSRELSKKKGKTKKKEILEILEIDELQQFISELlKSDKIILPLLVFLG 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 496418241  165 AKRTsdaQAKSKSTVKERASRIEKAYKFALHDKvDFEGAMEWLKHYDKNIKDRKE 219
Cdd:pfam13476 139 QERE---EEFERKEKKERLEELEKALEEKEDEK-KLLEKLLQLKEKKKELEELKE 189
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-52 1.52e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 1.52e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGLGAYLQ 52
Cdd:COG4717    1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAMLLERLE 52
COG4938 COG4938
Predicted ATPase [General function prediction only];
201-356 1.11e-06

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 49.97  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 201 EGAMEWLKHYDKNIKDRKEFEGTREAFFEALQQAIPALSEIDFDNGEIEAVVSVTGhTPSRHHFSYMSDGLQSMINIVAE 280
Cdd:COG4938   77 EYTADFLAELENLEILDDKSKELLEQVEEWLEKIFPGKVEVDASSDLVRLVFRPSG-NGKRIPLSNVGSGVSELLPILLA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 281 IAHRCIElngflgqhaikmtPGIVMIDEIDLYLHPHWQKHVLQDLTNAFPM-IQFIVSTHSPFIVQSLQ----EGQLVSF 355
Cdd:COG4938  156 LLSAAKP-------------GSLLIIEEPEAHLHPKAQSALAELLAELANSgVQVIIETHSDYILNGLRnlikEGKLLDP 222

                 .
gi 496418241 356 D 356
Cdd:COG4938  223 D 223
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
2-47 3.28e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 47.70  E-value: 3.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496418241   2 RIKEVNIVNFKGFQN-ETVTFNGNLTVVIGNNTAGKTTLLKALQVGL 47
Cdd:COG0419    1 KLLRLRLENFRSYRDtETIDFDDGLNLIVGPNGAGKSTILEAIRYAL 47
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1-47 6.94e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 6.94e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGL 47
Cdd:PRK03918   1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGL 47
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
2-79 9.92e-06

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 47.46  E-value: 9.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496418241   2 RIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALqvglgaYLQSLktlpgGTSYRRnfSSLDKFMRFDQE 79
Cdd:COG1195    1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAI------YLLAT-----GRSFRT--ARDAELIRFGAD 65
recF PRK00064
recombination protein F; Reviewed
1-79 1.61e-05

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 46.69  E-value: 1.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKAlqVGLGAYLQSLKTlpggtsyrrnfSSLDKFMRFDQE 79
Cdd:PRK00064   1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEA--IYLLAPGRSHRT-----------ARDKELIRFGAE 66
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
3-56 1.82e-05

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: 46.14  E-value: 1.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496418241   3 IKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKAlqVGLGAYLQSLKT 56
Cdd:cd03242    1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEA--ISLLATGKSHRT 52
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
3-60 1.11e-04

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 42.84  E-value: 1.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496418241   3 IKEVNIVNFKGFQNET-VTFNGNLTVVIGNNTAGKTTLLKALQVGLGayLQSLKTLPGG 60
Cdd:cd03278    1 LKKLELKGFKSFADKTtIPFPPGLTAIVGPNGSGKSNIIDAIRWVLG--EQSAKSLRGE 57
recF PRK14079
recombination protein F; Provisional
1-51 1.36e-04

recombination protein F; Provisional


Pssm-ID: 184491 [Multi-domain]  Cd Length: 349  Bit Score: 44.01  E-value: 1.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGLGAYL 51
Cdd:PRK14079   1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTGEL 51
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
3-47 1.83e-04

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: 42.59  E-value: 1.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 496418241   3 IKEVNIVNFKGF-QNETVTFNGNLTVVIGNNTAGKTTLLKALQVGL 47
Cdd:cd03240    1 IDKLSIRNIRSFhERSEIEFFSPLTLIVGQNGAGKTTIIEALKYAL 46
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-43 4.74e-04

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 41.61  E-value: 4.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496418241   1 MRIKEVNIVNFKGFQNETVTFNG-NLTV-------VIGNNTAGKTTLLKAL 43
Cdd:COG1101    2 LELKNLSKTFNPGTVNEKRALDGlNLTIeegdfvtVIGSNGAGKSTLLNAI 52
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1-73 5.24e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 40.42  E-value: 5.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496418241   1 MRIKEVNIVNFkgfqnetvtFNGNLTVVIGNNTAGKTTLLKALQVGLGayLQSLKTLPGGTSYRRNFSSLDKF 73
Cdd:cd03227    8 PSYFVPNDVTF---------GEGSLTIITGPNGSGKSTILDAIGLALG--GAQSATRRRSGVKAGCIVAAVSA 69
ABC_SMC_head cd03239
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ...
3-59 6.73e-04

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: 40.37  E-value: 6.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496418241   3 IKEVNIVNFKGFQNETVTFNGN-LTVVIGNNTAGKTTLLKALQVGLGAylQSLKTLPG 59
Cdd:cd03239    1 IKQITLKNFKSYRDETVVGGSNsFNAIVGPNGSGKSNIVDAICFVLGG--KAAKLRRG 56
retron_eff_Eco8 NF038234
retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner ...
266-347 3.16e-03

retron Eco8 family effector endonuclease; This ATPase, found as the effector protein partner next to a reverse transcriptase in Eco8 type retron systems, is a predicted OLD family endonuclease.


Pssm-ID: 468422 [Multi-domain]  Cd Length: 679  Bit Score: 40.01  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241 266 YMSDGLQS------MINIVAEIAHRCIelngflgqhaikMTPgIVMIDEIDLYLHPH---------WQKHVLQDLTNAFP 330
Cdd:NF038234 245 TQSDGTNSfnfiklFLNLLITLSRREY------------ITP-FIFIDEPELGLHPKlneqlineiYESYSFKKKDNKTP 311
                         90
                 ....*....|....*..
gi 496418241 331 MIQFIVSTHSPFIVQSL 347
Cdd:NF038234 312 YPKIILATHSPRIIKNI 328
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
5-101 3.19e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 38.67  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241   5 EVNIVNFkGFQNETVTFNGNLTV-------VIGNNTAGKTTLLKALqVGLgaylqsLKTLPGgtsyrrnfssldKFMRFD 77
Cdd:cd03235    1 EVEDLTV-SYGGHPVLEDVSFEVkpgeflaIVGPNGAGKSTLLKAI-LGL------LKPTSG------------SIRVFG 60
                         90       100       110
                 ....*....|....*....|....*....|
gi 496418241  78 QELRD------YVPNtekpRITIHADFPIT 101
Cdd:cd03235   61 KPLEKerkrigYVPQ----RRSIDRDFPIS 86
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
1-79 4.28e-03

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. 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: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 39.26  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496418241    1 MRIKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQvglgaylqslkTLPGGTSYRrnfSSLDK-FMRFDQE 79
Cdd:TIGR00611   1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAIY-----------YLALGRSHR---TSRDKpLIRFGAE 66
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
3-49 4.55e-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: 38.35  E-value: 4.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496418241   3 IKEVNIVNFKGFQNETVTFNGNLTVVIGNNTAGKTTLLKALQVGLGA 49
Cdd:cd03276    1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGG 47
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-62 5.63e-03

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: 39.27  E-value: 5.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496418241     2 RIKEVNIVNFKGFQNET-VTFNGNLTVVIGNNTAGKTTLLKALQVGLGAylQSLKTLPGGTS 62
Cdd:TIGR02168    1 RLKKLELAGFKSFADPTtINFDKGITGIVGPNGCGKSNIVDAIRWVLGE--QSAKALRGGKM 60
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
3-44 9.53e-03

ATP-binding cassette domain of eukaryotic SMC3 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: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 37.62  E-value: 9.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 496418241   3 IKEVNIVNFKGFQNETVT--FNGNLTVVIGNNTAGKTTLLKALQ 44
Cdd:cd03272    1 IKQVIIQGFKSYKDQTVIepFSPKHNVVVGRNGSGKSNFFAAIR 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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