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Conserved domains on  [gi|2084395991|ref|WP_221435896|]
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DNA repair protein RecN [Aeromonas caviae]

Protein Classification

DNA repair protein RecN( domain architecture ID 11485034)

DNA repair protein RecN may be involved in recombinational repair of damaged DNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-554 0e+00

recombination and repair protein; Provisional


:

Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 953.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWL 80
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  81 ATNELENDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLLDDVR 160
Cdd:PRK10869   81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 161 RHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYDNEET 240
Cdd:PRK10869  161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 241 TIAGLLQTAVDRAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHVKPA 320
Cdd:PRK10869  241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 321 ELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAIEVRPD 400
Cdd:PRK10869  321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 401 AQsSLSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLRQ 480
Cdd:PRK10869  401 PE-HLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084395991 481 LGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANARELLAS 554
Cdd:PRK10869  480 LGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
 
Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-554 0e+00

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 953.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWL 80
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  81 ATNELENDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLLDDVR 160
Cdd:PRK10869   81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 161 RHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYDNEET 240
Cdd:PRK10869  161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 241 TIAGLLQTAVDRAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHVKPA 320
Cdd:PRK10869  241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 321 ELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAIEVRPD 400
Cdd:PRK10869  321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 401 AQsSLSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLRQ 480
Cdd:PRK10869  401 PE-HLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084395991 481 LGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANARELLAS 554
Cdd:PRK10869  480 LGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-554 0e+00

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 746.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWL 80
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  81 ATNELE-NDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLLDDV 159
Cdd:COG0497    81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 160 RRHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYDnEE 239
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSG-GE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 240 TTIAGLLQTAVDRAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHVKP 319
Cdd:COG0497   240 GGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 320 AELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAIEVRP 399
Cdd:COG0497   320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 400 DAQssLSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLR 479
Cdd:COG0497   400 LEE--PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLA 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084395991 480 QLGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANARELLAS 554
Cdd:COG0497   478 RLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLAL 552
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-552 7.12e-171

DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273187 [Multi-domain]  Cd Length: 563  Bit Score: 495.41  E-value: 7.12e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLE-GNPAARAW 79
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTEsLDDADYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  80 LATNELE---NDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLL 156
Cdd:TIGR00634  81 LQAIELEeedEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 157 DDVRRHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYD 236
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 237 NEETTIAGLLQTAVD-RAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKH 315
Cdd:TIGR00634 241 DVDVQEGSLLEGLGEaQLALASVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 316 HVKPAELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAI 395
Cdd:TIGR00634 321 GASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 396 EVRPDAQSS----LSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTA 471
Cdd:TIGR00634 401 EIKTSLPSGakarAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 472 AVVGRLLRQLGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANAREL 551
Cdd:TIGR00634 481 QAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL 560

                  .
gi 2084395991 552 L 552
Cdd:TIGR00634 561 L 561
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
2-148 1.56e-59

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins 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 that contain 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: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 198.58  E-value: 1.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   2 LTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWLA 81
Cdd:cd03241     1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084395991  82 TNELENDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDG 148
Cdd:cd03241    81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
AAA_23 pfam13476
AAA domain;
5-199 1.29e-14

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 72.53  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   5 LTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFllegnpaarawlatnE 84
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRI---------------G 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  85 LENDGECIVRRVLSAEGRSRSY-------INGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDgyaghhlLLD 157
Cdd:pfam13476  66 LEGKGKAYVEITFENNDGRYTYaiersreLSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLV-------FLG 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2084395991 158 DVRRHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDE 199
Cdd:pfam13476 139 QEREEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEK 180
 
Name Accession Description Interval E-value
PRK10869 PRK10869
recombination and repair protein; Provisional
1-554 0e+00

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 953.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWL 80
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  81 ATNELENDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLLDDVR 160
Cdd:PRK10869   81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 161 RHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYDNEET 240
Cdd:PRK10869  161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGEFEQIDEEYKRLANSGQLLTTSQNALQLLADGEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 241 TIAGLLQTAVDRAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHVKPA 320
Cdd:PRK10869  241 NILSQLYSAKQLLSELIGMDSKLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHVSPE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 321 ELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAIEVRPD 400
Cdd:PRK10869  321 ELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDVKFD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 401 AQsSLSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLRQ 480
Cdd:PRK10869  401 PE-HLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLLRQ 479
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084395991 481 LGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANARELLAS 554
Cdd:PRK10869  480 LGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELLAA 553
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-554 0e+00

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 746.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWL 80
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  81 ATNELE-NDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLLDDV 159
Cdd:COG0497    81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 160 RRHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYDnEE 239
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSG-GE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 240 TTIAGLLQTAVDRAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHVKP 319
Cdd:COG0497   240 GGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 320 AELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAIEVRP 399
Cdd:COG0497   320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 400 DAQssLSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLR 479
Cdd:COG0497   400 LEE--PGPNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLA 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084395991 480 QLGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANARELLAS 554
Cdd:COG0497   478 RLARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELLAL 552
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-552 7.12e-171

DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273187 [Multi-domain]  Cd Length: 563  Bit Score: 495.41  E-value: 7.12e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLE-GNPAARAW 79
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTEsLDDADYPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  80 LATNELE---NDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDGYAGHHLLL 156
Cdd:TIGR00634  81 LQAIELEeedEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 157 DDVRRHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQRLANGTELMQECGYCLDLLYD 236
Cdd:TIGR00634 161 KAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDEALEAEQQRLSNLEKLRELSQNALAALRG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 237 NEETTIAGLLQTAVD-RAETLVGMDSRLGNVLGMLNEALIGVQESHSELRSYLDRLELDPERFNELESRLSKAINLARKH 315
Cdd:TIGR00634 241 DVDVQEGSLLEGLGEaQLALASVIDGSLRELAEQVGNALTEVEEATRELQNYLDELEFDPERLNEIEERLAQIKRLKRKY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 316 HVKPAELAHYHQELAADLARLNSDEERLEGMEDELASARQAFVQAAEALSLSRQRYAEELGAKVSASMHELAMPDGRFAI 395
Cdd:TIGR00634 321 GASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVEQELKALAMEKAEFTV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 396 EVRPDAQSS----LSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTA 471
Cdd:TIGR00634 401 EIKTSLPSGakarAGAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTTLIFDEVDVGVSGETA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 472 AVVGRLLRQLGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGGDQITDNTLANAREL 551
Cdd:TIGR00634 481 QAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLAGLEKSDLTLAHAQEL 560

                  .
gi 2084395991 552 L 552
Cdd:TIGR00634 561 L 561
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
2-148 1.56e-59

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins 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 that contain 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: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 198.58  E-value: 1.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   2 LTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFLLEGNPAARAWLA 81
Cdd:cd03241     1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084395991  82 TNELENDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDG 148
Cdd:cd03241    81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
396-537 3.40e-57

ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins 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 that contain 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: 213208 [Multi-domain]  Cd Length: 276  Bit Score: 192.42  E-value: 3.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 396 EVRPDAQSSLSPLGIDRVEFMVTTNPGQPIQPLGKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVG 475
Cdd:cd03241   135 LLNPERQLDLLDGGLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVG 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084395991 476 RLLRQLGESTQVMVVTHLPQVAGKGHQHMVVSKHTDGKTTETQMQALTPGARLNELARLLGG 537
Cdd:cd03241   215 KKLKELSRSHQVLCITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
AAA_23 pfam13476
AAA domain;
5-199 1.29e-14

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 72.53  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   5 LTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASMVRPGSDKTEVSARFllegnpaarawlatnE 84
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRI---------------G 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  85 LENDGECIVRRVLSAEGRSRSY-------INGVPVPLAQLRNLGQLLVNVHGQHAHQMLLKPDYQLALLDgyaghhlLLD 157
Cdd:pfam13476  66 LEGKGKAYVEITFENNDGRYTYaiersreLSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLV-------FLG 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2084395991 158 DVRRHYQQWRQLQNELNRLKAEQQQREARRQLIEYQVQELDE 199
Cdd:pfam13476 139 QEREEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLKEK 180
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1-380 5.36e-10

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: 62.30  E-value: 5.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991    1 MLTQLTVNNF-AIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEASM------------VRPGSDKTEVSAR 67
Cdd:pfam02463    1 YLKRIEIEGFkSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLrserlsdlihskSGAFVNSAEVEIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   68 FLLEGNpaarawlatNELENDGECIVRRVLSAEGRSRSYINGVPVPLAQLRNL----GQLLVNVH---GQHAHQMLL--K 138
Cdd:pfam02463   81 FDNEDH---------ELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELlesqGISPEAYNflvQGGKIEIIAmmK 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  139 PDYQLALLDGYAGhhLLLDDVRRHYQQW--------RQLQNELNRLKaEQQQREARR--QLIEYQVQELDEFALQPGEFE 208
Cdd:pfam02463  152 PERRLEIEEEAAG--SRLKRKKKEALKKlieetenlAELIIDLEELK-LQELKLKEQakKALEYYQLKEKLELEEEYLLY 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  209 EIEEEHQRlangtELMQEcgycLDLLYDNEETTIAGLLQTAVDRAETLVgmdsRLGNVLGMLNEaligVQESHSELRSYL 288
Cdd:pfam02463  229 LDYLKLNE-----ERIDL----LQELLRDEQEEIESSKQEIEKEEEKLA----QVLKENKEEEK----EKKLQEEELKLL 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  289 DRLELDPERFNELESRLSKAINLARKHHVKPAELAHYHQ--------ELAADLARLNSDEERLEGMEDELASARQAFVQA 360
Cdd:pfam02463  292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELkkekeeieELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
                          410       420
                   ....*....|....*....|
gi 2084395991  361 AEALSLSRQRYAEELGAKVS 380
Cdd:pfam02463  372 EEELLAKKKLESERLSSAAK 391
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
432-497 1.00e-09

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: 57.37  E-value: 1.00e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084395991 432 ASGGELSRISLAIVVISARKISTPTLIFDEVDVGISG-PTAAVVGRLLRQLGESTQVMVVTHLPQVA 497
Cdd:cd03227    78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPrDGQALAEAILEHLVKGAQVIVITHLPELA 144
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-73 5.91e-08

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 53.09  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   1 MLTQLTVNNF-AIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERAEAS------MVRPGSDKTEVSARFLLEGN 73
Cdd:COG0419     1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRsklrsdLINVGSEEASVELEFEHGGK 80
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
169-515 1.05e-06

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: 51.90  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  169 LQNELNRLKAEQQQREARRQLIEYQVQELDefalqpgefeeieeehQRLANGTELMQECGYCLDLLYDNEETtiagLLQT 248
Cdd:pfam02463  852 AEEELERLEEEITKEELLQELLLKEEELEE----------------QKLKDELESKEEKEKEEKKELEEESQ----KLNL 911
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  249 AVDRAETLVGMDSRLGNVLGMLNEALIgvqESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHVKPAElahyhqE 328
Cdd:pfam02463  912 LEEKENEIEERIKEEAEILLKYEEEPE---ELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE------E 982
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  329 LAADLARLNSDEERLEGMEDELASARQAFVQaaealsLSRQRYAEELGAKVSASMHELAM-----PDGRFAIEVRpdaqS 403
Cdd:pfam02463  983 FEEKEERYNKDELEKERLEEEKKKLIRAIIE------ETCQRLKEFLELFVSINKGWNKVffyleLGGSAELRLE----D 1052
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  404 SLSPLGiDRVEFMVTTnPGQPIQPLGkVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLRQLGE 483
Cdd:pfam02463 1053 PDDPFS-GGIEISARP-PGKGVKNLD-LLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSK 1129
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2084395991  484 STQVMVVTHLPQVAGKGHQHMVVSKHTDGKTT 515
Cdd:pfam02463 1130 NAQFIVISLREEMLEKADKLVGVTMVENGVST 1161
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
433-497 1.42e-06

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like 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 that contain 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: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 48.40  E-value: 1.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084395991 433 SGGELSRISLAIVVISARKIstptLIFDEVDVGISGPTAAVVGRLLRQLGES-TQVMVVTHLPQVA 497
Cdd:cd00267    82 SGGQRQRVALARALLLNPDL----LLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELA 143
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
2-68 3.85e-06

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: 47.84  E-value: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   2 LTQLTVNNF-AIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGE------RAE--------ASMVRPGSDKTEVSA 66
Cdd:cd03278     1 LKKLELKGFkSFADKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEqsakslRGEkmsdvifaGSETRKPANFAEVTL 80

                  ..
gi 2084395991  67 RF 68
Cdd:cd03278    81 TF 82
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-49 1.39e-05

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: 47.30  E-value: 1.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2084395991   2 LTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGER 49
Cdd:COG3593     3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPS 50
PRK01156 PRK01156
chromosome segregation protein; Provisional
17-380 1.55e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.97  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  17 ELDLQPGMTCITGETGAGKSIAIDALGLCL-----GERAEaSMVRPGSDKTEVSARFLLEG--------------NPAAR 77
Cdd:PRK01156   18 EIEFDTGINIITGKNGAGKSSIVDAIRFALftdkrTEKIE-DMIKKGKNNLEVELEFRIGGhvyqirrsierrgkGSRRE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  78 AwlatnELENDGECIVR-----------------------RVLSAEGRSRSYINGVPvplAQLRNLGQLLVNVHGQHAHQ 134
Cdd:PRK01156   97 A-----YIKKDGSIIAEgfddttkyieknilgiskdvflnSIFVGQGEMDSLISGDP---AQRKKILDEILEINSLERNY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 135 MLLKpDYQLALLDGYAGHHLLLDDVRRHyqqwrqlQNELNRLKAEQQQREARRQLIEYQVQELDEfalqpgefeEIEEEH 214
Cdd:PRK01156  169 DKLK-DVIDMLRAEISNIDYLEEKLKSS-------NLELENIKKQIADDEKSHSITLKEIERLSI---------EYNNAM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 215 QRLANGTELMQECGYCLDLL--YDNEETTIAGLLQTAVDRAETLVGMDSRLGNVlgmLNEAligVQESHSELRSYLdRLE 292
Cdd:PRK01156  232 DDYNNLKSALNELSSLEDMKnrYESEIKTAESDLSMELEKNNYYKELEERHMKI---INDP---VYKNRNYINDYF-KYK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 293 LDPERFNELESRLSKAINLARKHHVKPAELAHYHQELAADLARLNS-DEERLEGMEDElaSARQAFVQAAEALSLSRQRY 371
Cdd:PRK01156  305 NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDlNNQILELEGYE--MDYNSYLKSIESLKKKIEEY 382
                         410
                  ....*....|..
gi 2084395991 372 A---EELGAKVS 380
Cdd:PRK01156  383 SkniERMSAFIS 394
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
156-492 2.88e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  156 LDDVRRHY--QQWRQLQNELNRLKAEQQQREARRQLIEYQVQELD------EFALQPGEFEEIEEEHQRLANGTELmqec 227
Cdd:TIGR02169  781 LNDLEARLshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlekeylEKEIQELQEQRIDLKEQIKSIEKEI---- 856
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  228 gycldllyDNEETTIAGLLQTAVDRAETLVGMDSRLGNVLG-------MLNEALIGVQESHSELRSYLDRLELDPERFNE 300
Cdd:TIGR02169  857 --------ENLNGKKEELEEELEELEAALRDLESRLGDLKKerdeleaQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  301 LESRLSKAINLARKHHVKPAELAHYH------------------------QELAADLARLNSDEERLEGMEDELAS---- 352
Cdd:TIGR02169  929 LEEELSEIEDPKGEDEEIPEEELSLEdvqaelqrveeeiralepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAiler 1008
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  353 -------ARQAFVQAAEALSLSRQryaeELGAKVSASMHELAM--PDGRFAievrpdaqSSLSplgidrvefMVTTNPGQ 423
Cdd:TIGR02169 1009 ieeyekkKREVFMEAFEAINENFN----EIFAELSGGTGELILenPDDPFA--------GGLE---------LSAKPKGK 1067
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084395991  424 PIQPLgKVASGGELSRISLAIVVISARKISTPTLIFDEVDVGISGPTAAVVGRLLRQLGESTQVMVVTH 492
Cdd:TIGR02169 1068 PVQRL-EAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEAQFIVVSL 1135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
17-375 1.77e-04

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: 44.66  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   17 ELDLQPGMTCITGETGAGKSIAIDALGLCLGE------RAE--------ASMVRPGSDKTEVSARFLLEGNPaarawLAT 82
Cdd:TIGR02168   18 TINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqsakalRGGkmedvifnGSETRKPLSLAEVELVFDNSDGL-----LPG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   83 NELEndgECIVRRVLSAEGRSRSYINGVPVPLAQLRNL------GQLLVNVHGQHAHQMLL--KPDYQLALLDGYAG--- 151
Cdd:TIGR02168   93 ADYS---EISITRRLYRDGESEYFINGQPCRLKDIQDLfldtglGKRSYSIIEQGKISEIIeaKPEERRAIFEEAAGisk 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  152 HH-------LLLDDVRRHYQQWRQLQNELNR-LKAEQQQREARRQLIEYQVQ------------------ELDEFALQPG 205
Cdd:TIGR02168  170 YKerrketeRKLERTRENLDRLEDILNELERqLKSLERQAEKAERYKELKAElrelelallvlrleelreELEELQEELK 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  206 EFEEIEEEHQRLANGTELMQEcgyclDL-LYDNEETTIAGLLQTAVDRAETLVgmdSRLGNVLGMLNEALIGVQESHSEL 284
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLE-----ELrLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEEL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  285 RSYLDRLELDPERFNELESRLSKAINLARKHHV-KPAELAHYHQELAADLARLNSDEERLEGMEDELASARqafvQAAEA 363
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELEsLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE----LQIAS 397
                          410
                   ....*....|..
gi 2084395991  364 LSLSRQRYAEEL 375
Cdd:TIGR02168  398 LNNEIERLEARL 409
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
421-492 2.90e-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: 42.07  E-value: 2.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084395991 421 PGQPIQPLgKVASGGE--LSRISLAIVVISARKIstPTLIFDEVDVGISGPTAAVVGRLLRQLGESTQVMVVTH 492
Cdd:cd03278   104 PGKKVQRL-SLLSGGEkaLTALALLFAIFRVRPS--PFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITH 174
ABC_SMC1_euk cd03275
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ...
22-116 3.01e-04

ATP-binding cassette domain of eukaryotic SMC1 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: 213242 [Multi-domain]  Cd Length: 247  Bit Score: 42.56  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  22 PGM--TCITGETGAGKSIAIDALGLCLGERaeASMVRpGSDKTEVSARFLLEGNPAARAWLATNELENDGECIVRRVLSA 99
Cdd:cd03275    20 PFDrfTCIIGPNGSGKSNLMDAISFVLGEK--SSHLR-SKNLKDLIYRARVGKPDSNSAYVTAVYEDDDGEEKTFRRIIT 96
                          90
                  ....*....|....*..
gi 2084395991 100 EGRSRSYINGVPVPLAQ 116
Cdd:cd03275    97 GGSSSYRINGKVVSLKE 113
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
5-50 8.57e-04

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: 40.66  E-value: 8.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2084395991   5 LTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDALGLCLGERA 50
Cdd:cd03276     4 ITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKA 49
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
4-72 1.27e-03

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 40.33  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   4 QLTVNNF------AIVKFLELDlQPGMTCITGETGAGKSIAIDALGLCL-GE-------RAEASMVRPGSDKTEVSARFL 69
Cdd:cd03279     5 KLELKNFgpfreeQVIDFTGLD-NNGLFLICGPTGAGKSTILDAITYALyGKtprygrqENLRSVFAPGEDTAEVSFTFQ 83

                  ...
gi 2084395991  70 LEG 72
Cdd:cd03279    84 LGG 86
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
4-70 1.33e-03

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: 39.65  E-value: 1.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084395991   4 QLTVNNFAIVkFLELDLQPG---MTCITGETGAGKSIAIDALGLCLGERAEA----SMVRPGSDKTEVSARFLL 70
Cdd:cd03227     1 KIVLGRFPSY-FVPNDVTFGegsLTIITGPNGSGKSTILDAIGLALGGAQSAtrrrSGVKAGCIVAAVSAELIF 73
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-44 1.59e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 41.07  E-value: 1.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2084395991   1 MLTQLTVNNF-AIVKfLELDLQPgMTCITGETGAGKSIAIDALGL 44
Cdd:COG4637     1 MITRIRIKNFkSLRD-LELPLGP-LTVLIGANGSGKSNLLDALRF 43
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
167-363 4.79e-03

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: 39.49  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 167 RQLQNELNRLKAEQQQREARRQLIEYQVQELDEFALQPGEFEEIEEEHQR--LANGTELMQECGYCLDLLYDNE------ 238
Cdd:pfam07888  55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKelSASSEELSEEKDALLAQRAAHEarirel 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 239 ETTIAGLLQTAVDRAETLVGMDSRLGNVLGMLNEA-----------LIGVQESHS------ELRSYLDRLELDPERFNEL 301
Cdd:pfam07888 135 EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEeaerkqlqaklQQTEEELRSlskefqELRNSLAQRDTQVLQLQDT 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084395991 302 ESRLSKAINLArkhHVKPAELAHYHQELAADLARLNSDEERLEGMEDELASA-----------RQAFVQAAEA 363
Cdd:pfam07888 215 ITTLTQKLTTA---HRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaaqrdrtqaelHQARLQAAQL 284
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
278-371 5.59e-03

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: 39.67  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991  278 QESHSELRSYLDRLELDPERFNELESRLSKAINLARKHHvkpAELAHYHQELAADLARLNSDEERLEGMEDELASARQAF 357
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS---EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
                           90
                   ....*....|....
gi 2084395991  358 VQAAEALSLSRQRY 371
Cdd:TIGR02169  458 EQLAADLSKYEQEL 471
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
17-117 5.63e-03

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: 39.67  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991   17 ELDLQPGMTCITGETGAGKSIAIDALGLCLGE------RAE-------ASMVRPGSDKTEVSARFLLEGNPAARAWlatn 83
Cdd:TIGR02169   18 VIPFSKGFTVISGPNGSGKSNIGDAILFALGLssskamRAErlsdlisNGKNGQSGNEAYVTVTFKNDDGKFPDEL---- 93
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2084395991   84 elendgECIVRRVLSAEGRSRSY-INGVPVPLAQL 117
Cdd:TIGR02169   94 ------EVVRRLKVTDDGKYSYYyLNGQRVRLSEI 122
COG4637 COG4637
Predicted ATPase [General function prediction only];
432-542 6.22e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 39.14  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084395991 432 ASGGELSRISLAIVVISARkiSTPTLIFDEVDVGISGPTAAVVGRLLRQLGESTQVMVVTHLPQV--AGKGHQHMVVSKH 509
Cdd:COG4637   259 LSDGTLRFLALLAALLSPR--PPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALldALEPEEVLVLERE 336
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2084395991 510 TDGKTTetqmqalTPGARLNELARLLGGDQITD 542
Cdd:COG4637   337 DDGETR-------IRRLSDLELPEWLEGYSLGE 362
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
2-42 8.36e-03

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: 38.73  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2084395991   2 LTQLTVNNFAIVKFLELDLQPGMTCITGETGAGKSIAIDAL 42
Cdd:pfam13175   3 IKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL 43
 
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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