NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1016901142|gb|AMX93578|]
View 

DNA repair protein RecN [Mesorhizobium ciceri]

Protein Classification

DNA repair protein RecN( domain architecture ID 11423061)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-550 0e+00

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


:

Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 664.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPARALL 80
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIE-DDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGAVRST 159
Cdd:COG0497    81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 160 GEAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEETDLAELRASMMRAEKIASEIHDAQDVLSG-PS 238
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGgEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 239 SPLPQLASLLRRLQRkVTEAPGLLDDVVKSLDEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLRAASRKHSVAV 318
Cdd:COG0497   241 GALDLLGQALRALER-LAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 319 DDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVMAELPALKLERAAFIVEMKS 398
Cdd:COG0497   320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 399 DAESRmEEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLAR 478
Cdd:COG0497   400 LEEPG-PNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016901142 479 LSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAGATITDEARAAAERLL 550
Cdd:COG0497   479 LARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELL 550
 
Name Accession Description Interval E-value
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-550 0e+00

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 664.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPARALL 80
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIE-DDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGAVRST 159
Cdd:COG0497    81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 160 GEAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEETDLAELRASMMRAEKIASEIHDAQDVLSG-PS 238
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGgEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 239 SPLPQLASLLRRLQRkVTEAPGLLDDVVKSLDEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLRAASRKHSVAV 318
Cdd:COG0497   241 GALDLLGQALRALER-LAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 319 DDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVMAELPALKLERAAFIVEMKS 398
Cdd:COG0497   320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 399 DAESRmEEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLAR 478
Cdd:COG0497   400 LEEPG-PNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016901142 479 LSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAGATITDEARAAAERLL 550
Cdd:COG0497   479 LARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELL 550
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-551 1.04e-126

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: 382.54  E-value: 1.04e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPArALL 80
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESLDDA-DYP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIE-----DDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGA 155
Cdd:TIGR00634  80 ALQAIEleeedEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 156 VRSTGEAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEE----------TDLAELRASMMRAEKIAS 225
Cdd:TIGR00634 160 VKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDealeaeqqrlSNLEKLRELSQNALAALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 226 EIHDAQD--VLSGPSSPLPQLASL----LRRLQRKVTEAPGLLDDVVKSLDEAMLSLdaaqsgveaalratEYDPQRLEK 299
Cdd:TIGR00634 240 GDVDVQEgsLLEGLGEAQLALASVidgsLRELAEQVGNALTEVEEATRELQNYLDEL--------------EFDPERLNE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 300 AEERLFSLRAASRKHSVAVDDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVM 379
Cdd:TIGR00634 306 IEERLAQIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVE 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 380 AELPALKLERAAFIVEMKSDAESRM-----EEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPT 454
Cdd:TIGR00634 386 QELKALAMEKAEFTVEIKTSLPSGAkaragAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTT 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 455 LVFDEIDTGVGGAVADAIGQRLARLSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLA 534
Cdd:TIGR00634 466 LIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLA 545
                         570
                  ....*....|....*..
gi 1016901142 535 GATITDEARAAAERLLR 551
Cdd:TIGR00634 546 GLEKSDLTLAHAQELLE 562
PRK10869 PRK10869
recombination and repair protein; Provisional
1-550 3.07e-117

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 358.09  E-value: 3.07e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPARALL 80
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIEDDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGAVRSTG 160
Cdd:PRK10869   81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 161 EAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEetdLAELRASMMRAEKIASEIHDAQDVLSGPSSP 240
Cdd:PRK10869  161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGE---FEQIDEEYKRLANSGQLLTTSQNALQLLADG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 241 LPQ-LASLLRRLQRKVTEAPGL---LDDVVKSLDEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLRAASRKHSV 316
Cdd:PRK10869  238 EEVnILSQLYSAKQLLSELIGMdskLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 317 AVDDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVMAELPALKLERAAFIVEM 396
Cdd:PRK10869  318 SPEELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 397 KSDAESRMEEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRL 476
Cdd:PRK10869  398 KFDPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLL 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016901142 477 ARLSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAGATITDEARAAAERLL 550
Cdd:PRK10869  478 RQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELL 551
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
407-535 1.29e-61

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: 204.36  E-value: 1.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 407 GIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLARLSKRVQVL 486
Cdd:cd03241   148 GLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVL 227
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1016901142 487 SVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAG 535
Cdd:cd03241   228 CITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
AAA_23 pfam13476
AAA domain;
5-47 1.52e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 57.51  E-value: 1.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1016901142   5 LSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALG 47
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALY 43
 
Name Accession Description Interval E-value
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
1-550 0e+00

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 664.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPARALL 80
Cdd:COG0497     1 MLTELSIRNFALIDELELEFGPGLTVLTGETGAGKSILLDALGLLLGGRADASLVRHGADKAEVEAVFDLSDDPPLAAWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIE-DDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGAVRST 159
Cdd:COG0497    81 EENGLDlDDGELILRREISADGRSRAFINGRPVTLSQLRELGELLVDIHGQHEHQSLLDPDAQRELLDAFAGLEELLEEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 160 GEAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEETDLAELRASMMRAEKIASEIHDAQDVLSG-PS 238
Cdd:COG0497   161 REAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKLREALQEALEALSGgEG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 239 SPLPQLASLLRRLQRkVTEAPGLLDDVVKSLDEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLRAASRKHSVAV 318
Cdd:COG0497   241 GALDLLGQALRALER-LAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTV 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 319 DDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVMAELPALKLERAAFIVEMKS 398
Cdd:COG0497   320 EELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKAVTAELADLGMPNARFEVEVTP 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 399 DAESRmEEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLAR 478
Cdd:COG0497   400 LEEPG-PNGADQVEFLFSANPGEPPKPLAKVASGGELSRIMLALKVVLADKDAVPTLIFDEVDTGVGGRVAEAVGEKLAR 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016901142 479 LSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAGATITDEARAAAERLL 550
Cdd:COG0497   479 LARNHQVLCVTHLPQVAAMADHHFRVSKEVDGGRTVTRVRPLDEEERVEEIARMLGGAEITEAALAHARELL 550
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
1-551 1.04e-126

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: 382.54  E-value: 1.04e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPArALL 80
Cdd:TIGR00634   1 MLTELRINNFALIRVLTVEFERGLTVLTGETGAGKSMIIDALSLLGGQRAGASRVRSGENRAVVEGRFTTESLDDA-DYP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIE-----DDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGA 155
Cdd:TIGR00634  80 ALQAIEleeedEDGEVILRRSISRDGRSRAYLNGKPVSASSLLEFTSELLDLHGQHDQQLLFRPDEQRQLLDTFAGANEK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 156 VRSTGEAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEE----------TDLAELRASMMRAEKIAS 225
Cdd:TIGR00634 160 VKAYRELYQAWLKARQQLKDRQQKEQELAQRLDFLQFQLEELEEADLQPGEDealeaeqqrlSNLEKLRELSQNALAALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 226 EIHDAQD--VLSGPSSPLPQLASL----LRRLQRKVTEAPGLLDDVVKSLDEAMLSLdaaqsgveaalratEYDPQRLEK 299
Cdd:TIGR00634 240 GDVDVQEgsLLEGLGEAQLALASVidgsLRELAEQVGNALTEVEEATRELQNYLDEL--------------EFDPERLNE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 300 AEERLFSLRAASRKHSVAVDDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVM 379
Cdd:TIGR00634 306 IEERLAQIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEEVDKLEEELDKAAVALSLIRRKAAERLAKRVE 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 380 AELPALKLERAAFIVEMKSDAESRM-----EEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPT 454
Cdd:TIGR00634 386 QELKALAMEKAEFTVEIKTSLPSGAkaragAYGADQVEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSSAAVTT 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 455 LVFDEIDTGVGGAVADAIGQRLARLSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLA 534
Cdd:TIGR00634 466 LIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKEGLDGRTATRVRPLSGEERVAELARMLA 545
                         570
                  ....*....|....*..
gi 1016901142 535 GATITDEARAAAERLLR 551
Cdd:TIGR00634 546 GLEKSDLTLAHAQELLE 562
PRK10869 PRK10869
recombination and repair protein; Provisional
1-550 3.07e-117

recombination and repair protein; Provisional


Pssm-ID: 236781 [Multi-domain]  Cd Length: 553  Bit Score: 358.09  E-value: 3.07e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPARALL 80
Cdd:PRK10869    1 MLAQLTISNFAIVRELEIDFQSGMTVITGETGAGKSIAIDALGLCLGGRAEASMVRPGATRADLCARFSLKDTPAALRWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  81 ADNAIEDDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDAFGGHLGAVRSTG 160
Cdd:PRK10869   81 EDNQLEDGNECLLRRVISSDGRSRGFINGTPVPLSQLRELGQLLIQIHGQHAHQLLLKPEHQKTLLDAYANETSLLQEMR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 161 EAWRHWRACEQELSRHRAKVAAAAREADYLRAAVAELTKLDPQPGEetdLAELRASMMRAEKIASEIHDAQDVLSGPSSP 240
Cdd:PRK10869  161 AAYQLWHQSCRDLAQHQQQSQERAARKQLLQYQLKELNEFAPQPGE---FEQIDEEYKRLANSGQLLTTSQNALQLLADG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 241 LPQ-LASLLRRLQRKVTEAPGL---LDDVVKSLDEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLRAASRKHSV 316
Cdd:PRK10869  238 EEVnILSQLYSAKQLLSELIGMdskLSGVLDMLEEALIQIQEASDELRHYLDRLDLDPNRLAELEQRLSKQISLARKHHV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 317 AVDDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVMAELPALKLERAAFIVEM 396
Cdd:PRK10869  318 SPEELPQHHQQLLEEQQQLDDQEDDLETLALAVEKHHQQALETAQKLHQSRQRYAKELAQLITESMHELSMPHGKFTIDV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 397 KSDAESRMEEGIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRL 476
Cdd:PRK10869  398 KFDPEHLSADGADRIEFRVTTNPGQPLQPIAKVASGGELSRIALAIQVITARKMETPALIFDEVDVGISGPTAAVVGKLL 477
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016901142 477 ARLSKRVQVLSVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAGATITDEARAAAERLL 550
Cdd:PRK10869  478 RQLGESTQVMCVTHLPQVAGCGHQHFFVSKETDGGMTETHMQPLDKKARLQELARLLGGSEVTRNTLANAKELL 551
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
407-535 1.29e-61

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: 204.36  E-value: 1.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 407 GIDQIEFWVRTNPGTRPGPMMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLARLSKRVQVL 486
Cdd:cd03241   148 GLDDVEFLFSTNPGEPLKPLAKIASGGELSRLMLALKAILARKDAVPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVL 227
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1016901142 487 SVTHAPQVAARAATHFLISKSGTTDRVATGIAEMDRPARQEEIARMLAG 535
Cdd:cd03241   228 CITHLPQVAAMADNHFLVEKEVEGGRTVTKVRELDKEERVEEIARMLSG 276
ABC_RecN cd03241
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ...
2-148 4.25e-61

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: 202.82  E-value: 4.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   2 LSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIAVFDVPRNHPARALLA 81
Cdd:cd03241     1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSLLLGGRASADLIRSGAEKAVVEGVFDISDEEEAKALLL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016901142  82 DNAIEDDGDIILRRLQTADGRTRVFVNDQPSSVTLMRDVGRALVEIHGQHDERALVDPGAHREVLDA 148
Cdd:cd03241    81 ELGIEDDDDLIIRREISRKGRSRYFINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDG 147
AAA_23 pfam13476
AAA domain;
5-47 1.52e-09

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 57.51  E-value: 1.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1016901142   5 LSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALG 47
Cdd:pfam13476   1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALY 43
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
430-500 3.10e-08

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: 53.13  E-value: 3.10e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016901142 430 ASGGELSRFLLALKVALADRGSAPTLVFDEIDTGV----GGAVADAIGQRLARLSkrvQVLSVTHAPQVAARAAT 500
Cdd:cd03227    78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLdprdGQALAEAILEHLVKGA---QVIVITHLPELAELADK 149
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
1-113 1.56e-07

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 51.93  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   1 MLSRLSIRDI-VLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDAS------LVRHGAAQGQVIAVFDVprn 73
Cdd:COG0419     1 KLLRLRLENFrSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRsklrsdLINVGSEEASVELEFEH--- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1016901142  74 hparalladnaieDDGDIILRRLQtadGRTRVFVNDQPSS 113
Cdd:COG0419    78 -------------GGKRYRIERRQ---GEFAEFLEAKPSE 101
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
2-57 5.50e-07

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: 51.93  E-value: 5.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016901142   2 LSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASLVRH 57
Cdd:COG3593     3 LEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE 58
recF PRK00064
recombination protein F; Reviewed
2-111 1.61e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 50.54  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   2 LSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALS-LALGaRG-----DASLVRHGAAQGQVIAVFDvprnhp 75
Cdd:PRK00064    3 LTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIYlLAPG-RShrtarDKELIRFGAEAAVIHGRVE------ 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1016901142  76 aralladnaiEDDGDIILRRLQTADGRTRVFVNDQP 111
Cdd:PRK00064   76 ----------KGGRELPLGLEIDKKGGRKVRINGEP 101
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
2-64 4.70e-06

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: 47.60  E-value: 4.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016901142   2 LSRLSIRDIVLI-EKLDIDFQPGLSVLTGETGAGKSILLDALSLAL---------GARGDASLVRHGAAQGQV 64
Cdd:cd03240     1 IDKLSIRNIRSFhERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtgelppnskGGAHDPKLIREGEVRAQV 73
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
2-69 6.37e-06

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: 48.06  E-value: 6.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016901142   2 LSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARG-----DASLVRHGAAQGQVIAVFD 69
Cdd:cd03242     1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAISLLATGKShrtsrDKELIRWGAEEAKISAVLE 73
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
11-66 1.05e-05

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: 45.81  E-value: 1.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016901142  11 VLIEKLDIDFQPG-LSVLTGETGAGKSILLDALSLALGARGDASLVRHGAAQGQVIA 66
Cdd:cd03227     9 SYFVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVA 65
COG4637 COG4637
Predicted ATPase [General function prediction only];
430-540 1.24e-05

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 47.62  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 430 ASGGELsRFLlALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLARLSKRVQVLSVTHAPQVAAraatHFLISKSGT 509
Cdd:COG4637   259 LSDGTL-RFL-ALLAALLSPRPPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLD----ALEPEEVLV 332
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1016901142 510 TDRVATGIAEMdRPARQEEIARMLAGATITD 540
Cdd:COG4637   333 LEREDDGETRI-RRLSDLELPEWLEGYSLGE 362
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
7-65 4.61e-05

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: 44.51  E-value: 4.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016901142   7 IRDIVLI-----EKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDA--------SLVRHGAAQGQVI 65
Cdd:cd03276     1 IESITLKnfmchRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDtnrgsslkDLIKDGESSAKIT 72
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
14-121 3.96e-04

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: 43.42  E-value: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142   14 EKLDIDFQPGLSVLTGETGAGKSILLDALSLALGARGDASL-----------VRHGAAQ-GQVIAVFDVPRNhparalla 81
Cdd:pfam02463   15 KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLrserlsdlihsKSGAFVNsAEVEITFDNEDH-------- 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1016901142   82 dNAIEDDGDIILRRLQTADGRTRVFVNDQPSSVT----LMRDVG 121
Cdd:pfam02463   87 -ELPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKevaeLLESQG 129
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
4-46 7.33e-04

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: 41.10  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1016901142   4 RLSIRDI-VLIEKLDIDFQP----GLSVLTGETGAGKSILLDALSLAL 46
Cdd:cd03279     5 KLELKNFgPFREEQVIDFTGldnnGLFLICGPTGAGKSTILDAITYAL 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-412 8.03e-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: 42.35  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  243 QLASLLRRLQRKVTEAPGLLDDvvksLDEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLRA--------ASRKH 314
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskelteLEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142  315 SVAVDDLAQLRDTMSADLADLDAGEERLHGLEKQAAAARETYDIAAAQLSSLR-HAAAVGLTKAVMAELPALKLERAAFI 393
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRIAATERRLEDL 843
                          170
                   ....*....|....*....
gi 1016901142  394 VEMKSDAESRMEEGIDQIE 412
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIE 862
COG4637 COG4637
Predicted ATPase [General function prediction only];
1-57 1.09e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 41.45  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPgLSVLTGETGAGKSILLDALSL-----------ALGARGDASLVRH 57
Cdd:COG4637     1 MITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDALRFlsdaargglqdALARRGGLEELLW 67
PRK01156 PRK01156
chromosome segregation protein; Provisional
1-46 1.45e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 1.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1016901142   1 MLSRLSIRDIVLIEKLDIDFQPGLSVLTGETGAGKSILLDALSLAL 46
Cdd:PRK01156    2 IIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFAL 47
DUF2813 pfam11398
Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which ...
13-52 2.01e-03

Protein of unknown function (DUF2813); This entry contains YjbD from Escherichia coli, which is annotated as a nucleotide triphosphate hydrolase.


Pssm-ID: 431868 [Multi-domain]  Cd Length: 372  Bit Score: 40.80  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1016901142  13 IEKLDIDFQPgLSVLTGETGAGKSILLDALSLALGARGDA 52
Cdd:pfam11398  14 INRLSLHFDQ-LTVLIGENAWGKSSLLDALSLLLNPTKEL 52
AAA_29 pfam13555
P-loop containing region of AAA domain;
17-46 6.67e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 35.27  E-value: 6.67e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1016901142  17 DIDFQP-GLSVLTGETGAGKSILLDALSLAL 46
Cdd:pfam13555  16 TIPIDPrGNTLLTGPSGSGKSTLLDAIQTLL 46
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
190-556 8.53e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 190 LRAAVAELTKLDpqpgeETDLAELRASMMRAEKIASEIHDAQDVLSGPSSPLPQLASLLRRLQRKVTEAPGLLDDVVKSL 269
Cdd:COG1196   272 LRLELEELELEL-----EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 270 DEAMLSLDAAQSGVEAALRATEYDPQRLEKAEERLFSLR----AASRKHSVAVDDLAQLRDTMSADLADLDAGEERLHGL 345
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 346 EKQAAAARETYDIAAAQLSSLRHAAAVGLTKAVMAELPALKLERAAFIVEmKSDAESRMEEGIDQIEFWVRTNPGTRPGP 425
Cdd:COG1196   427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE-AALAELLEELAEAAARLLLLLEAEADYEG 505
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016901142 426 MMKVASGGELSRFLLALKVALADRGSAPTLVFDEIDTGVGGAVADAIGQRLARLSKRVQVLSVTHAPQV----AARAATH 501
Cdd:COG1196   506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRAR 585
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1016901142 502 FLISKSGTTDRVATGIAEMDRPARQEEIARMLAGATITDEARAAAERLLRENIAA 556
Cdd:COG1196   586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH