NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|7661844|ref|NP_054727|]
View 

coiled-coil domain-containing protein 22 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein 22( domain architecture ID 12064803)

coiled-coil domain-containing protein 22 (CCDC22) is a DUF812 domain-containing protein that is involved in regulation of NF-kappa-B signaling

Gene Symbol:  CCDC22
PubMed:  33942254

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-597 0e+00

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


:

Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 760.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844      1 MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     81 PLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAILLRAIGSQIRDQLALPWVPPHLRTpkLQHLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    161 QKPFHASRLVVPELSSRG-----EPREFQASpLLLPVPTQVPQPVGRVASLLEHHALQLCQQTGRDRPGDEDWVHrtSRL 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRKGKTlknskELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLA--SRL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    236 PPQEDTRAQRQRLQKQLTEHLRQSW-----GLLGAPIQARDLGELLQAWGAGAKTG--APKGSRFTHSEKFTFHLEPQAQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAAlagteATSGASRSAQDLAELLSSFSGSSTTDtgLTKGSRFTHTEKLQFTNEAPAA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    309 ATqvsdVPATSRRPEQVTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    389 AVELLPDGTANLAKLQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    469 RKEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 7661844    549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETELGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
 
Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-597 0e+00

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 760.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844      1 MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     81 PLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAILLRAIGSQIRDQLALPWVPPHLRTpkLQHLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    161 QKPFHASRLVVPELSSRG-----EPREFQASpLLLPVPTQVPQPVGRVASLLEHHALQLCQQTGRDRPGDEDWVHrtSRL 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRKGKTlknskELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLA--SRL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    236 PPQEDTRAQRQRLQKQLTEHLRQSW-----GLLGAPIQARDLGELLQAWGAGAKTG--APKGSRFTHSEKFTFHLEPQAQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAAlagteATSGASRSAQDLAELLSSFSGSSTTDtgLTKGSRFTHTEKLQFTNEAPAA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    309 ATqvsdVPATSRRPEQVTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    389 AVELLPDGTANLAKLQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    469 RKEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 7661844    549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETELGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-626 3.08e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     329 AQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESecrhsklstaEREQALRLKSRAVELLPDGTANLAKLQLVVE 408
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE----------ELEQLRKELEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     409 NSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDcrelESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDV 488
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEE----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     489 SRLayTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCS 568
Cdd:TIGR02168  820 ANL--RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 7661844     569 QLIQTIEDTGtimREVRDLEEQIEtELGKKtlsnLEKIREDYRALRQENAGLLGRVRE 626
Cdd:TIGR02168  898 ELSEELRELE---SKRSELRRELE-ELREK----LAQLELRLEGLEVRIDNLQERLSE 947
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-625 3.63e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   332 QELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAE-REQALRLKS---------RAVELLPDGTANLA 401
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKElkekaeeyiKLSEFYEEYLDELR 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   402 KLQLVVENSAQRVIHLAGQWEKhrvpLLAEYRHLRKLQDcRELESSRRLAEIQELHQsvraAAEEARRKEEVYKQLMSEL 481
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKK-KLKELEKRLEELEERHE----LYEEAKAKKEELERLKKRL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   482 ETLPRDvsrlaytqRILEIVGNIRKQKEEITKilsDTKELQKEINSLSGKLDRTFAVTDELvfKDAK-----------KD 550
Cdd:PRK03918 382 TGLTPE--------KLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL--KKAKgkcpvcgreltEE 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   551 DAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLE-------------------EQIETELGKKTLSNLEKIREDYR 611
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeseliklkelaeqlKELEEKLKKYNLEELEKKAEEYE 528

                        330
                 ....*....|....
gi 7661844   612 ALRQENAGLLGRVR 625
Cdd:PRK03918 529 KLKEKLIKLKGEIK 542
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-627 9.05e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 9.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  333 ELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSRAVELLpdgTANLAKLQLVVENSAQ 412
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL---LAELARLEQDIARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  413 RVIHLAGQWEKhrvpLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDVSRLA 492
Cdd:COG1196 310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  493 ytQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQ 572
Cdd:COG1196 386 --EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7661844  573 TIEDTGTIMREVRDLEEQIETELGKKtlsnlEKIREDYRALRQENAGLLGRVREA 627
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKAA 513
 
Name Accession Description Interval E-value
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 1-597 0e+00

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 760.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844      1 MEEADRILIHSLRQAGTAVPPDVQTLRAFTTELVVEAVVRCLRVINPAVGSGLSPLLPLAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     81 PLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAILLRAIGSQIRDQLALPWVPPHLRTpkLQHLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    161 QKPFHASRLVVPELSSRG-----EPREFQASpLLLPVPTQVPQPVGRVASLLEHHALQLCQQTGRDRPGDEDWVHrtSRL 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRKGKTlknskELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLA--SRL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    236 PPQEDTRAQRQRLQKQLTEHLRQSW-----GLLGAPIQARDLGELLQAWGAGAKTG--APKGSRFTHSEKFTFHLEPQAQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAAlagteATSGASRSAQDLAELLSSFSGSSTTDtgLTKGSRFTHTEKLQFTNEAPAA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    309 ATqvsdVPATSRRPEQVTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    389 AVELLPDGTANLAKLQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    469 RKEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 7661844    549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETELGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 329-626 3.08e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     329 AQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESecrhsklstaEREQALRLKSRAVELLPDGTANLAKLQLVVE 408
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE----------ELEQLRKELEELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     409 NSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDcrelESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDV 488
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEE----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     489 SRLayTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCS 568
Cdd:TIGR02168  820 ANL--RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 7661844     569 QLIQTIEDTGtimREVRDLEEQIEtELGKKtlsnLEKIREDYRALRQENAGLLGRVRE 626
Cdd:TIGR02168  898 ELSEELRELE---SKRSELRRELE-ELREK----LAQLELRLEGLEVRIDNLQERLSE 947
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 328-610 2.84e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.00  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     328 AAQEQELESLREQLEGVNRSIEEVEADMKTLGVSfVQAESECRHSKLS------TAEREQALRLKSRAVELLPDGTANLA 401
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKK-IKDLGEEEQLRVKekigelEAEIASLERSIAEKERELEDAEERLA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     402 KLQLVVENSAQRVIHLAGQ---WEKHRVPLLAEYRHLRKlqdcrELESSRrlAEIQELHQSVRAAAEEARRKEEVYKQLM 478
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREieeERKRRDKLTEEYAELKE-----ELEDLR--AELEEVDKEFAETRDELKDYREKLEKLK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     479 SELETLPRDVSRLAYT-QRILEIVGNIRKQ----KEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAV 553
Cdd:TIGR02169  399 REINELKRELDRLQEElQRLSEELADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7661844     554 RKAYKYLAALHENCSQL---IQTIEDTGTIMREVRD-LEEQIETELGkkTLSNLEKIREDY 610
Cdd:TIGR02169  479 DRVEKELSKLQRELAEAeaqARASEERVRGGRAVEEvLKASIQGVHG--TVAQLGSVGERY 537
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-625 3.63e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   332 QELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAE-REQALRLKS---------RAVELLPDGTANLA 401
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKElkekaeeyiKLSEFYEEYLDELR 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   402 KLQLVVENSAQRVIHLAGQWEKhrvpLLAEYRHLRKLQDcRELESSRRLAEIQELHQsvraAAEEARRKEEVYKQLMSEL 481
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKK-KLKELEKRLEELEERHE----LYEEAKAKKEELERLKKRL 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   482 ETLPRDvsrlaytqRILEIVGNIRKQKEEITKilsDTKELQKEINSLSGKLDRTFAVTDELvfKDAK-----------KD 550
Cdd:PRK03918 382 TGLTPE--------KLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL--KKAKgkcpvcgreltEE 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   551 DAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLE-------------------EQIETELGKKTLSNLEKIREDYR 611
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeseliklkelaeqlKELEEKLKKYNLEELEKKAEEYE 528

                        330
                 ....*....|....
gi 7661844   612 ALRQENAGLLGRVR 625
Cdd:PRK03918 529 KLKEKLIKLKGEIK 542
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-626 4.35e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     333 ELESLREQLEGVNRSIEEVEADMKTLgvsfvQAESEcrhsklsTAEREQALRLKSRAVEllpdGTANLAKLQLVvensaq 412
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERL-----RRERE-------KAERYQALLKEKREYE----GYELLKEKEAL------ 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     413 rvihlagqwEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRK-EEVYKQLMSELETLPRDVSRL 491
Cdd:TIGR02169  236 ---------ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASL 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     492 -----AYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDrtfAVTDELVFKDAKKDDAVRKAY---KYLAAL 563
Cdd:TIGR02169  307 ersiaEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEevdKEFAET 383

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7661844     564 HENCSQLIQTIEDTGtimrevRDLEEqIETELGKKtLSNLEKIREDYRALRQENAGLLGRVRE 626
Cdd:TIGR02169  384 RDELKDYREKLEKLK------REINE-LKRELDRL-QEELQRLSEELADLNAAIAGIEAKINE 438
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 334-615 5.38e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.73  E-value: 5.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     334 LESLREQLEGVNRSIEEVEADMKTLgvsfvqaESECR----------HSKLSTAEREQALRLKSRAV-ELLPDGTANLAK 402
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAM-------KSECQgqmerqmaaiQGKNESLEKVSSLTAQLESTkEMLRKVVEELTA 486

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     403 LQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQDCRELessrRLAEIQELhqsvraaaeeaRRKEEVYKQLMSELE 482
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL----KLQELQHL-----------KNEGDHLRNVQTECE 551

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     483 TLPRdvsRLAYTQRILEIvgnIRKQKEEITK-----------ILSDTKELQKEINslsgklDRTFAVTDELVFKDaKKDD 551
Cdd:pfam15921  552 ALKL---QMAEKDKVIEI---LRQQIENMTQlvgqhgrtagaMQVEKAQLEKEIN------DRRLELQEFKILKD-KKDA 618

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7661844     552 AVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETELgKKTLSNLEKIREDYRALRQ 615
Cdd:pfam15921  619 KIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEV-KTSRNELNSLSEDYEVLKR 681
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 333-627 9.05e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 9.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  333 ELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSRAVELLpdgTANLAKLQLVVENSAQ 412
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL---LAELARLEQDIARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  413 RVIHLAGQWEKhrvpLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDVSRLA 492
Cdd:COG1196 310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  493 ytQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQ 572
Cdd:COG1196 386 --EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7661844  573 TIEDTGTIMREVRDLEEQIETELGKKtlsnlEKIREDYRALRQENAGLLGRVREA 627
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKAA 513
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-627 1.03e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   333 ELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESEcrhsklsTAEREQAL-RLKSRAV-------ELLPDGTANL-AKL 403
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKE-------IKELKKAIeELKKAKGkcpvcgrELTEEHRKELlEEY 457

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   404 QLVVENSAQRVIHLAGQWEKhrvpLLAEYRHLRK-LQDCRELESSRRLAE-IQELHQS--------VRAAAEEARRKEEV 473
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERK----LRKELRELEKvLKKESELIKLKELAEqLKELEEKlkkynleeLEKKAEEYEKLKEK 533

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   474 YKQLMSELETLPRDVSRL-AYTQRILEIVGNIRKQKEEITKILSDTKELQ-KEINSLSGKLDRTFAVTDE-LVFKDAKKD 550
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLeELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEyLELKDAEKE 613

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7661844   551 daVRKAYKYLAALHENCSQLIQTIEDTGTimrEVRDLEEQIEtELGKK-TLSNLEKIREDYRALRQENAGLLGRVREA 627
Cdd:PRK03918 614 --LEREEKELKKLEEELDKAFEELAETEK---RLEELRKELE-ELEKKySEEEYEELREEYLELSRELAGLRAELEEL 685
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 331-627 1.04e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     331 EQELESLREQLEGVNRSIEEVEADMKTLGVsfvQAESECRHSKLSTAERE-----QALRLKSRAVELLPDgTANLAKLQL 405
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLER---QAEKAERYKELKAELRElelalLVLRLEELREELEEL-QEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     406 VVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKLQdcRELESSRrlAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLP 485
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQ--KELYALA--NEISRLEQQKQILRERLANLERQLEELEAQLEELE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     486 RDvsrlaytqrileivgnIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHE 565
Cdd:TIGR02168  330 SK----------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7661844     566 NCSQL---IQTIEDTGT-IMREVRDLEEQIETELGKKTLSNLEKIREDYRALRQENAGLLGRVREA 627
Cdd:TIGR02168  394 QIASLnneIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
445-615 2.56e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   445 ESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDVSRLAYTQRILEI-VGNIRKQKEEITKILSDTKELQK 523
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkIRELEERIEELKKEIEELEEKVK 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   524 EINSLSGKLDRTFAVTDELVfkdaKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIEtELgKKTLSNL 603
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYE----EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-EL-EKRLEEL 357

                        170
                 ....*....|..
gi 7661844   604 EKIREDYRALRQ 615
Cdd:PRK03918 358 EERHELYEEAKA 369
PTZ00121 PTZ00121
MAEBL; Provisional
 340-609 1.05e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    340 QLEGVNRSIEEVEADMK-------TLGVSFVQAEsECRHSKLSTAERE-QALRLKSRAVELlpdgtanlAKLQLVVENSA 411
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKednradeATEEAFGKAE-EAKKTETGKAEEArKAEEAKKKAEDA--------RKAEEARKAED 1138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    412 QRVIHLAGQWEKHRVPLLAeyrhlRKLQDCRELESSRRLAEIQELHQSVRA----------AAEEARRKEEVYKqlmSEL 481
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIA-----RKAEDARKAEEARKAEDAKKAEAARKAeevrkaeelrKAEDARKAEAARK---AEE 1210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    482 ETLPRDVSRLAYTQRILEI--VGNIRKQKEEITKilSDTKELQKEINSLSGKLDRTFAVTDELV-FKDAKKDDAVRKAYK 558
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVkkAEEAKKDAEEAKK--AEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKKAEE 1288

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7661844    559 YLAALHENCSQLIQTIEDTGTIMREVRDLEE-QIETELGKKTLSNLEKIRED 609
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEaKKKAEEAKKKADAAKKKAEE 1340
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 328-563 2.29e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  328 AAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHsklstaEREQALRLKSRAVELlpdgTANLAKLQLVV 407
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR------LEERRRELEERLEEL----EEELAELEEEL 332

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  408 ENSAQRVIHLAGQwEKHRVPLLAEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRD 487
Cdd:COG1196 333 EELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7661844  488 VS--RLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAAL 563
Cdd:COG1196 412 LLerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 331-621 4.72e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    331 EQELESLREQLEGVNRSIEEVEADMKTLgvsfvqaESECRHSKLSTAEREQALRLKSRAVELLPDGTANLAKLQLVVENS 410
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDL-------ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    411 AQRVIHLAGQWEKhrvpllaEYRHLRKLQDCRELESSRRLAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDVSR 490
Cdd:TIGR04523 442 IKDLTNQDSVKEL-------IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844    491 LayTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLsgKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQL 570
Cdd:TIGR04523 515 L--TKKISSLKEKIEKLESEKKEKESKISDLEDELNKD--DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL 590

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7661844    571 IQTIEDtgtimrEVRDLEEQIEtELGKKTLS---NLEKIREDYRALRQENAGLL 621
Cdd:TIGR04523 591 IDQKEK------EKKDLIKEIE-EKEKKISSlekELEKAKKENEKLSSIIKNIK 637
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 325-548 1.12e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  325 VTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAEREQALRLKSRAVELLPDGTANLAKLQ 404
Cdd:COG4942  13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  405 LVVENSAQ----------RVIHLAGQWEKHRVPLLAE--YRHLRKLQDCRELESSRR------LAEIQELHQSVRAAAEE 466
Cdd:COG4942  93 AELRAELEaqkeelaellRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARReqaeelRADLAELAALRAELEAE 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844  467 ARRKEEVYKQLMSELETLPRDVSRLAYTQRILEivGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKD 546
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250


                ..
gi 7661844  547 AK 548
Cdd:COG4942 251 LK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 320-625 1.13e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     320 RRPEQVTWAAQEQELESLREQLEGVNRSIEEVEadmktLGVSFVQAESECRHSKLSTAEREQAlRLKSRAVELlpdgtan 399
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELR-----LEVSELEEEIEELQKELYALANEIS-RLEQQKQIL------- 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     400 LAKLQLVVENSAQRVIHLAgQWEKHRVPLLAEyrhLRKLQDcrelessrRLAEIQELHQSVRAAAEEARRKEEVYKQLMS 479
Cdd:TIGR02168  308 RERLANLERQLEELEAQLE-ELESKLDELAEE---LAELEE--------KLEELKEELESLEAELEELEAELEELESRLE 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     480 ELEtlprdvsrlaytQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDdavrkayky 559
Cdd:TIGR02168  376 ELE------------EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--------- 434

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7661844     560 LAALHENCSQLIQTIEDTGTIMREVRDLEEQIETElgkktlsnLEKIREDYRALRQENAGLLGRVR 625
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELERLEEALEELREE--------LEEAEQALDAAERELAQLQARLD 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
333-618 1.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   333 ELESLREQLEGVNrsIEEVEADMKtlgvsfvqaESECRHSKLSTAEREQaLRLKSRAVELLPdgtanlaklqlvVENSAQ 412
Cdd:PRK03918 504 QLKELEEKLKKYN--LEELEKKAE---------EYEKLKEKLIKLKGEI-KSLKKELEKLEE------------LKKKLA 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   413 RVIHLAGQWEKHRVPLLAEYRHLrKLQDCRELESsrRLAEIQELHQ---SVRAAAEEARRKEEVYKQLMSELEtlprdvs 489
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEEL-GFESVEELEE--RLKELEPFYNeylELKDAEKELEREEKELKKLEEELD------- 629

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   490 rlaytqrileivgnirKQKEEITKILSDTKELQKEINSLSGKLDRTfavtdelvfKDAKKDDAVRKAYKYLAALHENCSQ 569
Cdd:PRK03918 630 ----------------KAFEELAETEKRLEELRKELEELEKKYSEE---------EYEELREEYLELSRELAGLRAELEE 684

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   570 LIQTIEdtgTIMREVRDLEEQIET--------ELGKKTLSNLEKIRE---DYRALRQENA 618
Cdd:PRK03918 685 LEKRRE---EIKKTLEKLKEELEErekakkelEKLEKALERVEELREkvkKYKALLKERA 741
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 331-533 1.30e-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: 41.98  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     331 EQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESECRHSKLSTAERE-QALR-LKSRAVELLPDGTANLAKLQLVVE 408
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElSKLEeEVSRIEARLREIEQKLNRLTLEKE 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     409 NSAQRVIHLagqwekhrvpllaeyrhLRKLQDCRELESSRRlAEIQELHQSVRAAAEEARRKEEVYKQLMSELETLPRDV 488
Cdd:TIGR02169  830 YLEKEIQEL-----------------QEQRIDLKEQIKSIE-KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 7661844     489 SRLAYTQRILEIvgNIRKQKEEITKILSDTKELQKEINSLSGKLD 533
Cdd:TIGR02169  892 DELEAQLRELER--KIEELEAQIEKKRKRLSELKAKLEALEEELS 934
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
331-613 5.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   331 EQELESLREQLEGVNRSIEEVEADMKTL------------------------GVSFVQAESECRHSKLSTAEREQALRLK 386
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTArerveeaealleagkcpecgqpveGSPHVETIEEDRERVEELEAELEDLEEE 490

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   387 SRAVELLPDGTANLAKLQLVVENSAQRVIHLAGQWEKHRVPLLAEYRHLRKL-QDCRELEssrrlAEIQELHQSVRAAAE 465
Cdd:PRK02224 491 VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrERAAELE-----AEAEEKREAAAEAEE 565

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   466 EARRKEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKE-INSLSGKLDRTFAVTDELvf 544
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDErRERLAEKRERKRELEAEF-- 643

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7661844   545 kdakKDDAVRKAykylAALHENCSQLIQTIEDTgtiMREVRDLEEQIETELG--KKTLSNLEKIREDYRAL 613
Cdd:PRK02224 644 ----DEARIEEA----REDKERAEEYLEQVEEK---LDELREERDDLQAEIGavENELEELEELRERREAL 703
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 320-576 7.88e-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: 39.28  E-value: 7.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     320 RRPEQVTWAAQEQELESLREQLEGVNRSIEEVEADMKTLGVSFVQAESE----------CRHSKLSTAEREQALRLKSRA 389
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqelqeqridLKEQIKSIEKEIENLNGKKEE 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     390 VEllpdgtANLAKLQLVVENSAQRVIHLAGQWEKHRvpllAEYRHLRKLQDcrELESSRrlaEIQELHQSVRAAaeearR 469
Cdd:TIGR02169  866 LE------EELEELEAALRDLESRLGDLKKERDELE----AQLRELERKIE--ELEAQI---EKKRKRLSELKA-----K 925

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844     470 KEEVYKQLMSELETLPRDVSRLAYTQRILEIVGNIRKQKEEITKI-------LSDTKELQKEINSLSGKLDRTFAVTDEL 542
Cdd:TIGR02169  926 LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaIQEYEEVLKRLDELKEKRAKLEEERKAI 1005

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 7661844     543 VFK----DAKKDDAVRKAYKylaALHENCSQLIQTIED 576
Cdd:TIGR02169 1006 LERieeyEKKKREVFMEAFE---AINENFNEIFAELSG 1040
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 452-626 9.89e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 9.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   452 EIQELHQSVRAAAEEARRkeevYKQLMSELE---TLPRDVSRLAYTQRILEIVGNIRKQKEEITKILSDtKELQKEINSL 528
Cdd:PRK05771 101 EIKELEEEISELENEIKE----LEQEIERLEpwgNFDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESD-VENVEYISTD 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661844   529 SGKldRTFAVTDElvFKDAKKDDAVRKAYKYLAalhencsqliQTIEDTGTIMREVRDLEEQIEtELGKKtlsnLEKIRE 608
Cdd:PRK05771 176 KGY--VYVVVVVL--KELSDEVEEELKKLGFER----------LELEEEGTPSELIREIKEELE-EIEKE----RESLLE 236

                        170
                 ....*....|....*...
gi 7661844   609 DYRALRQENAGLLGRVRE 626
Cdd:PRK05771 237 ELKELAKKYLEELLALYE 254
 
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