NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|133922578|ref|NP_613069|]
View 

coiled-coil domain-containing protein 22 [Mus musculus]

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: 756.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578    1 MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   81 PLELGYQNFLYPSEPDLRDLLLFLAERLPSDASEDADQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTpkVQRLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  161 QQPFHSSRLVLPEL-----NSSGELWEFQASpLLLPAPTQVPQLQGRAASLLEHHASQLCQHVNRDCPGDEDRVrwASRV 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRkgktlKNSKELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGL--ASRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  236 PSQEDSRAPQQRLHKQLIEHLRQSWGP-----LGAPTQVRDLGEMLQTWGARAMTGV--PKGSRFTHSEKFTFHLEPQVQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAgteatSGASRSAQDLAELLSSFSGSSTTDTglTKGSRFTHTEKLQFTNEAPAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  309 AAqvadVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  389 TVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  469 RKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 133922578  549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETEMGK 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: 756.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578    1 MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   81 PLELGYQNFLYPSEPDLRDLLLFLAERLPSDASEDADQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTpkVQRLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  161 QQPFHSSRLVLPEL-----NSSGELWEFQASpLLLPAPTQVPQLQGRAASLLEHHASQLCQHVNRDCPGDEDRVrwASRV 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRkgktlKNSKELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGL--ASRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  236 PSQEDSRAPQQRLHKQLIEHLRQSWGP-----LGAPTQVRDLGEMLQTWGARAMTGV--PKGSRFTHSEKFTFHLEPQVQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAgteatSGASRSAQDLAELLSSFSGSSTTDTglTKGSRFTHTEKLQFTNEAPAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  309 AAqvadVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  389 TVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  469 RKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 133922578  549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETEMGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-625 3.66e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 332 QELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAE-QEQALRLKSrtVELLPDGAANLAKLQLVVESS 410
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKE--LKEKAEEYIKLSEFYEEYLDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 411 AQRLIHLASQWEKhrvpLLAEYRhlRRLQDCRELESsrRLAEIQELHHSVRAAAEEARRKEEVY---KQLVSELETLPKD 487
Cdd:PRK03918 309 LREIEKRLSRLEE----EINGIE--ERIKELEEKEE--RLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERLKKR 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 488 VSRLAyTQRILEIVGNIRKQKEEITKilsDTKELQKEINSLSGKLDRTFAVTDELvfKDAK-----------KDDAVRKA 556
Cdd:PRK03918 381 LTGLT-PEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL--KKAKgkcpvcgreltEEHRKELL 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 557 YKYLAALHENCSQLIQTIEDTGTIMREVRDLE-------------------EQIETEMGKKTLSNLEKICEDYRALRQEN 617
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeseliklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                 ....*...
gi 133922578 618 AGLLGRVR 625
Cdd:PRK03918 535 IKLKGEIK 542
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
327-538 4.66e-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: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   327 RAAQEQELESLREQLASVNHNIEEVEADMKTLGINL--------VQVETECRQSELSVAEQEQALRLKSRTVEllpDGAA 398
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASLERSIAEKERELE---DAEE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   399 NLAKLQLVVESSAQRLIHLA---SQWEKHRVPLLAEYRHLRRlqdcrELESSRrlAEIQELHHSVRAAAEEARRKEEVYK 475
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKE-----ELEDLR--AELEEVDKEFAETRDELKDYREKLE 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133922578   476 QLVSELETLPKDVSRLAYT-QRILEIVGNIRKQ----KEEITKILSDTKELQKEINSLSGKLDRTFAV 538
Cdd:TIGR02169  396 KLKREINELKRELDRLQEElQRLSEELADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
333-598 1.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 333 ELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLpdgAANLAKLQLVVESSAQ 412
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL---LAELARLEQDIARLEE 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 413 RLIHLASQWEKhrvpLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELEtlPKDVSRLA 492
Cdd:COG1196  310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEE 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 493 YTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQ 572
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                        250       260
                 ....*....|....*....|....*.
gi 133922578 573 TIEDTGTIMREVRDLEEQIETEMGKK 598
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEA 489
 
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: 756.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578    1 MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   81 PLELGYQNFLYPSEPDLRDLLLFLAERLPSDASEDADQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTpkVQRLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  161 QQPFHSSRLVLPEL-----NSSGELWEFQASpLLLPAPTQVPQLQGRAASLLEHHASQLCQHVNRDCPGDEDRVrwASRV 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRkgktlKNSKELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGL--ASRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  236 PSQEDSRAPQQRLHKQLIEHLRQSWGP-----LGAPTQVRDLGEMLQTWGARAMTGV--PKGSRFTHSEKFTFHLEPQVQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAgteatSGASRSAQDLAELLSSFSGSSTTDTglTKGSRFTHTEKLQFTNEAPAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  309 AAqvadVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  389 TVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  469 RKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 133922578  549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETEMGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-625 3.66e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 332 QELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAE-QEQALRLKSrtVELLPDGAANLAKLQLVVESS 410
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKE--LKEKAEEYIKLSEFYEEYLDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 411 AQRLIHLASQWEKhrvpLLAEYRhlRRLQDCRELESsrRLAEIQELHHSVRAAAEEARRKEEVY---KQLVSELETLPKD 487
Cdd:PRK03918 309 LREIEKRLSRLEE----EINGIE--ERIKELEEKEE--RLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERLKKR 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 488 VSRLAyTQRILEIVGNIRKQKEEITKilsDTKELQKEINSLSGKLDRTFAVTDELvfKDAK-----------KDDAVRKA 556
Cdd:PRK03918 381 LTGLT-PEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL--KKAKgkcpvcgreltEEHRKELL 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 557 YKYLAALHENCSQLIQTIEDTGTIMREVRDLE-------------------EQIETEMGKKTLSNLEKICEDYRALRQEN 617
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeseliklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                 ....*...
gi 133922578 618 AGLLGRVR 625
Cdd:PRK03918 535 IKLKGEIK 542
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
327-538 4.66e-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: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   327 RAAQEQELESLREQLASVNHNIEEVEADMKTLGINL--------VQVETECRQSELSVAEQEQALRLKSRTVEllpDGAA 398
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASLERSIAEKERELE---DAEE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   399 NLAKLQLVVESSAQRLIHLA---SQWEKHRVPLLAEYRHLRRlqdcrELESSRrlAEIQELHHSVRAAAEEARRKEEVYK 475
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKE-----ELEDLR--AELEEVDKEFAETRDELKDYREKLE 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133922578   476 QLVSELETLPKDVSRLAYT-QRILEIVGNIRKQ----KEEITKILSDTKELQKEINSLSGKLDRTFAV 538
Cdd:TIGR02169  396 KLKREINELKRELDRLQEElQRLSEELADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
333-598 1.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 333 ELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLpdgAANLAKLQLVVESSAQ 412
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL---LAELARLEQDIARLEE 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 413 RLIHLASQWEKhrvpLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELEtlPKDVSRLA 492
Cdd:COG1196  310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEE 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 493 YTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQ 572
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                        250       260
                 ....*....|....*....|....*.
gi 133922578 573 TIEDTGTIMREVRDLEEQIETEMGKK 598
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEA 489
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
311-605 1.70e-06

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: 51.17  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  311 QVADVPATSQRLEQDTRAAQEQ------ELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALR 384
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQREleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  385 LKSRTVEllpdgaaNLAKLQLVVESSAQRLIHLASQWEKhrvpllaEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAA 464
Cdd:TIGR04523 423 LLEKEIE-------RLKETIIKNNSEIKDLTNQDSVKEL-------IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578  465 EEARRKEEVYKQLVSELETLPKDVSRLayTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLsgKLDRTFAVTDELVF 544
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDL--TKKISSLKEKIEKLESEKKEKESKISDLEDELNKD--DFELKKENLEKEID 564
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133922578  545 KDAKKDDAVRKAYKYLAALHENCSQLIQTIEDtgtimrEVRDLEEQIETEMgkKTLSNLEK 605
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEK------EKKDLIKEIEEKE--KKISSLEK 617
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
329-601 4.84e-06

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: 50.06  E-value: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   329 AQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAANLAK----LQ 404
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   405 LVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQ-----DCRELESSRRlaEIQELHHSVRAAAEEARRKEEVYKQLVS 479
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieqLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   480 ELETLPKDVSRLAYT-----QRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVR 554
Cdd:TIGR02168  832 RIAATERRLEDLEEQieelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 133922578   555 KAYKYLAALHENCSQLIQTIEDT--------GTIMREVRDLEEQIETEMGKKTLS 601
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLevridnlqERLSEEYSLTLEEAEALENKIEDD 966
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
303-627 1.20e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 303 LEPQVQAAQvaDVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQA 382
Cdd:PRK03918 357 LEERHELYE--EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 383 LR---LKSRtvELLPDGAANL-AKLQLVVESSAQRLIHLASQWEKHRVPL------LAEYRHLRRLQDC----RELESSR 448
Cdd:PRK03918 435 KGkcpVCGR--ELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELrelekvLKKESELIKLKELaeqlKELEEKL 512
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 449 RLAEIQELhhsvRAAAEEARRKEEVYKQLVSELETLPKDVSRL-AYTQRILEIVGNIRKQKEEITKILSDTKELQ-KEIN 526
Cdd:PRK03918 513 KKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeELKKKLAELEKKLDELEEELAELLKELEELGfESVE 588
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 527 SLSGKLDRTFAVTDE-LVFKDAKKDdaVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETEMGKKTLSNLEk 605
Cdd:PRK03918 589 ELEERLKELEPFYNEyLELKDAEKE--LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR- 665
                        330       340
                 ....*....|....*....|..
gi 133922578 606 icEDYRALRQENAGLLGRVREA 627
Cdd:PRK03918 666 --EEYLELSRELAGLRAELEEL 685
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
328-548 1.21e-05

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: 47.84  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 328 AAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAANLAKLQLVV 407
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 408 ESSAQRLIH-----LASQWEKHRVPLLAE-------YRHLRRLQDCRELESSRR------LAEIQELHHSVRAAAEEARR 469
Cdd:COG4942   96 RAELEAQKEelaelLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARReqaeelRADLAELAALRAELEAERAE 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 133922578 470 KEEVYKQLVSELETLPKDVSRLAYTQRILEivGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAK 548
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
331-627 1.44e-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: 48.51  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   331 EQELESLREQLASVNHNIEEVEADMKTLGinlvqvetecRQSELsvAEQEQALRLKSRTVELlpdgaanlaklqlvvESS 410
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLE----------RQAEK--AERYKELKAELRELEL---------------ALL 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   411 AQRLIHLASQWEKHRVPLLAEYRHLRRLQDcrelESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELETLPKDV-- 488
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqi 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   489 --SRLAYTQRILEIVGNIR--------KQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYK 558
Cdd:TIGR02168  307 lrERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133922578   559 YLAALHENCSQL---IQTIEDTGT-IMREVRDLEEQIETEMGKKTLSNLEKICEDYRALRQENAGLLGRVREA 627
Cdd:TIGR02168  387 KVAQLELQIASLnneIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
334-615 4.17e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 334 LESLREQLASVNHNIEEVEADMKTLGINLVQVETE-CRQSELS----VAEQEQAL--RLKSRTVELLPDGAANLAKLQLV 406
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlKKESELIklkeLAEQLKELeeKLKKYNLEELEKKAEEYEKLKEK 533
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 407 VESSAQRLIHLASQWEKHRvPLLAEYRHLRRLQDCRELESSRRLAEIQEL-HHSVRAAAEEARRKEEVYKQLVSeletLP 485
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPFYNEYLE----LK 608
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 486 KDVSRLAYTQRILEivgnirKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKdaKKDDAVRKAYKYLAALHE 565
Cdd:PRK03918 609 DAEKELEREEKELK------KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRA 680
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 133922578 566 NCSQLIQTIEdtgTIMREVRDLEEQIET-EMGKKTLSNLEKICEDYRALRQ 615
Cdd:PRK03918 681 ELEELEKRRE---EIKKTLEKLKEELEErEKAKKELEKLEKALERVEELRE 728
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
445-615 7.15e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 445 ESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELETLPKDVSRLAYTQRILEI-VGNIRKQKEEITKILSDTKELQK 523
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkIRELEERIEELKKEIEELEEKVK 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 524 EINSLSGKLDRTFAVTDELVfkdaKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIEtEMgKKTLSNL 603
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYE----EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-EL-EKRLEEL 357
                        170
                 ....*....|..
gi 133922578 604 EKICEDYRALRQ 615
Cdd:PRK03918 358 EERHELYEEAKA 369
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
320-484 8.29e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 320 QRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAAN 399
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 400 LAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVS 479
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                 ....*
gi 133922578 480 ELETL 484
Cdd:COG1196  464 LLAEL 468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
333-626 1.05e-04

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: 45.44  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   333 ELESLREQLASVNHNIEEVEADMKTLginlvqvetecrQSELSVAEQEQALRLKSRTVELLpdgaanlaklqlvvessaq 412
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERL------------RREREKAERYQALLKEKREYEGY------------------- 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   413 rliHLASQWEKHR---VPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRK-EEVYKQLVSELETLPKDV 488
Cdd:TIGR02169  227 ---ELLKEKEALErqkEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEI 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   489 SRL-----AYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDrtfAVTDELVFKDAKKDDAVRKAY---KYL 560
Cdd:TIGR02169  304 ASLersiaEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEevdKEF 380
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133922578   561 AALHENCSQLIQTIEDTGtimREVRDLEEQIEtemgkKTLSNLEKICEDYRALRQENAGLLGRVRE 626
Cdd:TIGR02169  381 AETRDELKDYREKLEKLK---REINELKRELD-----RLQEELQRLSEELADLNAAIAGIEAKINE 438
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
317-533 3.42e-04

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: 43.90  E-value: 3.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   317 ATSQRLEQDTRAAQ--EQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSEL--SVAEQEQALRLKSRTVEL 392
Cdd:TIGR02169  734 KLKERLEELEEDLSslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEAR 813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   393 LPDGAANLAKLQLVVESSAQRLIHLasqwekhrvpllaeyrhLRRLQDCRELESSRRlAEIQELHHSVRAAAEEARRKEE 472
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQEL-----------------QEQRIDLKEQIKSIE-KEIENLNGKKEELEEELEELEA 875
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133922578   473 VYKQLVSELETLPKDVSRLAYTQRILEIvgNIRKQKEEITKILSDTKELQKEINSLSGKLD 533
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELER--KIEELEAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-534 1.17e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 306 QVQAAQVADVPATSQRLEQdTRAAQEQELESLREQLASVNHNIEEVEADM-------KTLGINLVQVETECRQSELSVAE 378
Cdd:COG1196  256 EELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIarleerrRELEERLEELEEELAELEEELEE 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 379 QEQALRLKSRTVELLpdgAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDcRELESSRRLAEIQELHH 458
Cdd:COG1196  335 LEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEE 410
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 133922578 459 SVRAAAEEARRKEEVYKQLVSELETLPKDVSR--LAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDR 534
Cdd:COG1196  411 ALLERLERLEEELEELEEALAELEEEEEEEEEalEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
331-627 3.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 331 EQELESLREQLASVNHNIEEVEADMKTLGinlvqvetecRQSElsVAEQEQALR--LKSRTVELLpdgAANLAKLQLVVE 408
Cdd:COG1196  178 ERKLEATEENLERLEDILGELERQLEPLE----------RQAE--KAERYRELKeeLKELEAELL---LLKLRELEAELE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 409 SSAQRLIHLASQWEKHRVPLL---AEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELETLp 485
Cdd:COG1196  243 ELEAELEELEAELEELEAELAeleAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL- 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 486 kDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHE 565
Cdd:COG1196  322 -EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 133922578 566 NCSQLIQTIEDtgtIMREVRDLEEQIETEmgKKTLSNLEKICEDYRALRQENAGLLGRVREA 627
Cdd:COG1196  401 QLEELEEAEEA---LLERLERLEEELEEL--EEALAELEEEEEEEEEALEEAAEEEAELEEE 457
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
324-625 4.13e-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: 40.43  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   324 QDTRAAQEQELESLREQLASVNHNIEEVEadmktLGINLVQVETECRQSELSVAEQEQAlRLKSRtvellpdgaanlakl 403
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELR-----LEVSELEEEIEELQKELYALANEIS-RLEQQ--------------- 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   404 qlvVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDcRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELEt 483
Cdd:TIGR02168  304 ---KQILRERLANLERQLEELEAQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE- 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578   484 lpkdvsrlaytQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDdavrkaykyLAAL 563
Cdd:TIGR02168  379 -----------EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKEL 438
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 133922578   564 HENCSQLIQTIEDTGTIMREVRDLEEQIETEmgkktlsnLEKICEDYRALRQENAGLLGRVR 625
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEELREE--------LEEAEQALDAAERELAQLQARLD 492
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
325-604 6.41e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 325 DTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINL------------------------VQVETECRQSELSVAEQE 380
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVeeaealleagkcpecgqpvegsphVETIEEDRERVEELEAEL 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 381 QALRLKSRTVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRL-QDCRELEssrrlAEIQELHHS 459
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrERAAELE-----AEAEEKREA 559
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 460 VRAAAEEARRKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKE-----------INSL 528
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDErrerlaekrerKREL 639
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922578 529 SGKLD----------RTFA------VTDELVFKDAKKDD------AVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRD 586
Cdd:PRK02224 640 EAEFDearieearedKERAeeyleqVEEKLDELREERDDlqaeigAVENELEELEELRERREALENRVEALEALYDEAEE 719
                        330       340
                 ....*....|....*....|.
gi 133922578 587 LEE---QIETEMGKKTLSNLE 604
Cdd:PRK02224 720 LESmygDLRAELRQRNVETLE 740
 
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