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Conserved domains on  [gi|26333345|dbj|BAC30390|]
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unnamed protein product [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

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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: 751.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345     1 MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    81 PLELGYQNFLYPSEPDLRDLLLFLAERLPSDASEDANQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTpkVQRLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   161 QQPFHSSRLVLPEL-----NSSGELWEFQASpLLLPAPTQVPQLQGRAASLLEHHASQLCQHVNRDCPGDEDRVrwASRV 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRkgktlKNSKELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGL--ASRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   236 PSQEDSRAPQQRLHKQLIEHLRQSWGP-----LGAPTQVRDLGEMLQTWGARAMTGV--PKGSRFTHSEKFTFHLEPQVQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAgteatSGASRSAQDLAELLSSFSGSSTTDTglTKGSRFTHTEKLQFTNEAPAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   309 AAqvadVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   389 TVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   469 RKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 26333345   549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIET*MGK 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: 751.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345     1 MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    81 PLELGYQNFLYPSEPDLRDLLLFLAERLPSDASEDANQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTpkVQRLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   161 QQPFHSSRLVLPEL-----NSSGELWEFQASpLLLPAPTQVPQLQGRAASLLEHHASQLCQHVNRDCPGDEDRVrwASRV 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRkgktlKNSKELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGL--ASRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   236 PSQEDSRAPQQRLHKQLIEHLRQSWGP-----LGAPTQVRDLGEMLQTWGARAMTGV--PKGSRFTHSEKFTFHLEPQVQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAgteatSGASRSAQDLAELLSSFSGSSTTDTglTKGSRFTHTEKLQFTNEAPAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   309 AAqvadVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   389 TVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   469 RKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 26333345   549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIET*MGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
327-538 7.98e-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: 52.38  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    327 RAAQEQELESLREQLASVNHNIEEVEADMKTLGINL--------VQVETECRQSELSVAEQEQALRLKSRTVEllpDGAA 398
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASLERSIAEKERELE---DAEE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    399 NLAKLQLVVESSAQRLIHLA---SQWEKHRVPLLAEYRHLRRlqdcrELESSRrlAEIQELHHSVRAAAEEARRKEEVYK 475
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKE-----ELEDLR--AELEEVDKEFAETRDELKDYREKLE 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26333345    476 QLVSELETLPKDVSRLAYT-QRILEIVGNIRKQ----KEEITKILSDTKELQKEINSLFGKLDRTFAV 538
Cdd:TIGR02169  396 KLKREINELKRELDRLQEElQRLSEELADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-625 2.01e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  332 QELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAE-QEQALRLKSrtVELLPDGAANLAKLQLVVESS 410
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKE--LKEKAEEYIKLSEFYEEYLDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  411 AQRLIHLASQWEKhrvpLLAEYRhlRRLQDCRELESsrRLAEIQELHHSVRAAAEEARRKEEVY---KQLVSELETLPKD 487
Cdd:PRK03918 309 LREIEKRLSRLEE----EINGIE--ERIKELEEKEE--RLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERLKKR 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  488 VSRLAyTQRILEIVGNIRKQKEEITKilsDTKELQKEINSLFGKLDRTFAVTDELvfKDAK-----------KDDAVRKA 556
Cdd:PRK03918 381 LTGLT-PEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL--KKAKgkcpvcgreltEEHRKELL 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  557 YKYLAALHENCSQLIQTIEDTGTIMREVRDLE-------------------EQIET*MGKKTLSNLEKICEDYRALRQEN 617
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeseliklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                 ....*...
gi 26333345  618 AGLLGRVR 625
Cdd:PRK03918 535 IKLKGEIK 542
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
333-592 3.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 333 ELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLpdgAANLAKLQLVVESSAQ 412
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL---LAELARLEQDIARLEE 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 413 RLIHLASQWEKhrvpLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELEtlPKDVSRLA 492
Cdd:COG1196 310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEE 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 493 YTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQ 572
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                       250       260
                ....*....|....*....|
gi 26333345 573 TIEDTGTIMREVRDLEEQIE 592
Cdd:COG1196 464 LLAELLEEAALLEAALAELL 483
 
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: 751.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345     1 MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGY 80
Cdd:pfam05667   1 MEEVDGIIIHSLRQIGCEIAEDVQSLKDFTTELLVEAVVRCLRVINPDLGINLPLTLPPGMSARFRVGTSLAQACQELGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    81 PLELGYQNFLYPSEPDLRDLLLFLAERLPSDASEDANQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTpkVQRLQGSAL 160
Cdd:pfam05667  81 RGEIGYQTFLYPNEPDIRKILMFLVEKLPRESSEAADQPVGKSAVLQRAIAAAIRSQLAAPWLPPECKP--HQRRQGSRA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   161 QQPFHSSRLVLPEL-----NSSGELWEFQASpLLLPAPTQVPQLQGRAASLLEHHASQLCQHVNRDCPGDEDRVrwASRV 235
Cdd:pfam05667 159 LRPFHTQTLVLPGRkgktlKNSKELKEFYSE-YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGL--ASRL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   236 PSQEDSRAPQQRLHKQLIEHLRQSWGP-----LGAPTQVRDLGEMLQTWGARAMTGV--PKGSRFTHSEKFTFHLEPQVQ 308
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAgteatSGASRSAQDLAELLSSFSGSSTTDTglTKGSRFTHTEKLQFTNEAPAA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   309 AAqvadVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSR 388
Cdd:pfam05667 316 TS----SPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKK 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   389 TVELLPDGAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEAR 468
Cdd:pfam05667 392 TLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   469 RKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAK 548
Cdd:pfam05667 472 QKEELYKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKLDRTFTVTDELVFKDAK 551
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 26333345   549 KDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIET*MGK 597
Cdd:pfam05667 552 KDESVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
327-538 7.98e-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: 52.38  E-value: 7.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    327 RAAQEQELESLREQLASVNHNIEEVEADMKTLGINL--------VQVETECRQSELSVAEQEQALRLKSRTVEllpDGAA 398
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeeqLRVKEKIGELEAEIASLERSIAEKERELE---DAEE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    399 NLAKLQLVVESSAQRLIHLA---SQWEKHRVPLLAEYRHLRRlqdcrELESSRrlAEIQELHHSVRAAAEEARRKEEVYK 475
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEreiEEERKRRDKLTEEYAELKE-----ELEDLR--AELEEVDKEFAETRDELKDYREKLE 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26333345    476 QLVSELETLPKDVSRLAYT-QRILEIVGNIRKQ----KEEITKILSDTKELQKEINSLFGKLDRTFAV 538
Cdd:TIGR02169  396 KLKREINELKRELDRLQEElQRLSEELADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
311-605 1.38e-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: 51.56  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   311 QVADVPATSQRLEQDTRAAQEQ------ELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALR 384
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQREleekqnEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   385 LKSRTVEllpdgaaNLAKLQLVVESSAQRLIHLASQWEKhrvpllaEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAA 464
Cdd:TIGR04523 423 LLEKEIE-------RLKETIIKNNSEIKDLTNQDSVKEL-------IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345   465 EEARRKEEVYKQLVSELETLPKDVSRLayTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLfgKLDRTFAVTDELVF 544
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDL--TKKISSLKEKIEKLESEKKEKESKISDLEDELNKD--DFELKKENLEKEID 564
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26333345   545 KDAKKDDAVRKAYKYLAALHENCSQLIQTIEDtgtimrEVRDLEEQIET*MgkKTLSNLEK 605
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEK------EKKDLIKEIEEKE--KKISSLEK 617
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
332-625 2.01e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  332 QELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAE-QEQALRLKSrtVELLPDGAANLAKLQLVVESS 410
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKE--LKEKAEEYIKLSEFYEEYLDE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  411 AQRLIHLASQWEKhrvpLLAEYRhlRRLQDCRELESsrRLAEIQELHHSVRAAAEEARRKEEVY---KQLVSELETLPKD 487
Cdd:PRK03918 309 LREIEKRLSRLEE----EINGIE--ERIKELEEKEE--RLEELKKKLKELEKRLEELEERHELYeeaKAKKEELERLKKR 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  488 VSRLAyTQRILEIVGNIRKQKEEITKilsDTKELQKEINSLFGKLDRTFAVTDELvfKDAK-----------KDDAVRKA 556
Cdd:PRK03918 381 LTGLT-PEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL--KKAKgkcpvcgreltEEHRKELL 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  557 YKYLAALHENCSQLIQTIEDTGTIMREVRDLE-------------------EQIET*MGKKTLSNLEKICEDYRALRQEN 617
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeseliklkelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                 ....*...
gi 26333345  618 AGLLGRVR 625
Cdd:PRK03918 535 IKLKGEIK 542
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
333-592 3.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 333 ELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLpdgAANLAKLQLVVESSAQ 412
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL---LAELARLEQDIARLEE 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 413 RLIHLASQWEKhrvpLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELEtlPKDVSRLA 492
Cdd:COG1196 310 RRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEE 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 493 YTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQ 572
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
                       250       260
                ....*....|....*....|
gi 26333345 573 TIEDTGTIMREVRDLEEQIE 592
Cdd:COG1196 464 LLAELLEEAALLEAALAELL 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
329-575 3.75e-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: 50.44  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    329 AQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAANLAK----LQ 404
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    405 LVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQ-----DCRELESSRRlaEIQELHHSVRAAAEEARRKEEVYKQLVS 479
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieqLKEELKALRE--ALDELRAELTLLNEEAANLRERLESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    480 ELETLPKDVSRLAYT-----QRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAKKDDAVR 554
Cdd:TIGR02168  832 RIAATERRLEDLEEQieelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
                          250       260
                   ....*....|....*....|.
gi 26333345    555 KAYKYLAALHENCSQLIQTIE 575
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLE 932
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
303-627 1.51e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  303 LEPQVQAAQvaDVPATSQRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQA 382
Cdd:PRK03918 357 LEERHELYE--EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  383 LR---LKSRtvELLPDGAANL-AKLQLVVESSAQRLIHLASQWEKHRVPL------LAEYRHLRRLQDC----RELESSR 448
Cdd:PRK03918 435 KGkcpVCGR--ELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELrelekvLKKESELIKLKELaeqlKELEEKL 512
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  449 RLAEIQELhhsvRAAAEEARRKEEVYKQLVSELETLPKDVSRL-AYTQRILEIVGNIRKQKEEITKILSDTKEL----QK 523
Cdd:PRK03918 513 KKYNLEEL----EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeELKKKLAELEKKLDELEEELAELLKELEELgfesVE 588
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  524 EINSLFGKLDRTFAVTDELvfKDAKKDdaVRKAYKYLAALHENCSQLIQTIEDTGTimrEVRDLEEQIET*MGKKTLSNL 603
Cdd:PRK03918 589 ELEERLKELEPFYNEYLEL--KDAEKE--LEREEKELKKLEEELDKAFEELAETEK---RLEELRKELEELEKKYSEEEY 661
                        330       340
                 ....*....|....*....|....
gi 26333345  604 EKICEDYRALRQENAGLLGRVREA 627
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEEL 685
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
328-548 1.93e-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: 47.45  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 328 AAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAANLAKLQLVV 407
Cdd:COG4942  16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 408 ESSAQRLIH-----LASQWEKHRVPLLAE-------YRHLRRLQDCRELESSRR------LAEIQELHHSVRAAAEEARR 469
Cdd:COG4942  96 RAELEAQKEelaelLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARReqaeelRADLAELAALRAELEAERAE 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26333345 470 KEEVYKQLVSELETLPKDVSRLAYTQRILEivGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAK 548
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
320-484 7.35e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 7.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 320 QRLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAAN 399
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 400 LAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVS 479
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                ....*
gi 26333345 480 ELETL 484
Cdd:COG1196 464 LLAEL 468
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
331-627 8.03e-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: 45.82  E-value: 8.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    331 EQELESLREQLASVNHNIEEVEADMKTLGinlvqvetecRQSELsvAEQEQALRLKSRTVELlpdgaanlaklqlvvESS 410
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLE----------RQAEK--AERYKELKAELRELEL---------------ALL 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    411 AQRLIHLASQWEKHRVPLLAEYRHLRRLQDcrelESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELETLPKDV-- 488
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqi 306
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    489 --SRLAYTQRILEIVGNIR--------KQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELVFKDAKKDDAVRKAYK 558
Cdd:TIGR02168  307 lrERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26333345    559 YLAALHENCSQL---IQTIEDTGT-IMREVRDLEEQIET*MGKKTLSNLEKICEDYRALRQENAGLLGRVREA 627
Cdd:TIGR02168  387 KVAQLELQIASLnneIERLEARLErLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
445-615 8.48e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  445 ESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELETLPKDVSRLAYTQRILEI-VGNIRKQKEEITKILSDTKELQK 523
Cdd:PRK03918 204 EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEkIRELEERIEELKKEIEELEEKVK 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345  524 EINSLFGKLDRTFAVTDELVfkdaKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIET*mgKKTLSNL 603
Cdd:PRK03918 284 ELKELKEKAEEYIKLSEFYE----EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKEL--EKRLEEL 357
                        170
                 ....*....|..
gi 26333345  604 EKICEDYRALRQ 615
Cdd:PRK03918 358 EERHELYEEAKA 369
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
333-626 1.66e-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: 45.06  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    333 ELESLREQLASVNHNIEEVEADMKTLginlvqvetecrQSELSVAEQEQALRLKSRTVELLpdgaanlaklqlvvessaq 412
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERL------------RREREKAERYQALLKEKREYEGY------------------- 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    413 rliHLASQWEKHR---VPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRK-EEVYKQLVSELETLPKDV 488
Cdd:TIGR02169  227 ---ELLKEKEALErqkEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEI 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    489 SRL-----AYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDrtfAVTDELVFKDAKKDDAVRKAY---KYL 560
Cdd:TIGR02169  304 ASLersiaEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEevdKEF 380
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26333345    561 AALHENCSQLIQTIEDTGtimREVRDLEEQIEt*mgkKTLSNLEKICEDYRALRQENAGLLGRVRE 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 2.19e-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: 44.67  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    317 ATSQRLEQDTRAAQ--EQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSEL--SVAEQEQALRLKSRTVEL 392
Cdd:TIGR02169  734 KLKERLEELEEDLSslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEAR 813
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    393 LPDGAANLAKLQLVVESSAQRLIHLasqwekhrvpllaeyrhLRRLQDCRELESSRRlAEIQELHHSVRAAAEEARRKEE 472
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQEL-----------------QEQRIDLKEQIKSIE-KEIENLNGKKEELEEELEELEA 875
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26333345    473 VYKQLVSELETLPKDVSRLAYTQRILEIvgNIRKQKEEITKILSDTKELQKEINSLFGKLD 533
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELER--KIEELEAQIEKKRKRLSELKAKLEALEEELS 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
321-534 5.91e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 5.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 321 RLEQDTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRLKsrtvellpdgAANL 400
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA----------EAEL 360
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 401 AKLQLVVESSAQRLIHLASQWEKHRVpllAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSE 480
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26333345 481 LETLPKDVSRLAYTQRILEivgNIRKQKEEITKILSDTKELQKEINSLFGKLDR 534
Cdd:COG1196 438 EEEEEALEEAAEEEAELEE---EEEALLELLAELLEEAALLEAALAELLEELAE 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-528 1.24e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 306 QVQAAQVADVPATSQRLEQdTRAAQEQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRL 385
Cdd:COG1196 256 EELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 386 KSRTVELLpdgAANLAKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAE 465
Cdd:COG1196 335 LEEELEEL---EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26333345 466 EARRKEEVYKQLVSELETLPK-DVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSL 528
Cdd:COG1196 412 LLERLERLEEELEELEEALAElEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
312-530 1.31e-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: 41.97  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    312 VADVPATSQRLEQDTRAAQ------EQELESLREQLASVNHNIEEVEADMKTLGINLVQVETECRQSELSVAEQEQALRL 385
Cdd:TIGR02168  819 AANLRERLESLERRIAATErrledlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    386 KSRTVELLPDGA-----------ANLAKLQLVVESSAQRLIHLASQ-WEKHRVPL-LAEYRHLRRLQDCRELESS-RRL- 450
Cdd:TIGR02168  899 LSEELRELESKRselrreleelrEKLAQLELRLEGLEVRIDNLQERlSEEYSLTLeEAEALENKIEDDEEEARRRlKRLe 978
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    451 AEIQELHHSVRAAAEEARRKEEVYKQLVSELETLPKDVSRLAYTqrileivgnIRKQKEEITKILSDT-----KELQKEI 525
Cdd:TIGR02168  979 NKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEA---------IEEIDREARERFKDTfdqvnENFQRVF 1049

                   ....*
gi 26333345    526 NSLFG 530
Cdd:TIGR02168 1050 PKLFG 1054
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
331-627 3.83e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 331 EQELESLREQLASVNHNIEEVEADMKTLGinlvqvetecRQSElsVAEQEQALRLKSRTVELlpdgaanlaklqlvvESS 410
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLE----------RQAE--KAERYRELKEELKELEA---------------ELL 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 411 AQRLIHLASQWEKhrvpLLAEYRHLRRLQDCRELESSRRLAEIQELHHSVRAAAEEARRKEEVYKQLVSELETLPKDVSR 490
Cdd:COG1196 231 LLKLRELEAELEE----LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345 491 LAytQRILEIVGNIRKQKEEITKILSDTKELQKEINSLFGKLDRTFAVTDELvfkDAKKDDAVRKAYKYLAALHENCSQL 570
Cdd:COG1196 307 LE--ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEEL 381
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26333345 571 IQTIEDTGTIMREVRDLEEQIET*mgKKTLSNLEKICEDYRALRQENAGLLGRVREA 627
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAELEEE 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
324-626 7.96e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 7.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    324 QDTRAAQEQELESLREQLASVNHNIEEVEadmktLGINLVQVETECRQSELSVAEQEQAlRLKSR---TVELLPDGAANL 400
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELR-----LEVSELEEEIEELQKELYALANEIS-RLEQQkqiLRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    401 AKLQLVVESSAQRLIHLA---SQWEKHRVPLLAEyrhlrrLQDCRELESSRRlAEIQELHHSVRAAAEEARRKEEVYKQL 477
Cdd:TIGR02168  319 EELEAQLEELESKLDELAeelAELEEKLEELKEE------LESLEAELEELE-AELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333345    478 VSELETLPKDVSRLAytQRILEIVGNIRKQKEEITKILSDTKELQKEinslfgKLDRTFAVTDELVFKDAKKDDAVRKAY 557
Cdd:TIGR02168  392 ELQIASLNNEIERLE--ARLERLEDRRERLQQEIEELLKKLEEAELK------ELQAELEELEEELEELQEELERLEEAL 463
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26333345    558 KYLAALHENCSQLIQTIEdtgtimREVRDLEEQIEt*MGKKTLSNLEKICEDYRAL---RQENAGLLGRVRE 626
Cdd:TIGR02168  464 EELREELEEAEQALDAAE------RELAQLQARLD--SLERLQENLEGFSEGVKALlknQSGLSGILGVLSE 527
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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