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Conserved domains on  [gi|240254053|ref|NP_001031019|]
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RUN/FYVE domain protein [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
75-315 5.86e-07

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    75 ESGSSINKQKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESF---LNAYQ 151
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   152 ESFCEMKCSIEARDRKILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENI 231
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   232 RALEEKLKCHETELQSKDNIISELSAQLES-EKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMK--------- 301
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreklaql 927
                          250
                   ....*....|....*....
gi 240254053   302 -----GLEMILQRIQESVS 315
Cdd:TIGR02168  928 elrleGLEVRIDNLQERLS 946
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
75-315 5.86e-07

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: 51.98  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    75 ESGSSINKQKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESF---LNAYQ 151
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   152 ESFCEMKCSIEARDRKILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENI 231
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   232 RALEEKLKCHETELQSKDNIISELSAQLES-EKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMK--------- 301
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreklaql 927
                          250
                   ....*....|....*....
gi 240254053   302 -----GLEMILQRIQESVS 315
Cdd:TIGR02168  928 elrleGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
91-343 3.23e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  91 IRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESFLNAYQESfcemKCSIEARDRKILM 170
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL----LAELARLEQDIAR 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 171 LHEKITSHLTLFDSIEKEASVIKKvihEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENIRALEEKLkchETELQSKDN 250
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAEAEEE 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 251 IISELSAQLESEKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQESVSLMTEEDRKVFTSILT 330
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                        250
                 ....*....|...
gi 240254053 331 FEQGSDERNKRSR 343
Cdd:COG1196  461 LLELLAELLEEAA 473
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
88-311 1.13e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  88 EDCIRKVQELQADLASSRETQEALERKVSYLQndysllenKQSELKTTIQNLLQSREsflnAYQESFCEMKCSIEARDRK 167
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERRE----DLEELIAERRETIEEKRER 538
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 168 ILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVF--IENIRA----LEEKLK-C 240
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaIADAEDeierLREKREaL 618
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 241 HETELQSKDNI------ISELSAQLES---EKSKNEHQHQVEELQK-------------TLQVKDLAVENLISEKEALYS 298
Cdd:PRK02224 619 AELNDERRERLaekrerKRELEAEFDEariEEAREDKERAEEYLEQveekldelreerdDLQAEIGAVENELEELEELRE 698
                        250
                 ....*....|...
gi 240254053 299 EMKGLEMILQRIQ 311
Cdd:PRK02224 699 RREALENRVEALE 711
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
88-328 3.73e-03

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 39.29  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   88 EDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESFLNAYQESFCEMKcSIEARDRk 167
Cdd:pfam04108  17 TDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLR-NTPVEPA- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  168 ilmLHEKITSHLTLFD-----SIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYekvfIENIRALEEKLKCHE 242
Cdd:pfam04108  95 ---LPPGEEKQKTLLDfidedSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKE----LESLSSPSESISLIP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  243 TELQSKDNIISELSAQLES-----EKSKNEHQHQVEELQKTLQV---KDLAVENLISEKEALYSEMKGLEMILQRIQESV 314
Cdd:pfam04108 168 TLLKELESLEEEMASLLESltnhyDQCVTAVKLTEGGRAEMLEVlenDARELDDVVPELQDRLDEMENNYERLQKLLEQK 247
                         250
                  ....*....|....
gi 240254053  315 SLMTEEDRKVFTSI 328
Cdd:pfam04108 248 NSLIDELLSALQLI 261
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
75-315 5.86e-07

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: 51.98  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    75 ESGSSINKQKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESF---LNAYQ 151
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   152 ESFCEMKCSIEARDRKILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENI 231
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   232 RALEEKLKCHETELQSKDNIISELSAQLES-EKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMK--------- 301
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRELESKRSELRRELEelreklaql 927
                          250
                   ....*....|....*....
gi 240254053   302 -----GLEMILQRIQESVS 315
Cdd:TIGR02168  928 elrleGLEVRIDNLQERLS 946
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-355 1.37e-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: 50.83  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    80 INKQKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQ------NDYSLLENKQSELKTTIQ-NLLQSRESFLNAYQE 152
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLvLRLEELREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   153 SFCEMKCSIEARDRKILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENIR 232
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   233 ALEEKLKCHETELQSKDNIISELSAQLESEKSK-NEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQ 311
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAElEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 240254053   312 ESVSlMTEEDRKVFTSILTFEQGSDERNKRSRHNDTVDKMEELL 355
Cdd:TIGR02168  407 ARLE-RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
92-315 1.95e-06

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: 50.45  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    92 RKVQELQADLASSRETQEALERKVSYLQNDyslLENKQSELKTTIQNLlQSRESFLNAYQESFCEmkcsIEARDRkilml 171
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQE---IENVKSELKELEARI-EELEEDLHKLEEALND----LEARLS----- 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   172 HEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKK-------EDVVTGLKEKMDHVSTYEKVF---IENIRALEEKLkch 241
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIekeIENLNGKKEEL--- 866
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   242 ETELQSKDNIISELSAQL--------ESEKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQES 313
Cdd:TIGR02169  867 EEELEELEAALRDLESRLgdlkkerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946

                   ..
gi 240254053   314 VS 315
Cdd:TIGR02169  947 PE 948
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
91-343 3.23e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  91 IRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESFLNAYQESfcemKCSIEARDRKILM 170
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL----LAELARLEQDIAR 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 171 LHEKITSHLTLFDSIEKEASVIKKvihEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENIRALEEKLkchETELQSKDN 250
Cdd:COG1196  307 LEERRRELEERLEELEEELAELEE---ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AELAEAEEE 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 251 IISELSAQLESEKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQESVSLMTEEDRKVFTSILT 330
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                        250
                 ....*....|...
gi 240254053 331 FEQGSDERNKRSR 343
Cdd:COG1196  461 LLELLAELLEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
92-308 3.78e-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: 46.20  E-value: 3.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    92 RKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSREsflnAYQESFCEMKcsieardrkilml 171
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD----ELAEELAELE------------- 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   172 hEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENIRALEEKLKCHETELQSKDNI 251
Cdd:TIGR02168  344 -EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 240254053   252 ISELSAQLEsEKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQ 308
Cdd:TIGR02168  423 IEELLKKLE-EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
78-312 1.09e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  78 SSINKQKQTEEdciRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSREsflnAYQESFCEM 157
Cdd:COG4942   30 EQLQQEIAELE---KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA----ELRAELEAQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 158 KCSIEARDRKILMLHEkiTSHLTLFDSIEKEASVIKKVIHeVQGLVDKKEDVVTGLKEKmdhvstyekvfIENIRALEEK 237
Cdd:COG4942  103 KEELAELLRALYRLGR--QPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRAD-----------LAELAALRAE 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254053 238 LkchETELQSKDNIISELSAQLES-EKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQE 312
Cdd:COG4942  169 L---EAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
88-311 1.13e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  88 EDCIRKVQELQADLASSRETQEALERKVSYLQndysllenKQSELKTTIQNLLQSREsflnAYQESFCEMKCSIEARDRK 167
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLEERRE----DLEELIAERRETIEEKRER 538
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 168 ILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVF--IENIRA----LEEKLK-C 240
Cdd:PRK02224 539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLaaIADAEDeierLREKREaL 618
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 241 HETELQSKDNI------ISELSAQLES---EKSKNEHQHQVEELQK-------------TLQVKDLAVENLISEKEALYS 298
Cdd:PRK02224 619 AELNDERRERLaekrerKRELEAEFDEariEEAREDKERAEEYLEQveekldelreerdDLQAEIGAVENELEELEELRE 698
                        250
                 ....*....|...
gi 240254053 299 EMKGLEMILQRIQ 311
Cdd:PRK02224 699 RREALENRVEALE 711
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
81-403 1.23e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  81 NKQKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTtIQNLLQSRESFLNAYQ--ESFCEMK 158
Cdd:COG4717   60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-LREELEKLEKLLQLLPlyQELEALE 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 159 CSIEARDRKILMLHEKITSHLTLFDSIEKeasvIKKVIHEVQGLVDKKEDVVTGLKEKmdhvstYEKVFIENIRALEEKL 238
Cdd:COG4717  139 AELAELPERLEELEERLEELRELEEELEE----LEAELAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRL 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 239 KCHETELQSKDNIISELSAQLESEKSKNEHQHQVEELQKTLQVkdLAVENLISEKEALYSE-MKGLEMILQRIQESVSLM 317
Cdd:COG4717  209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL--LLIAAALLALLGLGGSlLSLILTIAGVLFLVLGLL 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 318 TEEDRKVFTSILTFEQGSDERNKRSRHNDtVDKMEELLYVAPVMHSQENSVKVIPSASPRCQHQKTDCRSIQDDDHQLDS 397
Cdd:COG4717  287 ALLFLLLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365

                 ....*.
gi 240254053 398 AEYLQH 403
Cdd:COG4717  366 EELEQE 371
ATG17_like pfam04108
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...
88-328 3.73e-03

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.


Pssm-ID: 427715 [Multi-domain]  Cd Length: 360  Bit Score: 39.29  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   88 EDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESFLNAYQESFCEMKcSIEARDRk 167
Cdd:pfam04108  17 TDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLR-NTPVEPA- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  168 ilmLHEKITSHLTLFD-----SIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYekvfIENIRALEEKLKCHE 242
Cdd:pfam04108  95 ---LPPGEEKQKTLLDfidedSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKE----LESLSSPSESISLIP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  243 TELQSKDNIISELSAQLES-----EKSKNEHQHQVEELQKTLQV---KDLAVENLISEKEALYSEMKGLEMILQRIQESV 314
Cdd:pfam04108 168 TLLKELESLEEEMASLLESltnhyDQCVTAVKLTEGGRAEMLEVlenDARELDDVVPELQDRLDEMENNYERLQKLLEQK 247
                         250
                  ....*....|....
gi 240254053  315 SLMTEEDRKVFTSI 328
Cdd:pfam04108 248 NSLIDELLSALQLI 261
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
94-319 4.18e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 4.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    94 VQELQADLassRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSRESFLNAYQESFC-----EMKCSIEARDRKi 168
Cdd:pfam15921  326 VSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrEKELSLEKEQNK- 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   169 lMLHEKITSHLTLFDSIEKE-----------ASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVF---IENIRAL 234
Cdd:pfam15921  402 -RLWDRDTGNSITIDHLRRElddrnmevqrlEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLestKEMLRKV 480
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   235 EEKLKCHETELQSKDNIISELSAQLESEKSKNEHQH------------QVEELQKtLQVKDLAVENLISEKEALYSEMKG 302
Cdd:pfam15921  481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNaeitklrsrvdlKLQELQH-LKNEGDHLRNVQTECEALKLQMAE 559
                          250
                   ....*....|....*..
gi 240254053   303 LEMILQRIQESVSLMTE 319
Cdd:pfam15921  560 KDKVIEILRQQIENMTQ 576
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-314 4.82e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  80 INKQKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSREsflnayqesfcemkc 159
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE--------------- 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 160 siEARDRKILMLHEKITSHLTLFDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTyEKVFIENIRALEEKLK 239
Cdd:COG1196  334 --ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEE 410
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240254053 240 CHETELQS-KDNIISELSAQLESEKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQESV 314
Cdd:COG1196  411 ALLERLERlEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
83-323 6.18e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053  83 QKQTEEDCIRKVQELQADLASSRETQEALERKVSYLQNDYSLLENKQSELKTTIQNLLQSresflnayqesfcemkcsIE 162
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE------------------LA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 163 ARDRKILMLHEKITshlTLFDSIEKEASVIKKVIHEVQ--GLVDKKEDVVTGLK-EKMDHVSTYEKVFIENIRALEEKLK 239
Cdd:COG4942   80 ALEAELAELEKEIA---ELRAELEAQKEELAELLRALYrlGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053 240 CHETELQSKDNIISELSAQLESEKSKNEHQHQveELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQESVSLMTE 319
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERA--ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234

                 ....
gi 240254053 320 EDRK 323
Cdd:COG4942  235 EAAA 238
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
87-320 7.00e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 7.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053    87 EEDCIRKVQELQADLASSRETQEALERKVSYLQndYSLLENKQS--ELKTTIQNLLQSRESFLNAYQESFCEMKCSIEAR 164
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKEKREYEG--YELLKEKEAleRQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   165 DRKILMLHEKITshltlfDSIEKEASVIKKVIHEVQGLVDKKEDVVTGLKEKMDHVSTYEKVFIENIRALEEKLKCHETE 244
Cdd:TIGR02169  271 EQLLEELNKKIK------DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240254053   245 LQS----KDNIISELSaqlESEKSKNEHQHQVEELQKTLQVKDLAVENLISEKEALYSEMKGLEMILQRIQESVSLMTEE 320
Cdd:TIGR02169  345 IEEerkrRDKLTEEYA---ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
 
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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