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Conserved domains on  [gi|1622852838|ref|XP_028687101|]
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leucine-rich repeat flightless-interacting protein 1 isoform X6 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRRFIP super family cl26610
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
52-338 4.04e-57

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


The actual alignment was detected with superfamily member pfam09738:

Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 198.38  E-value: 4.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  52 MKELERQQKEpseysghlnsssrassrassaraspvVEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRR 122
Cdd:pfam09738  20 MRELERQQKE--------------------------VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 123 GSGDTSISIDTEASIREIKelnelkdqiqdvegkymqglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDM 202
Cdd:pfam09738  74 SSEDSSISLEDEGSLRDIK------------------------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 203 LLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE----------------IRQLQQKQASSI 266
Cdd:pfam09738 130 LEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVS 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622852838 267 REISDLQETIewkdkKIGALE-RQKEFFDsvrsERDDLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 338
Cdd:pfam09738 210 VEAAEVLESA-----GEGSLDvRLKKLAD----EKEELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
52-338 4.04e-57

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 198.38  E-value: 4.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  52 MKELERQQKEpseysghlnsssrassrassaraspvVEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRR 122
Cdd:pfam09738  20 MRELERQQKE--------------------------VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 123 GSGDTSISIDTEASIREIKelnelkdqiqdvegkymqglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDM 202
Cdd:pfam09738  74 SSEDSSISLEDEGSLRDIK------------------------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 203 LLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE----------------IRQLQQKQASSI 266
Cdd:pfam09738 130 LEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVS 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622852838 267 REISDLQETIewkdkKIGALE-RQKEFFDsvrsERDDLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 338
Cdd:pfam09738 210 VEAAEVLESA-----GEGSLDvRLKKLAD----EKEELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
218-335 3.72e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 218 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 297
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852838 298 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 335
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
112-305 4.92e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  112 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 191
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  192 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSIREIS 270
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622852838  271 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 305
Cdd:TIGR02168  972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
237-316 4.38e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 237 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 314
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 1622852838 315 KK 316
Cdd:PRK05431   90 DE 91
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
52-338 4.04e-57

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 198.38  E-value: 4.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  52 MKELERQQKEpseysghlnsssrassrassaraspvVEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRR 122
Cdd:pfam09738  20 MRELERQQKE--------------------------VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 123 GSGDTSISIDTEASIREIKelnelkdqiqdvegkymqglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDM 202
Cdd:pfam09738  74 SSEDSSISLEDEGSLRDIK------------------------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 203 LLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE----------------IRQLQQKQASSI 266
Cdd:pfam09738 130 LEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVS 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622852838 267 REISDLQETIewkdkKIGALE-RQKEFFDsvrsERDDLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 338
Cdd:pfam09738 210 VEAAEVLESA-----GEGSLDvRLKKLAD----EKEELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
218-335 3.72e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 218 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 297
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852838 298 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 335
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
112-305 4.92e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  112 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 191
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  192 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSIREIS 270
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622852838  271 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 305
Cdd:TIGR02168  972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
214-314 8.04e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 8.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  214 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 289
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100
                   ....*....|....*....|....*....
gi 1622852838  290 KE----FFDSVRSERDDLREEVVMLKEEL 314
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
134-316 1.03e-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: 43.12  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  134 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 213
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  214 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 293
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622852838  294 DS---------VRSERDDLREEVVMLKEELKK 316
Cdd:TIGR02168  420 QQeieellkklEEAELKELQAELEELEEELEE 451
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
218-316 3.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 218 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 297
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                          90
                  ....*....|....*....
gi 1622852838 298 sERDDLREEVVMLKEELKK 316
Cdd:COG4717   133 -ELEALEAELAELPERLEE 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
129-315 3.89e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  129 ISIDTEASIREIKE-LNELKDQIQDVEGKYMQGLKEMKDS---LAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLL 204
Cdd:TIGR02169  281 IKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  205 ELEEQLAESRRQYEEKNKEFerekhahsilqfqfAEVKEALKEREEMLEeirQLQQKQASSIREISDLQETIEWKDKKIG 284
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEF--------------AETRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELA 423
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622852838  285 ----ALERQKEFFDSVRSERDDLREEVVMLKEELK 315
Cdd:TIGR02169  424 dlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
137-317 4.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 137 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLEleeqlaesRRQ 216
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREE-------LEKLEKLLQL--------LPL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 217 YEEKNKeferekhahsiLQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIE-----WKDKKIGALERQKE 291
Cdd:COG4717   131 YQELEA-----------LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEelleqLSLATEEELQDLAE 199
                         170       180
                  ....*....|....*....|....*.
gi 1622852838 292 FFDSVRSERDDLREEVVMLKEELKKH 317
Cdd:COG4717   200 ELEELQQRLAELEEELEEAQEELEEL 225
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
137-336 4.31e-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: 40.82  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  137 IREI-KELNELKDQIQDVEGkymqglkemkdSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRR 215
Cdd:TIGR02169  793 IPEIqAELSKLEEEVSRIEA-----------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  216 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIRE----ISDLQETIEWKDKKIGALERQKE 291
Cdd:TIGR02169  862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrLSELKAKLEALEEELSEIEDPKG 941
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622852838  292 FFDSVRSER---DDLREEVVMLKEELKKHGIILNSEIATNGETSDTLN 336
Cdd:TIGR02169  942 EDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
237-316 4.38e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 237 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 314
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 1622852838 315 KK 316
Cdd:PRK05431   90 DE 91
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
239-317 7.79e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 7.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852838 239 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKH 317
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
138-291 7.89e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838 138 REIKELNELKDQIQDVEGKYMQgLKEMKDSLaEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQlaesRRQY 217
Cdd:COG4717    92 ELQEELEELEEELEELEAELEE-LREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEEL 165
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852838 218 EEKNKEFEREKHAHSILQFQFAEVKEalKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKE 291
Cdd:COG4717   166 EELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
132-317 8.28e-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: 40.05  E-value: 8.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  132 DTEASIREI-KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVdtlKDMLLELEEQL 210
Cdd:TIGR02169  234 ALERQKEAIeRQLASLEEELEKLTEE----ISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRV---KEKIGELEAEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  211 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 290
Cdd:TIGR02169  304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
                          170       180
                   ....*....|....*....|....*..
gi 1622852838  291 efFDSVRSERDDLREEVVMLKEELKKH 317
Cdd:TIGR02169  380 --FAETRDELKDYREKLEKLKREINEL 404
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
134-313 9.90e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 9.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  134 EASIREIKE-LNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleEQLAE 212
Cdd:TIGR02169  832 EKEIQELQEqRIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRE 900
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852838  213 SRRQYEEKNKEFEREKHAHSILQfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALE----R 288
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELK----AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmL 976
                          170       180
                   ....*....|....*....|....*
gi 1622852838  289 QKEFFDSVRSERDDLREEVVMLKEE 313
Cdd:TIGR02169  977 AIQEYEEVLKRLDELKEKRAKLEEE 1001
 
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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