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Conserved domains on  [gi|1622852835|ref|XP_014966924|]
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leucine-rich repeat flightless-interacting protein 1 isoform X5 [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 ...
162-388 2.10e-59

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: 205.32  E-value: 2.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 162 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 232
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 233 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE-------- 304
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpd 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 305 --------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERDDLREEVVMLKEEL---KKHGIILN 372
Cdd:pfam09738 190 entngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKEELLDEVRKLKLQLeeeKSKRNSTR 260
                         250
                  ....*....|....*.
gi 1622852835 373 SEIATNGETSDTLNNV 388
Cdd:pfam09738 261 SSQSPDGFGLENGSHV 276
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
162-388 2.10e-59

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: 205.32  E-value: 2.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 162 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 232
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 233 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE-------- 304
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpd 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 305 --------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERDDLREEVVMLKEEL---KKHGIILN 372
Cdd:pfam09738 190 entngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKEELLDEVRKLKLQLeeeKSKRNSTR 260
                         250
                  ....*....|....*.
gi 1622852835 373 SEIATNGETSDTLNNV 388
Cdd:pfam09738 261 SSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-385 3.39e-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: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852835 348 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 385
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
264-364 5.40e-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: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  264 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 339
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100
                   ....*....|....*....|....*....
gi 1622852835  340 KE----FFDSVRSERDDLREEVVMLKEEL 364
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKL 346
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
287-366 4.37e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 287 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 364
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 1622852835 365 KK 366
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 ...
162-388 2.10e-59

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: 205.32  E-value: 2.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 162 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 232
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 233 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE-------- 304
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpd 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 305 --------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERDDLREEVVMLKEEL---KKHGIILN 372
Cdd:pfam09738 190 entngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKEELLDEVRKLKLQLeeeKSKRNSTR 260
                         250
                  ....*....|....*.
gi 1622852835 373 SEIATNGETSDTLNNV 388
Cdd:pfam09738 261 SSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-385 3.39e-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: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852835 348 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 385
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
264-364 5.40e-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: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  264 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 339
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100
                   ....*....|....*....|....*....
gi 1622852835  340 KE----FFDSVRSERDDLREEVVMLKEEL 364
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
206-355 5.40e-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: 5.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  206 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLkdmllelEEQLAESRRQYEEKNKEFEREKHAHSILQ 285
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEGLE 935
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852835  286 FQFAEVKEALKEREEM-LEEIRQLQQKQASSIREISDLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 355
Cdd:TIGR02168  936 VRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
201-442 2.35e-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: 42.03  E-value: 2.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  201 TSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TNFMYQVDTLKDMLLELEEQL 260
Cdd:pfam15921  485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRNVQTECEALKLQMAEKDKVI 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  261 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALER 338
Cdd:pfam15921  565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSER 644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  339 QKEFFDsVRSERDDLREEVVMLKEEL----KKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKAEL----NALKSTgDG 410
Cdd:pfam15921  645 LRAVKD-IKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNKLKMQ--LKSAQSELeqtrNTLKSM-EG 720
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622852835  411 TLGRASEVEV--KNEIVANVGK-----------REILHNTEKEQH 442
Cdd:pfam15921  721 SDGHAMKVAMgmQKQITAKRGQidalqskiqflEEAMTNANKEKH 765
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
268-366 2.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                          90
                  ....*....|....*....
gi 1622852835 348 sERDDLREEVVMLKEELKK 366
Cdd:COG4717   133 -ELEALEAELAELPERLEE 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-386 2.49e-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: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  185 TLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESR 264
Cdd:TIGR02168  653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  265 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIR-----------QLQQKQASSIREISDLQETIewkDKKI 333
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeaeieELEAQIEQLKEELKALREAL---DELR 809
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622852835  334 GALERQKEFFDSVRSERDDLREEVVML----------KEELKKHGIILNSEIATNGETSDTLN 386
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAEIEELEELIEELE 872
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
289-367 4.04e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.28  E-value: 4.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852835 289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKH 367
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
287-366 4.37e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 287 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 364
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 1622852835 365 KK 366
Cdd:PRK05431   90 DE 91
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
207-365 6.92e-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: 40.44  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  207 TEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAhsilqf 286
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE------ 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835  287 qFAEVKEALKEREEMLEeirQLQQKQASSIREISDLQETIEWKDKKIG----ALERQKEFFDSVRSERDDLREEVVMLKE 362
Cdd:TIGR02169  380 -FAETRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELAdlnaAIAGIEAKINELEEEKEDKALEIKKQEW 455

                   ...
gi 1622852835  363 ELK 365
Cdd:TIGR02169  456 KLE 458
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
288-365 9.74e-03

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 36.80  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852835 288 FAEVKEALKER---EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdsvrsERDDLREEVVMLKEEL 364
Cdd:pfam02403  11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83

                  .
gi 1622852835 365 K 365
Cdd:pfam02403  84 K 84
 
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.
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