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Conserved domains on  [gi|1622852822|ref|XP_014966906|]
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leucine-rich repeat flightless-interacting protein 1 isoform X1 [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 ...
 259-509 6.49e-56

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: 196.07  E-value: 6.49e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  259 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 329
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  330 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 409
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  410 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 472
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852822  473 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 509
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
 259-509 6.49e-56

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: 196.07  E-value: 6.49e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  259 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 329
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  330 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 409
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  410 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 472
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852822  473 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 509
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
389-506 2.22e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.32  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  389 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 468
Cdd:COG2433    388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622852822  469 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 506
Cdd:COG2433    458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-476 1.82e-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: 45.82  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  283 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKA----MVSNAQLDN 358
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerASLEEALAL 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  359 EKTNFMYQVDTLKDMLLELEEqlaeSRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSI 437
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDE 967

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622852822  438 REISDLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 476
Cdd:TIGR02168  968 EEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 408-487 4.21e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  408 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 485
Cdd:PRK05431    10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89


                   ..
gi 1622852822  486 KK 487
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 ...
 259-509 6.49e-56

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: 196.07  E-value: 6.49e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  259 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 329
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  330 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 409
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  410 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 472
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852822  473 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 509
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
389-506 2.22e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.32  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  389 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 468
Cdd:COG2433    388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622852822  469 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 506
Cdd:COG2433    458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
308-485 4.63e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 4.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  308 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaesRRQ 387
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----EAE 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  388 YEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQL-QQKQASSIREISDLQETIEWKDKKIGALERQKEffdS 466
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELE---E 217

                          170
                   ....*....|....*....
gi 1622852822  467 VRSERDDLREEVVMLKEEL 485
Cdd:COG4717    218 AQEELEELEEELEQLENEL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-476 1.82e-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: 45.82  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  283 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKA----MVSNAQLDN 358
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerASLEEALAL 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  359 EKTNFMYQVDTLKDMLLELEEqlaeSRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSI 437
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDE 967

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622852822  438 REISDLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 476
Cdd:TIGR02168  968 EEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 385-485 2.58e-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: 45.05  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  385 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 460
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100
                   ....*....|....*....|....*....
gi 1622852822  461 KE----FFDSVRSERDDLREEVVMLKEEL 485
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 305-487 3.58e-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: 44.66  E-value: 3.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  305 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 384
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  385 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 464
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622852822  465 DS---------VRSERDDLREEVVMLKEELKK 487
Cdd:TIGR02168  420 QQeieellkklEEAELKELQAELEELEEELEE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 303-487 5.91e-04

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: 43.86  E-value: 5.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  303 DTEASIREIKELNELKD-QIQDVEGKYMQGLKEMKDSLAEVEEKykKAMVSNaqLDNEKTNFMYQVDTLKDMLLELEEQL 381
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKN--NSEIKD--LTNQDSVKELIIKNLDNTRESLETQL 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  382 AESRRQY-------EEKNKEFEREKhahsilqfqfAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI 454
Cdd:TIGR04523  471 KVLSRSInkikqnlEQKQKELKSKE----------KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622852822  455 GALERQKEFFDSVRSeRDDLREEVVMLKEELKK 487
Cdd:TIGR04523  541 SDLEDELNKDDFELK-KENLEKEIDEKNKEIEE 572
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 300-486 1.03e-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: 43.13  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  300 ISIDTEASIREIKE-LNELKDQIQDVEGKYMQGLKEMKDS---LAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLL 375
Cdd:TIGR02169  281 IKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  376 ELEEQLAESRRQYEEKNKEFerekhahsilqfqfAEVKEALKEREEMLEeirQLQQKQASSIREISDLQETIEWKDKKIG 455
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEF--------------AETRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELA 423

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622852822  456 ----ALERQKEFFDSVRSERDDLREEVVMLKEELK 486
Cdd:TIGR02169  424 dlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
410-488 1.08e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.21  E-value: 1.08e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852822  410 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKH 488
Cdd:COG1340      8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
389-487 1.14e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  389 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 468
Cdd:COG4717     53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132

                           90
                   ....*....|....*....
gi 1622852822  469 sERDDLREEVVMLKEELKK 487
Cdd:COG4717    133 -ELEALEAELAELPERLEE 150
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 312-487 1.29e-03

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: 42.70  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  312 KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAES--RRQYE 389
Cdd:TIGR04523  496 KELKKLNEEKKELEEK----VKDLTKKISSLKEKIEK-------LESEKKEKESKISDLEDELNKDDFELKKEnlEKEID 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  390 EKNKEFEREKHahsilqfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDS--- 466
Cdd:TIGR04523  565 EKNKEIEELKQ----------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSiik 634

                          170       180
                   ....*....|....*....|..
gi 1622852822  467 -VRSERDDLREEVVMLKEELKK 487
Cdd:TIGR04523  635 nIKSKKNKLKQEVKQIKETIKE 656
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 308-507 1.31e-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: 42.75  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  308 IREI-KELNELKDQIQDVEGkymqglkemkdSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRR 386
Cdd:TIGR02169  793 IPEIqAELSKLEEEVSRIEA-----------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  387 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIRE----ISDLQETIEWKDKKIGALERQKE 462
Cdd:TIGR02169  862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrLSELKAKLEALEEELSEIEDPKG 941

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622852822  463 FFDSVRSER---DDLREEVVMLKEELKKHGIILNSEIATNGETSDTLN 507
Cdd:TIGR02169  942 EDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 303-488 1.79e-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: 42.36  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  303 DTEASIREI-KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVdtlKDMLLELEEQL 381
Cdd:TIGR02169  234 ALERQKEAIeRQLASLEEELEKLTEE----ISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRV---KEKIGELEAEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  382 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 461
Cdd:TIGR02169  304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379

                          170       180
                   ....*....|....*....|....*..
gi 1622852822  462 efFDSVRSERDDLREEVVMLKEELKKH 488
Cdd:TIGR02169  380 --FAETRDELKDYREKLEKLKREINEL 404
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
309-462 2.23e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  309 REIKELNELKDQIQDVEGKYMQgLKEMKDSLaEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQlaesRRQY 388
Cdd:COG4717     92 ELQEELEELEEELEELEAELEE-LREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEEL 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852822  389 EEKNKEFEREKHAHSILQFQFAEVKEalKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKE 462
Cdd:COG4717    166 EELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 305-484 2.31e-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: 41.98  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  305 EASIREIKE-LNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleEQLAE 383
Cdd:TIGR02169  832 EKEIQELQEqRIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRE 900

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  384 SRRQYEEKNKEFEREKHAHSILQfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALE----R 459
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELK----AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmL 976

                          170       180
                   ....*....|....*....|....*
gi 1622852822  460 QKEFFDSVRSERDDLREEVVMLKEE 484
Cdd:TIGR02169  977 AIQEYEEVLKRLDELKEKRAKLEEE 1001
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-507 2.71e-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: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  281 ATLASLGGTSSRRGSGDTSISIDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 356
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  357 DNEktnfmyqVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIR--------- 427
Cdd:TIGR02168  711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeae 783

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  428 --QLQQKQASSIREISDLQETIewkDKKIGALERQKEFFDSVRSERDDLREEVVML----------KEELKKHGIILNSE 495
Cdd:TIGR02168  784 ieELEAQIEQLKEELKALREAL---DELRAELTLLNEEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAE 860

                          250
                   ....*....|..
gi 1622852822  496 IATNGETSDTLN 507
Cdd:TIGR02168  861 IEELEELIEELE 872
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 409-486 3.47e-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: 38.34  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  409 FAEVKEALKER---EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdsvrsERDDLREEVVMLKEEL 485
Cdd:pfam02403   11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83


                   .
gi 1622852822  486 K 486
Cdd:pfam02403   84 K 84
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 408-487 4.21e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  408 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 485
Cdd:PRK05431    10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89


                   ..
gi 1622852822  486 KK 487
Cdd:PRK05431    90 DE 91
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 301-485 5.00e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  301 SIDTEASIREIKEL---NELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMvsnAQLDNEKTNFM--YQVDTLKDMLL 375
Cdd:COG5185    304 SIDIKKATESLEEQlaaAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL---EAIKEEIENIVgeVELSKSSEELD 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  376 ELEEQLAESRRQYEEKNKEfeREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIG 455
Cdd:COG5185    381 SFKDTIESTKESLDEIPQN--QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD 458

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1622852822  456 AL------ERQKEFFDSVRSERDDLREEVVMLKEEL 485
Cdd:COG5185    459 EEsqsrleEAYDEINRSVRSKKEDLNEELTQIESRV 494
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
303-486 7.26e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  303 DTEASIRE-IKELNELKDQIQDvegkymqglkeMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQL 381
Cdd:PRK02224   262 DLRETIAEtEREREELAEEVRD-----------LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  382 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASsirEISDLQETIEWKDKKIG----AL 457
Cdd:PRK02224   331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE---EIEELEEEIEELRERFGdapvDL 407

                          170       180
                   ....*....|....*....|....*....
gi 1622852822  458 ERQKEFFDSVRSERDDLREEVVMLKEELK 486
Cdd:PRK02224   408 GNAEDFLEELREERDELREREAELEATLR 436
PTZ00121 PTZ00121
MAEBL; Provisional
 310-508 8.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  310 EIKELNELKDQIQDVEGKYMQGLK--EMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQ 387
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  388 YEEKNK----EFEREKHAHSILQFQFAEVKEALKEREEmleEIRQLQQKQASSIReiSDLQETIEWKDKKIGALERQKEF 463
Cdd:PTZ00121  1753 EEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDE---KRRMEVDKKIKDIF--DNFANIIEGGKEGNLVINDSKEM 1827

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622852822  464 FDSVRSERDDLREEVVMLKEELKKHGIILNSEiatNGETSDTLNN 508
Cdd:PTZ00121  1828 EDSAIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEAD 1869
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 306-563 9.77e-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: 40.10  E-value: 9.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  306 ASIREIKELneLKDQIQDVEGKYM---QGLKEMKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TN 362
Cdd:pfam15921  468 AQLESTKEM--LRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRN 545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  363 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISD 442
Cdd:pfam15921  546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852822  443 LQETIEWKDKKI--GALERQKEFFDsVRSERDDLREEVVMLKEEL----KKHGIILNSEIATNGETSDTLNNVGYQgpTK 516
Cdd:pfam15921  626 RVSDLELEKVKLvnAGSERLRAVKD-IKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNKLKMQ--LK 702

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852822  517 MTKAEL----NALKSTgDGTLGRASEVEV--KNEIVANVGK-----------REILHNTEKEQH 563
Cdd:pfam15921  703 SAQSELeqtrNTLKSM-EGSDGHAMKVAMgmQKQITAKRGQidalqskiqflEEAMTNANKEKH 765
 
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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