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Conserved domains on  [gi|1622852828|ref|XP_014966908|]
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leucine-rich repeat flightless-interacting protein 1 isoform X3 [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 ...
246-496 1.70e-55

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: 194.92  E-value: 1.70e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  246 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 316
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  317 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 396
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  397 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 459
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852828  460 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 496
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 ...
246-496 1.70e-55

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: 194.92  E-value: 1.70e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  246 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 316
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  317 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 396
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  397 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 459
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852828  460 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 496
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
376-493 2.55e-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: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  376 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 455
Cdd:COG2433    388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622852828  456 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 493
Cdd:COG2433    458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
270-463 2.12e-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: 45.43  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  270 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 349
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  350 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSIREIS 428
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622852828  429 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 463
Cdd:TIGR02168  972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
395-474 4.26e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  395 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 472
Cdd:PRK05431    10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                   ..
gi 1622852828  473 KK 474
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 ...
246-496 1.70e-55

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: 194.92  E-value: 1.70e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  246 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 316
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  317 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 396
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  397 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 459
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852828  460 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 496
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
376-493 2.55e-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: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  376 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 455
Cdd:COG2433    388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622852828  456 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 493
Cdd:COG2433    458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-472 5.50e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  295 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaesRRQ 374
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----EAE 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  375 YEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQL-QQKQASSIREISDLQETIEWKDKKIGALERQKEffdS 453
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELE---E 217
                          170
                   ....*....|....*....
gi 1622852828  454 VRSERDDLREEVVMLKEEL 472
Cdd:COG4717    218 AQEELEELEEELEQLENEL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
270-463 2.12e-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: 45.43  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  270 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 349
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  350 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSIREIS 428
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1622852828  429 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 463
Cdd:TIGR02168  972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
372-472 3.03e-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: 3.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  372 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 447
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100
                   ....*....|....*....|....*....
gi 1622852828  448 KE----FFDSVRSERDDLREEVVMLKEEL 472
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
292-474 4.33e-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: 44.28  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  292 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 371
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  372 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 451
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622852828  452 DS---------VRSERDDLREEVVMLKEELKK 474
Cdd:TIGR02168  420 QQeieellkklEEAELKELQAELEELEEELEE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
290-474 9.45e-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: 43.09  E-value: 9.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  290 DTEASIREIKELNELKD-QIQDVEGKYMQGLKEMKDSLAEVEEKykKAMVSNaqLDNEKTNFMYQVDTLKDMLLELEEQL 368
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKN--NSEIKD--LTNQDSVKELIIKNLDNTRESLETQL 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  369 AESRRQY-------EEKNKEFEREKhahsilqfqfAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI 441
Cdd:TIGR04523  471 KVLSRSInkikqnlEQKQKELKSKE----------KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622852828  442 GALERQKEFFDSVRSeRDDLREEVVMLKEELKK 474
Cdd:TIGR04523  541 SDLEDELNKDDFELK-KENLEKEIDEKNKEIEE 572
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
287-473 1.26e-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: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  287 ISIDTEASIREIKE-LNELKDQIQDVEGKYMQGLKEMKDS---LAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLL 362
Cdd:TIGR02169  281 IKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  363 ELEEQLAESRRQYEEKNKEFerekhahsilqfqfAEVKEALKEREEMLEeirQLQQKQASSIREISDLQETIEWKDKKIG 442
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEF--------------AETRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELA 423
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622852828  443 ----ALERQKEFFDSVRSERDDLREEVVMLKEELK 473
Cdd:TIGR02169  424 dlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
376-474 1.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  376 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 455
Cdd:COG4717     53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                           90
                   ....*....|....*....
gi 1622852828  456 sERDDLREEVVMLKEELKK 474
Cdd:COG4717    133 -ELEALEAELAELPERLEE 150
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
397-475 1.34e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 1.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852828  397 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKH 475
Cdd:COG1340      8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
295-494 1.63e-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: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  295 IREI-KELNELKDQIQDVEGkymqglkemkdSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRR 373
Cdd:TIGR02169  793 IPEIqAELSKLEEEVSRIEA-----------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  374 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIRE----ISDLQETIEWKDKKIGALERQKE 449
Cdd:TIGR02169  862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrLSELKAKLEALEEELSEIEDPKG 941
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622852828  450 FFDSVRSER---DDLREEVVMLKEELKKHGIILNSEIATNGETSDTLN 494
Cdd:TIGR02169  942 EDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
299-474 1.92e-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: 42.31  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  299 KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAES--RRQYE 376
Cdd:TIGR04523  496 KELKKLNEEKKELEEK----VKDLTKKISSLKEKIEK-------LESEKKEKESKISDLEDELNKDDFELKKEnlEKEID 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  377 EKNKEFEREKHahsilqfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDS--- 453
Cdd:TIGR04523  565 EKNKEIEELKQ----------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSiik 634
                          170       180
                   ....*....|....*....|..
gi 1622852828  454 -VRSERDDLREEVVMLKEELKK 474
Cdd:TIGR04523  635 nIKSKKNKLKQEVKQIKETIKE 656
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
290-475 2.20e-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: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  290 DTEASIREI-KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVdtlKDMLLELEEQL 368
Cdd:TIGR02169  234 ALERQKEAIeRQLASLEEELEKLTEE----ISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRV---KEKIGELEAEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  369 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 448
Cdd:TIGR02169  304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
                          170       180
                   ....*....|....*....|....*..
gi 1622852828  449 efFDSVRSERDDLREEVVMLKEELKKH 475
Cdd:TIGR02169  380 --FAETRDELKDYREKLEKLKREINEL 404
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
296-449 2.63e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  296 REIKELNELKDQIQDVEGKYMQgLKEMKDSLaEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQlaesRRQY 375
Cdd:COG4717     92 ELQEELEELEEELEELEAELEE-LREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEEL 165
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852828  376 EEKNKEFEREKHAHSILQFQFAEVKEalKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKE 449
Cdd:COG4717    166 EELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
292-471 2.88e-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: 41.59  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  292 EASIREIKE-LNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleEQLAE 370
Cdd:TIGR02169  832 EKEIQELQEqRIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRE 900
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  371 SRRQYEEKNKEFEREKHAHSILQfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALE----R 446
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELK----AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmL 976
                          170       180
                   ....*....|....*....|....*
gi 1622852828  447 QKEFFDSVRSERDDLREEVVMLKEE 471
Cdd:TIGR02169  977 AIQEYEEVLKRLDELKEKRAKLEEE 1001
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
268-494 3.59e-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: 41.58  E-value: 3.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  268 ATLASLGGTSSRRGSGDTSISIDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 343
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  344 DNEktnfmyqVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIR--------- 414
Cdd:TIGR02168  711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeae 783
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  415 --QLQQKQASSIREISDLQETIewkDKKIGALERQKEFFDSVRSERDDLREEVVML----------KEELKKHGIILNSE 482
Cdd:TIGR02168  784 ieELEAQIEQLKEELKALREAL---DELRAELTLLNEEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAE 860
                          250
                   ....*....|..
gi 1622852828  483 IATNGETSDTLN 494
Cdd:TIGR02168  861 IEELEELIEELE 872
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
396-473 4.19e-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: 37.95  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  396 FAEVKEALKER---EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdsvrsERDDLREEVVMLKEEL 472
Cdd:pfam02403   11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83

                   .
gi 1622852828  473 K 473
Cdd:pfam02403   84 K 84
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
395-474 4.26e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  395 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 472
Cdd:PRK05431    10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                   ..
gi 1622852828  473 KK 474
Cdd:PRK05431    90 DE 91
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
288-472 7.55e-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: 40.33  E-value: 7.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  288 SIDTEASIREIKEL---NELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMvsnAQLDNEKTNFM--YQVDTLKDMLL 362
Cdd:COG5185    304 SIDIKKATESLEEQlaaAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL---EAIKEEIENIVgeVELSKSSEELD 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  363 ELEEQLAESRRQYEEKNKEfeREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIG 442
Cdd:COG5185    381 SFKDTIESTKESLDEIPQN--QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD 458
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1622852828  443 AL------ERQKEFFDSVRSERDDLREEVVMLKEEL 472
Cdd:COG5185    459 EEsqsrleEAYDEINRSVRSKKEDLNEELTQIESRV 494
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
290-473 8.06e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  290 DTEASIRE-IKELNELKDQIQDvegkymqglkeMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQL 368
Cdd:PRK02224   262 DLRETIAEtEREREELAEEVRD-----------LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  369 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASsirEISDLQETIEWKDKKIG----AL 444
Cdd:PRK02224   331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE---EIEELEEEIEELRERFGdapvDL 407
                          170       180
                   ....*....|....*....|....*....
gi 1622852828  445 ERQKEFFDSVRSERDDLREEVVMLKEELK 473
Cdd:PRK02224   408 GNAEDFLEELREERDELREREAELEATLR 436
PTZ00121 PTZ00121
MAEBL; Provisional
297-495 9.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 9.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  297 EIKELNELKDQIQDVEGKYMQGLK--EMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQ 374
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852828  375 YEEKNK----EFEREKHAHSILQFQFAEVKEALKEREEmleEIRQLQQKQASSIReiSDLQETIEWKDKKIGALERQKEF 450
Cdd:PTZ00121  1753 EEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDE---KRRMEVDKKIKDIF--DNFANIIEGGKEGNLVINDSKEM 1827
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622852828  451 FDSVRSERDDLREEVVMLKEELKKHGIILNSEiatNGETSDTLNN 495
Cdd:PTZ00121  1828 EDSAIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEAD 1869
 
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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