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Conserved domains on  [gi|1622852825|ref|XP_014966907|]
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leucine-rich repeat flightless-interacting protein 1 isoform X2 [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 ...
 249-499 5.87e-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: 5.87e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  249 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 319
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  320 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 399
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  400 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 462
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852825  463 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 499
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 ...
 249-499 5.87e-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: 5.87e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  249 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 319
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  320 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 399
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  400 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 462
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852825  463 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 499
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
379-496 2.09e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  379 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 458
Cdd:COG2433    388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622852825  459 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 496
Cdd:COG2433    458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 273-466 1.72e-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: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  273 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKA----MVSNAQLDN 348
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerASLEEALAL 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  349 EKTNFMYQVDTLKDMLLELEEqlaeSRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSI 427
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDE 967

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622852825  428 REISDLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 466
Cdd:TIGR02168  968 EEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 398-477 4.02e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  398 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 475
Cdd:PRK05431    10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89


                   ..
gi 1622852825  476 KK 477
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 ...
 249-499 5.87e-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: 5.87e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  249 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 319
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  320 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 399
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  400 AEVKEALKEREEMLEE----------------IRQLQQKQASSIREISDLQETIewkdkKIGALE-RQKEFFDsvrsERD 462
Cdd:pfam09738  166 AELKEQLKQRDELIEKhglvivpdentngeeeNSPADAKRALVSVEAAEVLESA-----GEGSLDvRLKKLAD----EKE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622852825  463 DLREEVVMLKEEL---KKHGIILNSEIATNGETSDTLNNV 499
Cdd:pfam09738  237 ELLDEVRKLKLQLeeeKSKRNSTRSSQSPDGFGLENGSHV 276
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
379-496 2.09e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 48.70  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  379 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 458
Cdd:COG2433    388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622852825  459 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 496
Cdd:COG2433    458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
298-475 4.69e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 4.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  298 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaesRRQ 377
Cdd:COG4717     70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----EAE 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  378 YEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQL-QQKQASSIREISDLQETIEWKDKKIGALERQKEffdS 456
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELE---E 217

                          170
                   ....*....|....*....
gi 1622852825  457 VRSERDDLREEVVMLKEEL 475
Cdd:COG4717    218 AQEELEELEEELEQLENEL 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 273-466 1.72e-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: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  273 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKA----MVSNAQLDN 348
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerASLEEALAL 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  349 EKTNFMYQVDTLKDMLLELEEqlaeSRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSI 427
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDE 967

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622852825  428 REISDLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 466
Cdd:TIGR02168  968 EEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 375-475 2.42e-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: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  375 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 450
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100
                   ....*....|....*....|....*....
gi 1622852825  451 KE----FFDSVRSERDDLREEVVMLKEEL 475
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 295-477 3.45e-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: 3.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  295 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 374
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  375 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 454
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622852825  455 DS---------VRSERDDLREEVVMLKEELKK 477
Cdd:TIGR02168  420 QQeieellkklEEAELKELQAELEELEEELEE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 293-477 4.52e-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: 44.24  E-value: 4.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  293 DTEASIREIKELNELKD-QIQDVEGKYMQGLKEMKDSLAEVEEKykKAMVSNaqLDNEKTNFMYQVDTLKDMLLELEEQL 371
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKN--NSEIKD--LTNQDSVKELIIKNLDNTRESLETQL 470

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  372 AESRRQY-------EEKNKEFEREKhahsilqfqfAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI 444
Cdd:TIGR04523  471 KVLSRSInkikqnlEQKQKELKSKE----------KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622852825  445 GALERQKEFFDSVRSeRDDLREEVVMLKEELKK 477
Cdd:TIGR04523  541 SDLEDELNKDDFELK-KENLEKEIDEKNKEIEE 572
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
400-478 9.50e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.59  E-value: 9.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852825  400 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKH 478
Cdd:COG1340      8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDEL 83
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 290-476 9.94e-04

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: 9.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  290 ISIDTEASIREIKE-LNELKDQIQDVEGKYMQGLKEMKDS---LAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLL 365
Cdd:TIGR02169  281 IKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  366 ELEEQLAESRRQYEEKNKEFerekhahsilqfqfAEVKEALKEREEMLEeirQLQQKQASSIREISDLQETIEWKDKKIG 445
Cdd:TIGR02169  361 ELKEELEDLRAELEEVDKEF--------------AETRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELA 423

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622852825  446 ----ALERQKEFFDSVRSERDDLREEVVMLKEELK 476
Cdd:TIGR02169  424 dlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 302-477 1.01e-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: 43.09  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  302 KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAES--RRQYE 379
Cdd:TIGR04523  496 KELKKLNEEKKELEEK----VKDLTKKISSLKEKIEK-------LESEKKEKESKISDLEDELNKDDFELKKEnlEKEID 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  380 EKNKEFEREKHahsilqfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDS--- 456
Cdd:TIGR04523  565 EKNKEIEELKQ----------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSiik 634

                          170       180
                   ....*....|....*....|..
gi 1622852825  457 -VRSERDDLREEVVMLKEELKK 477
Cdd:TIGR04523  635 nIKSKKNKLKQEVKQIKETIKE 656
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
379-477 1.11e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  379 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 458
Cdd:COG4717     53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132

                           90
                   ....*....|....*....
gi 1622852825  459 sERDDLREEVVMLKEELKK 477
Cdd:COG4717    133 -ELEALEAELAELPERLEE 150
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 298-497 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  298 IREI-KELNELKDQIQDVEGkymqglkemkdSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRR 376
Cdd:TIGR02169  793 IPEIqAELSKLEEEVSRIEA-----------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  377 QYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIRE----ISDLQETIEWKDKKIGALERQKE 452
Cdd:TIGR02169  862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrLSELKAKLEALEEELSEIEDPKG 941

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1622852825  453 FFDSVRSER---DDLREEVVMLKEELKKHGIILNSEIATNGETSDTLN 497
Cdd:TIGR02169  942 EDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 293-478 1.72e-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: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  293 DTEASIREI-KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVdtlKDMLLELEEQL 371
Cdd:TIGR02169  234 ALERQKEAIeRQLASLEEELEKLTEE----ISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRV---KEKIGELEAEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  372 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 451
Cdd:TIGR02169  304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379

                          170       180
                   ....*....|....*....|....*..
gi 1622852825  452 efFDSVRSERDDLREEVVMLKEELKKH 478
Cdd:TIGR02169  380 --FAETRDELKDYREKLEKLKREINEL 404
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 295-474 2.19e-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: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  295 EASIREIKE-LNELKDQIQDVEgkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlleleEQLAE 373
Cdd:TIGR02169  832 EKEIQELQEqRIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRE 900

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  374 SRRQYEEKNKEFEREKHAHSILQfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALE----R 449
Cdd:TIGR02169  901 LERKIEELEAQIEKKRKRLSELK----AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmL 976

                          170       180
                   ....*....|....*....|....*
gi 1622852825  450 QKEFFDSVRSERDDLREEVVMLKEE 474
Cdd:TIGR02169  977 AIQEYEEVLKRLDELKEKRAKLEEE 1001
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
299-452 2.20e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  299 REIKELNELKDQIQDVEGKYMQgLKEMKDSLaEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQlaesRRQY 378
Cdd:COG4717     92 ELQEELEELEEELEELEAELEE-LREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEEL 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852825  379 EEKNKEFEREKHAHSILQFQFAEVKEalKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKE 452
Cdd:COG4717    166 EELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 271-497 2.48e-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: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  271 ATLASLGGTSSRRGSGDTSISIDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 346
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  347 DNEktnfmyqVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIR--------- 417
Cdd:TIGR02168  711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeae 783

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  418 --QLQQKQASSIREISDLQETIewkDKKIGALERQKEFFDSVRSERDDLREEVVML----------KEELKKHGIILNSE 485
Cdd:TIGR02168  784 ieELEAQIEQLKEELKALREAL---DELRAELTLLNEEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAE 860

                          250
                   ....*....|..
gi 1622852825  486 IATNGETSDTLN 497
Cdd:TIGR02168  861 IEELEELIEELE 872
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 399-476 3.02e-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: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  399 FAEVKEALKER---EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdsvrsERDDLREEVVMLKEEL 475
Cdd:pfam02403   11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83


                   .
gi 1622852825  476 K 476
Cdd:pfam02403   84 K 84
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 398-477 4.02e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.82  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  398 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 475
Cdd:PRK05431    10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89


                   ..
gi 1622852825  476 KK 477
Cdd:PRK05431    90 DE 91
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 291-475 4.20e-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: 41.10  E-value: 4.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  291 SIDTEASIREIKEL---NELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMvsnAQLDNEKTNFM--YQVDTLKDMLL 365
Cdd:COG5185    304 SIDIKKATESLEEQlaaAEAEQELEESKRETETGIQNLTAEIEQGQESLTENL---EAIKEEIENIVgeVELSKSSEELD 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  366 ELEEQLAESRRQYEEKNKEfeREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIG 445
Cdd:COG5185    381 SFKDTIESTKESLDEIPQN--QRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD 458

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1622852825  446 AL------ERQKEFFDSVRSERDDLREEVVMLKEEL 475
Cdd:COG5185    459 EEsqsrleEAYDEINRSVRSKKEDLNEELTQIESRV 494
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
293-476 6.65e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 6.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  293 DTEASIRE-IKELNELKDQIQDvegkymqglkeMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQL 371
Cdd:PRK02224   262 DLRETIAEtEREREELAEEVRD-----------LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  372 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASsirEISDLQETIEWKDKKIG----AL 447
Cdd:PRK02224   331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE---EIEELEEEIEELRERFGdapvDL 407

                          170       180
                   ....*....|....*....|....*....
gi 1622852825  448 ERQKEFFDSVRSERDDLREEVVMLKEELK 476
Cdd:PRK02224   408 GNAEDFLEELREERDELREREAELEATLR 436
PTZ00121 PTZ00121
MAEBL; Provisional
 300-498 7.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  300 EIKELNELKDQIQDVEGKYMQGLK--EMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQ 377
Cdd:PTZ00121  1673 DKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  378 YEEKNK----EFEREKHAHSILQFQFAEVKEALKEREEmleEIRQLQQKQASSIReiSDLQETIEWKDKKIGALERQKEF 453
Cdd:PTZ00121  1753 EEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDE---KRRMEVDKKIKDIF--DNFANIIEGGKEGNLVINDSKEM 1827

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622852825  454 FDSVRSERDDLREEVVMLKEELKKHGIILNSEiatNGETSDTLNN 498
Cdd:PTZ00121  1828 EDSAIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEAD 1869
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
301-477 9.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 9.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  301 IKELNELKDQIQDV---EGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMllelEEQLAESRRQ 377
Cdd:PRK03918   171 IKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  378 YEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWK---DKKIGALERQKEFF 454
Cdd:PRK03918   247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGI 326

                          170       180
                   ....*....|....*....|...
gi 1622852825  455 DSVRSERDDLREEVVMLKEELKK 477
Cdd:PRK03918   327 EERIKELEEKEERLEELKKKLKE 349
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 296-553 9.66e-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: 9.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  296 ASIREIKELneLKDQIQDVEGKYM---QGLKEMKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TN 352
Cdd:pfam15921  468 AQLESTKEM--LRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRN 545

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  353 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISD 432
Cdd:pfam15921  546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852825  433 LQETIEWKDKKI--GALERQKEFFDsVRSERDDLREEVVMLKEEL----KKHGIILNSEIATNGETSDTLNNVGYQgpTK 506
Cdd:pfam15921  626 RVSDLELEKVKLvnAGSERLRAVKD-IKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNKLKMQ--LK 702

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852825  507 MTKAEL----NALKSTgDGTLGRASEVEV--KNEIVANVGK-----------REILHNTEKEQH 553
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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