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Conserved domains on  [gi|27370460|ref|NP_766534|]
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keratin-like protein KRT222 isoform 1 [Mus musculus]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
2-149 5.15e-33

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 123.11  E-value: 5.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460     2 ELSQLLNEIRANYEQLLTRNQIETVLSTRIQLEEdITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLEN 81
Cdd:pfam00038 167 DLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEE-LQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370460    82 SLQASEQHYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEEIR 149
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
2-149 5.15e-33

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 123.11  E-value: 5.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460     2 ELSQLLNEIRANYEQLLTRNQIETVLSTRIQLEEdITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLEN 81
Cdd:pfam00038 167 DLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEE-LQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370460    82 SLQASEQHYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEEIR 149
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-147 6.15e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 6.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   2 ELSQLLNEIRANYeQLLTRNQIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLEN 81
Cdd:COG1196 217 ELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370460  82 SLQASEQ---HYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEE 147
Cdd:COG1196 296 ELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-147 1.90e-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: 42.75  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460      2 ELSQLLNEIRANYEQlltRNQIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEARRQCHHL--------QVEIESLH 73
Cdd:TIGR02169  224 EGYELLKEKEALERQ---KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELE 300
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370460     74 AVERGLENSLQASEQHYQ---MQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEE 147
Cdd:TIGR02169  301 AEIASLERSIAEKERELEdaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
2-149 5.15e-33

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 123.11  E-value: 5.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460     2 ELSQLLNEIRANYEQLLTRNQIETVLSTRIQLEEdITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLEN 81
Cdd:pfam00038 167 DLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEE-LQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370460    82 SLQASEQHYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEEIR 149
Cdd:pfam00038 246 QLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-147 6.15e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 6.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   2 ELSQLLNEIRANYeQLLTRNQIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLEN 81
Cdd:COG1196 217 ELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370460  82 SLQASEQ---HYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEE 147
Cdd:COG1196 296 ELARLEQdiaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
23-147 2.49e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.62  E-value: 2.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460  23 IETVLSTRIqlEEDITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLENslqaseqhyqmQLQDLESVIG 102
Cdd:COG2433 378 IEEALEELI--EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA-----------ELEEKDERIE 444
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 27370460 103 RLERELQEVRRGIERQLREHEMLlntkMRLEQEIATYRRLLEQEE 147
Cdd:COG2433 445 RLERELSEARSEERREIRKDREI----SRLDREIERLERELEEER 485
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-149 5.45e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 5.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   20 RNQIETVLSTRIQLEEDITKkMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVeRGLENSLQASEQhyqmQLQDLE- 98
Cdd:COG4913  609 RAKLAALEAELAELEEELAE-AEERLEALEAELDALQERREALQRLAEYSWDEIDV-ASAEREIAELEA----ELERLDa 682
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27370460   99 --SVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEEIR 149
Cdd:COG4913  683 ssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-149 1.69e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   2 ELSQLLNEIRANYEQLLTRNQIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLEN 81
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370460  82 SLQASEQHYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEEIR 149
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2-147 1.90e-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: 42.75  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460      2 ELSQLLNEIRANYEQlltRNQIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEARRQCHHL--------QVEIESLH 73
Cdd:TIGR02169  224 EGYELLKEKEALERQ---KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELE 300
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370460     74 AVERGLENSLQASEQHYQ---MQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEE 147
Cdd:TIGR02169  301 AEIASLERSIAEKERELEdaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
5-136 2.09e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.19  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460     5 QLLNEIRANYEQLLTRN-QIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLENSL 83
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGvKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMM 234
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27370460    84 QASEQHYQMQLQDLESvigRLERE----LQEVRRGIERQLREHEMLLNTKMR-----LEQEI 136
Cdd:pfam02841 235 EAQERSYQEHVKQLIE---KMEAEreqlLAEQERMLEHKLQEQEELLKEGFKteaesLQKEI 293
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
35-120 3.54e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460  35 EDITKKMDKDGEALKAAQAELKEARRQCHHLQVEIESLHAVERGLENSLQASEQhyqmQLQDLESVIGRLERELQEVRRG 114
Cdd:COG4942  30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEIAELRAELEAQKEE 105

                ....*.
gi 27370460 115 IERQLR 120
Cdd:COG4942 106 LAELLR 111
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
46-137 4.19e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460  46 EALKAAQAELKEARRQCHHLQVEIESLHAVERGLENSLQASEQhyqmQLQDLESVIGRLERELQEVRRGIERQLREHEML 125
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELAELEKEIAEL 95
                        90
                ....*....|..
gi 27370460 126 LNTKMRLEQEIA 137
Cdd:COG4942  96 RAELEAQKEELA 107
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2-141 4.50e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   2 ELSQLLNEI----RANYEQLLTRNQIETVLSTRIQLEEDITKKMDKDGEALKAAQAELKEarrqchhLQVEIESLHAVER 77
Cdd:COG4942 105 ELAELLRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA-------LRAELEAERAELE 177
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370460  78 GLENSLQASEQHYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRR 141
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2-149 5.43e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 5.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   2 ELSQLLNEIRANYEQLLTR-----NQIETVLSTRIQLEEDITK------KMDKDGEALKAAQAELKEARRQCHHLQVEIE 70
Cdd:COG1196 278 ELELELEEAQAEEYELLAElarleQDIARLEERRRELEERLEEleeelaELEEELEELEEELEELEEELEEAEEELEEAE 357
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27370460  71 SLHAVERGLENSLQASEQHYQMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEEIR 149
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-148 7.74e-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: 37.73  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460      2 ELSQLLNEIR--------ANYEQLLTRNQIETVLSTRIQLEEDITKKMDKDGEA---LKAAQAELKEARRQCHHLQVEIE 70
Cdd:TIGR02168  706 ELEELEEELEqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeIEELEERLEEAEEELAEAEAEIE 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460     71 SLHAVERGLENSLQASEQHY---QMQLQDLESVIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIATYRRLLEQEE 147
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALdelRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865

                   .
gi 27370460    148 I 148
Cdd:TIGR02168  866 E 866
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2-137 8.67e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 37.69  E-value: 8.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370460   2 ELSQLLNEIRANYEQLLTRNQIETVLSTRIQLEEDITKKMDKDGE---ALKAAQAELKEARRQchhLQVEIESLHAVERG 78
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQ---LQQEAQRILASLEA 320
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27370460  79 LENSLQASEQHYQMQLQDLES---VIGRLERELQEVRRGIERQLREHEMLLNTKMRLEQEIA 137
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEArlaELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
 
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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