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Conserved domains on  [gi|767934685|ref|XP_011512442|]
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sperm flagellar protein 2 isoform X6 [Homo sapiens]

Protein Classification

CH_2 and NK domain-containing protein( domain architecture ID 10533623)

CH_2 and NK domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
 5-97 2.92e-24

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


:

Pssm-ID: 461871  Cd Length: 91  Bit Score: 98.66  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685     5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294    1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77

                           90
                   ....*....|....
gi 767934685    84 GIITEKPGVATKLL 97
Cdd:pfam06294   78 DLANGKPGAAERLL 91
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 629-811 7.44e-13

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member cd01428:

Pssm-ID: 450170 [Multi-domain]  Cd Length: 194  Bit Score: 69.19  E-value: 7.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 708
Cdd:cd01428    44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 787
Cdd:cd01428   106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170

                         170       180
                  ....*....|....*....|....
gi 767934685  788 PLLEqwFSEPENILIKINAEIDKE 811
Cdd:cd01428   171 PLID--YYKKKGKLVEIDGSGDID 192
 
Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
 5-97 2.92e-24

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


Pssm-ID: 461871  Cd Length: 91  Bit Score: 98.66  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685     5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294    1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77

                           90
                   ....*....|....
gi 767934685    84 GIITEKPGVATKLL 97
Cdd:pfam06294   78 DLANGKPGAAERLL 91
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 629-811 7.44e-13

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 69.19  E-value: 7.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 708
Cdd:cd01428    44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 787
Cdd:cd01428   106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170

                         170       180
                  ....*....|....*....|....
gi 767934685  788 PLLEqwFSEPENILIKINAEIDKE 811
Cdd:cd01428   171 PLID--YYKKKGKLVEIDGSGDID 192
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 629-821 1.35e-09

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 60.14  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 708
Cdd:COG0563    45 LGKKAKEYMDAGELVPDEIVIGLVKERLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKL----------------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNLR---DQ---IQHRIIG 782
Cdd:COG0563   108 -------------DAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVCDKCGGELVQradDNeetVRKRLEV 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767934685  783 FLDN-WPLLEqwFSEPENILIKINAEIDKESLCEKVKEIL 821
Cdd:COG0563   175 YHEQtAPLID--YYRKKGKLVEIDGEGSIEEVTADILAIL 212
adk PRK00279
adenylate kinase; Reviewed
 629-738 3.32e-08

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 55.93  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 708
Cdd:PRK00279   45 LGKEAKSYMDAGELVPDEIVIGLVKERLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKL----------------- 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRM 738
Cdd:PRK00279  108 -------------DAVIEIDVPDEELVERL 124
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 629-684 1.18e-07

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 54.55  E-value: 1.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934685   629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQD-CILDGFPMTLNQAQLLEEAL 684
Cdd:TIGR01351   44 LGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENgFILDGFPRTLSQAEALDALL 100
ADK pfam00406
Adenylate kinase;
628-685 1.75e-05

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 47.30  E-value: 1.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767934685   628 QLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALT 685
Cdd:pfam00406   40 ELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFLLDGFPRTVPQAEALEELLE 97
 
Name Accession Description Interval E-value
CH_2 pfam06294
CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably ...
 5-97 2.92e-24

CH-like domain in sperm protein; Spef is a region of sperm flagellar proteins. It probably exerts a role in spermatogenesis in that the protein is expressed predominantly in adult tissue. It is present in the tails of developing and epididymal sperm internal to the fibrous sheath and around the dense outer fibres of the sperm flagellum. The amino-terminal domain (residues 1-110) shows a possible calponin homology (CH) domain; however Spef does not bind actin directly under in vitro conditions, so the function of the amino-terminal calponin-like domain is unclear. Transcription aberrations leading to a truncated protein result in immotile sperm.


Pssm-ID: 461871  Cd Length: 91  Bit Score: 98.66  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685     5 LCQWLNkELKVSRTVspKSFAKAFSSGYLLGEVLHKFELQD-DFSEFLDSRVSSAKLNNFSRLEPTLNLLGVQFDQNVAH 83
Cdd:pfam06294    1 LLKWLQ-SLDLSRPV--RNIARDFSDGFLVAEILSRYYPKLvDLHNYSPGSSVAAKLNNWETLEKVLKKLGIKLSKEDIE 77

                           90
                   ....*....|....
gi 767934685    84 GIITEKPGVATKLL 97
Cdd:pfam06294   78 DLANGKPGAAERLL 91
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 629-811 7.44e-13

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 69.19  E-value: 7.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNlteverkkaqkstlaidp 708
Cdd:cd01428    44 LGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKKGFILDGFPRTVDQAEALDELLDEGIKP------------------ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNlrDQIQHRIIGFLDN-W 787
Cdd:cd01428   106 -------------DKVIELDVPDEVLIERILGRRICPVSGRVYHLGKDDVTGEPLSQRSDDNE--ETIKKRLEVYKEQtA 170

                         170       180
                  ....*....|....*....|....
gi 767934685  788 PLLEqwFSEPENILIKINAEIDKE 811
Cdd:cd01428   171 PLID--YYKKKGKLVEIDGSGDID 192
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 629-821 1.35e-09

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 60.14  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 708
Cdd:COG0563    45 LGKKAKEYMDAGELVPDEIVIGLVKERLAQPDCANGFILDGFPRTVAQAEALDELLAELGIKL----------------- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRMNDIIAEELSYKTAHEDISQRVAAENQDKDGDQNLR---DQ---IQHRIIG 782
Cdd:COG0563   108 -------------DAVIELDVDDEELVERLSGRRVCPNCGATYHVKFNPPKVEGVCDKCGGELVQradDNeetVRKRLEV 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767934685  783 FLDN-WPLLEqwFSEPENILIKINAEIDKESLCEKVKEIL 821
Cdd:COG0563   175 YHEQtAPLID--YYRKKGKLVEIDGEGSIEEVTADILAIL 212
adk PRK00279
adenylate kinase; Reviewed
 629-738 3.32e-08

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 55.93  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLteverkkaqkstlaidp 708
Cdd:PRK00279   45 LGKEAKSYMDAGELVPDEIVIGLVKERLAQPDCKNGFLLDGFPRTIPQAEALDEMLKELGIKL----------------- 107

                          90       100       110
                  ....*....|....*....|....*....|
gi 767934685  709 atskeiplpspafDFVILLDVSDTSSMSRM 738
Cdd:PRK00279  108 -------------DAVIEIDVPDEELVERL 124
adk TIGR01351
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ...
 629-684 1.18e-07

adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 273569 [Multi-domain]  Cd Length: 210  Bit Score: 54.55  E-value: 1.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767934685   629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQD-CILDGFPMTLNQAQLLEEAL 684
Cdd:TIGR01351   44 LGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNENgFILDGFPRTLSQAEALDALL 100
adk PRK02496
adenylate kinase; Provisional
 623-694 6.72e-06

adenylate kinase; Provisional


Pssm-ID: 179433 [Multi-domain]  Cd Length: 184  Bit Score: 48.59  E-value: 6.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767934685  623 LTTRAQLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLTEV 694
Cdd:PRK02496   40 IKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQPDAANGWILDGFPRKVTQAAFLDELLQEIGQSGERV 111
PLN02674 PLN02674
adenylate kinase
 597-684 1.25e-05

adenylate kinase


Pssm-ID: 178279 [Multi-domain]  Cd Length: 244  Bit Score: 48.73  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934685  597 GETMLSANADKTPkaeevkssdsflklttraqLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQ 676
Cdd:PLN02674   63 GDMLRAAVAAKTP-------------------LGIKAKEAMDKGELVSDDLVVGIIDEAMKKPSCQKGFILDGFPRTVVQ 123


                  ....*...
gi 767934685  677 AQLLEEAL 684
Cdd:PLN02674  124 AQKLDEML 131
ADK pfam00406
Adenylate kinase;
628-685 1.75e-05

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 47.30  E-value: 1.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767934685   628 QLGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALT 685
Cdd:pfam00406   40 ELGKEAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFLLDGFPRTVPQAEALEELLE 97
PRK14526 PRK14526
adenylate kinase; Provisional
 629-684 2.77e-05

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 47.54  E-value: 2.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 684
Cdd:PRK14526   45 LGKEIKQIVENGQLVPDSITIKIVEDKINTIKNNDNFILDGFPRNINQAKALDKFL 100
PRK14528 PRK14528
adenylate kinase; Provisional
 629-694 1.88e-03

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 41.54  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEALTGCNRNLTEV 694
Cdd:PRK14528   46 MGIEAKRYMDAGDLVPDSVVIGIIKDRIREADCKNGFLLDGFPRTVEQADALDALLKNEGKSIDKA 111
AAA_17 pfam13207
AAA domain;
630-684 2.46e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 40.30  E-value: 2.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767934685   630 GAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 684
Cdd:pfam13207   39 LVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIVDGHPRIKTPAGYLPGLP 93
PRK13808 PRK13808
adenylate kinase; Provisional
 629-684 7.08e-03

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 41.03  E-value: 7.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767934685  629 LGAKSEQLLKKGKSIPDVLLVDIIVNAINEIPVNQDCILDGFPMTLNQAQLLEEAL 684
Cdd:PRK13808   45 VGLKAKDIMASGGLVPDEVVVGIISDRIEQPDAANGFILDGFPRTVPQAEALDALL 100
 
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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