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Conserved domains on  [gi|767902101|ref|XP_011538875|]
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deubiquitinase MYSM1 isoform X2 [Homo sapiens]

Protein Classification

SWIRM and MPN_2A_DUB domain-containing protein( domain architecture ID 11088987)

protein containing domains SANT, SWIRM, and MPN_2A_DUB

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 504-686 1.65e-97

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


:

Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 299.95  E-value: 1.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 504 KQEPFQVKVASEALLIMDLHAHVSMAEVIGLLGGRYSEVDKVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFS 583
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSETEIRESLESRGLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 584 VIGWYHSHPAFDPNPSLRDIDTQAKYQSYFS---RGGAKFIGMIVSPYNRNNPLPYSQITCLVISEEISP-DGSYRLPYK 659
Cdd:cd08067   81 VVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKgsdSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENrPNEYGVPML 160

                        170       180
                 ....*....|....*....|....*..
gi 767902101 660 FEVQQMLEEPQWGLVFEKTRWIIEKYR 686
Cdd:cd08067  161 MSYTVSQDEFLTQDVLKELRWLVEFYR 187
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 315-394 5.47e-22

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


:

Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 90.31  E-value: 5.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101  315 DRNIIQEEEKQAIPEFFEGRQaKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLknCGDVNCIGRIHTYLELIGAINF 394
Cdd:pfam04433   2 DPDKLHPIEKRLLPEFFNGKS-KTPEVYLEIRNFILNLWRENPKEYLTKTDARRAL--KGDVNLISRIHEFLERWGLINF 78
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 52-96 8.53e-11

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


:

Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 57.51  E-value: 8.53e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767902101   52 VKWTIEEKELFEQGLAKFGRRWTKISKLIGSRTVLQVKSYARQYF 96
Cdd:pfam00249   2 GPWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
 
Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 504-686 1.65e-97

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 299.95  E-value: 1.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 504 KQEPFQVKVASEALLIMDLHAHVSMAEVIGLLGGRYSEVDKVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFS 583
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSETEIRESLESRGLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 584 VIGWYHSHPAFDPNPSLRDIDTQAKYQSYFS---RGGAKFIGMIVSPYNRNNPLPYSQITCLVISEEISP-DGSYRLPYK 659
Cdd:cd08067   81 VVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKgsdSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENrPNEYGVPML 160

                        170       180
                 ....*....|....*....|....*..
gi 767902101 660 FEVQQMLEEPQWGLVFEKTRWIIEKYR 686
Cdd:cd08067  161 MSYTVSQDEFLTQDVLKELRWLVEFYR 187
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 315-394 5.47e-22

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 90.31  E-value: 5.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101  315 DRNIIQEEEKQAIPEFFEGRQaKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLknCGDVNCIGRIHTYLELIGAINF 394
Cdd:pfam04433   2 DPDKLHPIEKRLLPEFFNGKS-KTPEVYLEIRNFILNLWRENPKEYLTKTDARRAL--KGDVNLISRIHEFLERWGLINF 78
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 52-96 8.53e-11

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 57.51  E-value: 8.53e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767902101   52 VKWTIEEKELFEQGLAKFGRRWTKISKLIGSRTVLQVKSYARQYF 96
Cdd:pfam00249   2 GPWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 509-636 4.60e-09

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 55.46  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101   509 QVKVASEALLIMDLHAhVSM--AEVIGLLGGrYSEVD--KVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFSV 584
Cdd:smart00232   1 EVKVHPLVPLNILKHA-IRDgpEEVCGVLLG-KSNKDrpEVKEVFAVPNEPQDDSVQEYDEDYSHLMDEELKKVNKDLEI 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767902101   585 IGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAKFIGMIVSPYNRNNPLPY 636
Cdd:smart00232  79 VGWYHSHPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLRAF 130
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 53-96 9.68e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 51.42  E-value: 9.68e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767902101  53 KWTIEEKELFEQGLAKFG-RRWTKISKLIGSRTVLQVKSYARQYF 96
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGkNNWEKIAKELPGRTPKQCRERWRNLL 45
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 530-609 1.10e-08

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 54.15  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 530 EVIGLLGGRYSEVDKVVEVcaaEPCNSLSTGLQC--EMDPVSQTQASETLAVRGFSVIGWYHSHPAFDPNPSLRDIDtQA 607
Cdd:COG1310   23 ECCGLLLGKGGGDKRVTRV---YPARNVAESPETrfEIDPEDLLAAEREARERGLEIVGIYHSHPDGPAYPSETDRA-QA 98


                 ..
gi 767902101 608 KY 609
Cdd:COG1310   99 AW 100
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
53-97 2.80e-08

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 50.30  E-value: 2.80e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767902101    53 KWTIEEKELFEQGLAKFG-RRWTKISKLIGSRTVLQVKSYARQYFK 97
Cdd:smart00717   3 EWTEEEDELLIELVKKYGkNNWEKIAKELPGRTAEQCRERWRNLLK 48
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 308-409 2.34e-07

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 54.12  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 308 PEQEIEIDRNIIQEEEKQAIPEFFEGRQ-AKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLknCGDVNCIGRIHTYL 386
Cdd:COG5259   55 PSYAEWFDGSKIHEIEKRSNPEFFNGRSpSKTPEVYKDYRNFMINSYRLNPNEYLTVTACRRNV--AGDVAAIVRVHRFL 132

                         90       100
                 ....*....|....*....|...
gi 767902101 387 ELIGAINFGCEQAVynRPQTVDK 409
Cdd:COG5259  133 EKWGLINYQVDPGT--RPSTIGP 153
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 509-612 2.36e-07

JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain and PAD-1-like domain, JABP1 domain or JAMM domain. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates.


Pssm-ID: 396120  Cd Length: 117  Bit Score: 50.04  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101  509 QVKVASEALL-IMDLHAHV--SMAEVIGLLGGRYSEvDKVVEV--CAAEPCNSLSTglQCEMDPVSQ---TQASETL--A 578
Cdd:pfam01398   5 TVIIHPLVLLkILDHANRGgkIGEEVMGVLLGKLEG-DGTIEItnSFALPQEETED--DVNAVALDQeymENMHEMLkkV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767902101  579 VRGFSVIGWYHSHPAFdPNPSLRDIDTQAKYQSY 612
Cdd:pfam01398  82 NRKEEVVGWYHTHPGL-CWLSSVDVHTHALYQRM 114
 
Name Accession Description Interval E-value
MPN_2A_DUB cd08067
Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A ...
 504-686 1.65e-97

Mov34/MPN/PAD-1 family: Histone H2A deubiquitinase; This family includes histone H2A deubiquitinase (Histone H2A DUB;MYSM1; myb-like, SWIRM and MPN domains 1; 2ADUB; 2A-DUB; KIAA19152ADUB, or KIAA1915/MYSM1), a member of JAMM/MPN+ deubiquitinases (DUBs), with possible Zn2+-dependent ubiquitin isopeptidase activity. It contains the SWIRM (Swi3p, Rsc8p and Moira), and SANT (SWI-SNF, ADA N-CoR, TFIIIB)/Myb domains; the SANT, but not the SWIRM, domain can bind directly to DNA. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. 2A-DUB interacts with p/CAF (p300/CBP-associated factor) in a co-regulatory protein complex, where the status of acetylation of nucleosomal histones modulates its deubiquitinase activity. 2A-DUB is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene; it participates in transcriptional regulation events in androgen receptor-dependent gene activation. In prostate tumors, the levels of uH2A are dramatically decreased, thus 2A-DUB serving as a cancer-related marker.


Pssm-ID: 163698 [Multi-domain]  Cd Length: 187  Bit Score: 299.95  E-value: 1.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 504 KQEPFQVKVASEALLIMDLHAHVSMAEVIGLLGGRYSEVDKVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFS 583
Cdd:cd08067    1 KIQPFKVTVSSNALLLMDFHCHLTTSEVIGYLGGTWDPNTQNLTILQAFPCRSRLTGLDCEMDPVSETEIRESLESRGLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 584 VIGWYHSHPAFDPNPSLRDIDTQAKYQSYFS---RGGAKFIGMIVSPYNRNNPLPYSQITCLVISEEISP-DGSYRLPYK 659
Cdd:cd08067   81 VVGWYHSHPTFPPNPSLRDIDTQLDYQIMFKgsdSGYEPCVGLICSPYDRRNSTPESQITCFWVMPPPENrPNEYGVPML 160

                        170       180
                 ....*....|....*....|....*..
gi 767902101 660 FEVQQMLEEPQWGLVFEKTRWIIEKYR 686
Cdd:cd08067  161 MSYTVSQDEFLTQDVLKELRWLVEFYR 187
MPN_euk_mb cd08058
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 515-640 1.41e-50

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); eukaryotic; This family contains eukaryotic MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains found in proteins with a variety of functions, including AMSH (associated molecule with the Src homology 3 domain (SH3) of STAM), H2A-DUB (histone H2A deubiquitinase), BRCC36 (BRCA1/BRCA2-containing complex subunit 36), as well as Rpn11 (regulatory particle number 11) and CSN5 (COP9 signalosome complex subunit 5). These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology. CSN5 is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Over-expression of CSN5 has been implicated in cancer initiation and progression. AMSH specifically cleaves Lys 63 and not Lys48-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. It is involved in the degradation of EGF receptor (EGFR) and possibly other ubiquitinated endocytosed proteins. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity; it is targeted to DNA damage foci after irradiation. 2A-DUB is specific for monoubiquitinated H2A (uH2A), regulating transcription by coordinating histone acetylation and deubiquitination, and destabilizing the association of linker histone H1 with nucleosomes. It is a positive regulator of androgen receptor (AR) transactivation activity on a reporter gene and serves as a marker in prostate tumors.


Pssm-ID: 163689  Cd Length: 119  Bit Score: 172.38  E-value: 1.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 515 EALLIMDLHAHVS-MAEVIGLLGGRYSE---VDKVVEVCAAEPCNSLSTGLQcemdpvsQTQASETLAVRGFSVIGWYHS 590
Cdd:cd08058    1 DALLKMLQHAESNtGIEVMGLLCGELTHnefTDKHVIVPKQSAGPDSCTGEN-------VEELFNVQTGRPLLVVGWYHS 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767902101 591 HPAFDPNPSLRDIDTQAKYQSYfsrgGAKFIGMIVSPYNRNNPLPYSQIT 640
Cdd:cd08058   74 HPTFTAWLSSVDIHTQASYQLM----LPEAIAIVVSPKHRNKDTGIFRLT 119
SWIRM pfam04433
SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid ...
 315-394 5.47e-22

SWIRM domain; This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA.


Pssm-ID: 461307 [Multi-domain]  Cd Length: 78  Bit Score: 90.31  E-value: 5.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101  315 DRNIIQEEEKQAIPEFFEGRQaKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLknCGDVNCIGRIHTYLELIGAINF 394
Cdd:pfam04433   2 DPDKLHPIEKRLLPEFFNGKS-KTPEVYLEIRNFILNLWRENPKEYLTKTDARRAL--KGDVNLISRIHEFLERWGLINF 78
MPN_BRCC36 cd08068
Mov34/MPN/PAD-1 family: BRCC36, a subunit of BRCA1-A complex; BRCC36 (BRCA1-A complex subunit ...
 510-664 6.68e-11

Mov34/MPN/PAD-1 family: BRCC36, a subunit of BRCA1-A complex; BRCC36 (BRCA1-A complex subunit BRCC36; BRCA1/BRCA2-containing complex subunit 36; BRCA1/BRCA2-containing complex subunit 3; BRCC3; BRISC complex subunit BRCC36; BRCC36 isopeptidase complex; Lys-63-specific deubiquitinase BRCC36) and BRCC36-like domains are members of JAMM/MPN+ deubiquitinases (DUBs), possibly with Zn2+-dependent ubiquitin isopeptidase activity. BRCC36 is part of the BRCA1/BRCA2/BARD1-containing nuclear complex that displays an E3 ubiquitin ligase activity. It is targeted to DNA damage foci after irradiation; RAP80 recruits the Abraxas-BRCC36-BRCA1-BARD1 complex to DNA double strand breaks (DSBs) for DNA repair through specific recognition of Lys 63-linked polyubiquitinated proteins by its tandem ubiquitin-interacting motifs. A new protein, MERIT40 (mediator of RAP80 interactions and targeting 40 kDa), also named NBA1 (new component of the BRCA1 A complex), exists in the same BRCA1-containing complex and is essential for the integrity of the complex. There are studies suggesting that MERIT40/NBA1 ties BRCA1 complex integrity, DSB recognition, and ubiquitin chain activities to the DNA damage response. It has also been shown that BRCA1-containing complex resembles the lid complex of the 26S proteasome.


Pssm-ID: 163699 [Multi-domain]  Cd Length: 244  Bit Score: 63.14  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 510 VKVASEALLIMDLHAH-VSMAEVIGLLGGrysevDKVVEVCAAEPCNSLSTGLQ-----------CEMDP---VSQTQAS 574
Cdd:cd08068    4 VHLSADVYLVCLTHALsTEKEEVMGLLIG-----EIEVSKKGEEVAIVHISAVIilrrsdkrkdrVEISPeqlSAASTEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 575 ETLAV---RGFSVIGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRggakFIGMIVSPYNRNNPLPYS--QITCLViSEEIS 649
Cdd:cd08068   79 ERLTEetgRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDSG----FVGLIFSCFNEDKSTKMGevQVTCFQ-SVQGN 153

                        170
                 ....*....|....*.
gi 767902101 650 PDGSY-RLPYKFEVQQ 664
Cdd:cd08068  154 KAGQYeRIEVPLEIVP 169
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 52-96 8.53e-11

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 57.51  E-value: 8.53e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767902101   52 VKWTIEEKELFEQGLAKFGRRWTKISKLIGSRTVLQVKSYARQYF 96
Cdd:pfam00249   2 GPWTPEEDELLLEAVEKLGNRWKKIAKLLPGRTDNQCKNRWQNYL 46
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 530-634 6.51e-10

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); This family contains archaeal and bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163701  Cd Length: 128  Bit Score: 57.65  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 530 EVIGLLGGRYSEVDKVVEvcAAEPC-NSLSTGLQC-EMDPVSQTQASETLAVRGFSVIGWYHSHPAFDPNPSLRDIDtQA 607
Cdd:cd08070   18 ECCGLLLGKGGGVTAIVT--EVYPVrNVAESPRRRfEIDPAEQLAAQREARERGLEVVGIYHSHPDGPARPSETDLR-LA 94

                         90       100
                 ....*....|....*....|....*....
gi 767902101 608 KY--QSYfsrggakfigMIVSPYNRNNPL 634
Cdd:cd08070   95 WPpgVSY----------LIVSLAGGAPEL 113
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 509-636 4.60e-09

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 55.46  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101   509 QVKVASEALLIMDLHAhVSM--AEVIGLLGGrYSEVD--KVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFSV 584
Cdd:smart00232   1 EVKVHPLVPLNILKHA-IRDgpEEVCGVLLG-KSNKDrpEVKEVFAVPNEPQDDSVQEYDEDYSHLMDEELKKVNKDLEI 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767902101   585 IGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAKFIGMIVSPYNRNNPLPY 636
Cdd:smart00232  79 VGWYHSHPDESPFPSEVDVATHESYQAPWPISVVLIVDPIKSFQGRLSLRAF 130
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 53-96 9.68e-09

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 51.42  E-value: 9.68e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767902101  53 KWTIEEKELFEQGLAKFG-RRWTKISKLIGSRTVLQVKSYARQYF 96
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGkNNWEKIAKELPGRTPKQCRERWRNLL 45
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 530-609 1.10e-08

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 54.15  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 530 EVIGLLGGRYSEVDKVVEVcaaEPCNSLSTGLQC--EMDPVSQTQASETLAVRGFSVIGWYHSHPAFDPNPSLRDIDtQA 607
Cdd:COG1310   23 ECCGLLLGKGGGDKRVTRV---YPARNVAESPETrfEIDPEDLLAAEREARERGLEIVGIYHSHPDGPAYPSETDRA-QA 98


                 ..
gi 767902101 608 KY 609
Cdd:COG1310   99 AW 100
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
53-97 2.80e-08

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 50.30  E-value: 2.80e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767902101    53 KWTIEEKELFEQGLAKFG-RRWTKISKLIGSRTVLQVKSYARQYFK 97
Cdd:smart00717   3 EWTEEEDELLIELVKKYGkNNWEKIAKELPGRTAEQCRERWRNLLK 48
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
 308-409 2.34e-07

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 54.12  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 308 PEQEIEIDRNIIQEEEKQAIPEFFEGRQ-AKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLknCGDVNCIGRIHTYL 386
Cdd:COG5259   55 PSYAEWFDGSKIHEIEKRSNPEFFNGRSpSKTPEVYKDYRNFMINSYRLNPNEYLTVTACRRNV--AGDVAAIVRVHRFL 132

                         90       100
                 ....*....|....*....|...
gi 767902101 387 ELIGAINFGCEQAVynRPQTVDK 409
Cdd:COG5259  133 EKWGLINYQVDPGT--RPSTIGP 153
JAB pfam01398
JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome ...
 509-612 2.36e-07

JAB1/Mov34/MPN/PAD-1 ubiquitin protease; Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain and PAD-1-like domain, JABP1 domain or JAMM domain. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates.


Pssm-ID: 396120  Cd Length: 117  Bit Score: 50.04  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101  509 QVKVASEALL-IMDLHAHV--SMAEVIGLLGGRYSEvDKVVEV--CAAEPCNSLSTglQCEMDPVSQ---TQASETL--A 578
Cdd:pfam01398   5 TVIIHPLVLLkILDHANRGgkIGEEVMGVLLGKLEG-DGTIEItnSFALPQEETED--DVNAVALDQeymENMHEMLkkV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767902101  579 VRGFSVIGWYHSHPAFdPNPSLRDIDTQAKYQSY 612
Cdd:pfam01398  82 NRKEEVVGWYHTHPGL-CWLSSVDVHTHALYQRM 114
MPN_RPN11_CSN5 cd08069
Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit ...
 509-612 3.17e-07

Mov34/MPN/PAD-1 family: proteasomal regulatory protein Rpn11 and signalosome complex subunit CSN5; This family contains proteasomal regulatory protein Rpn11 (26S proteasome regulatory subunit rpn11; PAD1; POH1; RPN11; PSMD14; Rpn11 subunit of the 19S-proteasome; regulatory particle number 11) and signalosomal CSN5 (COP9 signalosome complex subunit 5; COP9 complex homolog subunit 5; c-Jun activation domain-binding protein-1; CSN5/JAB1; JAB1). COP9 signalosome (CSN) and the proteasome lid are paralogous complexes and their respective subunits CSN5 and Rpn11 are most closely related between the two complexes, both containing the conserved JAMM (JAB1/MPN/Mov34 metalloenzyme) motif involved in zinc ion coordination and providing the active site for isopeptidase activity. Rpn11 is responsible for substrate deubiquitination during proteasomal degradation. It is essential for maintaining a correct cell cycle and normal mitochondrial morphology and physiology; mutations in Rpn11 cause cell cycle and mitochondrial defects, temperature sensitivity and sensitivity to DNA damaging reagents such as UV. It has been shown that the C-terminal region of Rpn11 is involved in the regulation of the mitochondrial fission and tubulation processes. CSN5, one of the eight subunits of CSN, is critical for nuclear export and the degradation of several tumor suppressor proteins, including p53, p27, and Smad4. Its MPN+ domain is critical for the physical interaction of RUNX3 and Jab1. It has been suggested that the direct interaction of CSN5/JAB1 with p27 provides p27 with a leucine-rich nuclear export signal (NES), which is required for binding to chromosomal region maintenance 1 (CRM1), and facilitates nuclear export. The over-expression of CSN5/JAB1 also has been implicated in cancer initiation and progression, including cancer of the lung, pancreas, mouth, thyroid, and breast, suggesting that the oncogenic activity of CSN5 is associated with the down-regulation of RUNX3.


Pssm-ID: 163700 [Multi-domain]  Cd Length: 268  Bit Score: 52.64  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 509 QVKVASEALLIMDLHAH--VSMaEVIGLLGGRyseVDK---VVEVCAAEPcnSLSTGLQCEMDPVSQTQASETLAV---- 579
Cdd:cd08069   11 KVYISSLALLKMLKHARagGPI-EVMGLMLGK---VDDytiIVVDVFALP--VEGTETRVNAQDEFQEYMVQYEMLkqtg 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767902101 580 RGFSVIGWYHSHPAFDPNPSLRDIDTQAKYQSY 612
Cdd:cd08069   85 RPENVVGWYHSHPGYGCWLSGIDVNTQQLNQQL 117
MPN cd07767
Mpr1p, Pad1p N-terminal (MPN) domains; MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) ...
 518-634 1.71e-06

Mpr1p, Pad1p N-terminal (MPN) domains; MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+) domains are found in the N-terminal termini of proteins with a variety of functions; they are components of the proteasome regulatory subunits, the signalosome (CSN), eukaryotic translation initiation factor 3 (eIF3) complexes, and regulators of transcription factors. These domains are isopeptidases that release ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. Catalytically active MPN domains contain a metalloprotease signature known as the JAB1/MPN/Mov34 metalloenzyme (JAMM) motif. For example, Rpn11 (also known as POH1 or PSMD14), a subunit of the 19S proteasome lid is involved in the ATP-dependent degradation of ubiquitinated proteins, contains the conserved JAMM motif involved in zinc ion coordination. Poh1 is a regulator of c-Jun, an important regulator of cell proliferation, differentiation, survival and death. JAB1 is a component of the COP9 signalosome (CSN), a regulatory particle of the ubiquitin (Ub)/26S proteasome system occurring in all eukaryotic cells; it cleaves the ubiquitin-like protein NEDD8 from the cullin subunit of the SCF (Skp1, Cullins, F-box proteins) family of E3 ubiquitin ligases. AMSH (associated molecule with the SH3 domain of STAM, also known as STAMBP), a member of JAMM/MPN+ deubiquitinases (DUBs), specifically cleaves Lys 63-linked polyubiquitin (poly-Ub) chains, thus facilitating the recycling and subsequent trafficking of receptors to the cell surface. Similarly, BRCC36, part of the nuclear complex that includes BRCA1 protein and is targeted to DNA damage foci after irradiation, specifically disassembles K63-linked polyUb. BRCC36 is aberrantly expressed in sporadic breast tumors, indicative of a potential role in the pathogenesis of the disease. Some variants of the JAB1/MPN domains lack key residues in their JAMM motif and are unable to coordinate a metal ion. Comparisons of key catalytic and metal binding residues explain why the MPN-containing proteins Mov34/PSMD7, Rpn8, CSN6, Prp8p, and the translation initiation factor 3 subunits f (p47) and h (p40) do not show catalytic isopeptidase activity. It has been proposed that the MPN domain in these proteins has a primarily structural function.


Pssm-ID: 163686 [Multi-domain]  Cd Length: 116  Bit Score: 47.51  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 518 LIMDLHAHVSMA--EVIGLLGGRYSEVDKVVEVCAAEPcnsLSTGLQcEMDPVSQTQASETLAVRGFSVIGWYHSHPAFD 595
Cdd:cd07767    1 LKMFLDAAKSINgkEVIGLLYGSKTKKVLDVDEVIAVP---FDEGDK-DDNVWFLMYLDFKKLNAGLRIVGWYHTHPKPS 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767902101 596 PNPSLRDIDTQAKYQSYFsrGGAKFIGMIVSPYNRNNPL 634
Cdd:cd07767   77 CFLSPNDLATHELFQRYF--PEKVMIIVDVKPKDLGNSW 113
MPN_archaeal cd08072
Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only ...
 530-632 4.34e-05

Mov34/MPN/PAD-1 family: archaeal JAB1/MPN/Mov34 metalloenzyme; This family contains only archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163703  Cd Length: 117  Bit Score: 43.40  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101 530 EVIGLLGGRYSEVDKVVEVCAAEpCNSLSTGLQCEMDPVsqtqasetlavrGFSVIGWYHSHPAFDPNPSLRDIdtqaky 609
Cdd:cd08072   20 EFAALLRGKDGVITELLILPGTE-SGEVSAVFPLLMLPL------------DMSIVGSVHSHPSGSPRPSDADL------ 80

                         90       100
                 ....*....|....*....|....
gi 767902101 610 qSYFSRGGAkfIGMIVS-PYNRNN 632
Cdd:cd08072   81 -SFFSKTGL--VHIIVGyPYDEDD 101
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 522-604 8.09e-05

Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism.


Pssm-ID: 464179  Cd Length: 113  Bit Score: 42.49  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767902101  522 LHAHVSMA---EVIGLLGGRYSEvDKVVEVCAAEPCNSLSTglqcEMDPVSQTQASETLAVRGFSVIGWYHSHPAFDPNP 598
Cdd:pfam14464   8 IVAHARAAhplECCGILLGNELE-SQSVRVIPLVNPMRNRF----EIDPGDSLRRVKAARERGLELVGIYHSHPGGPAYP 82


                  ....*.
gi 767902101  599 SLRDID 604
Cdd:pfam14464  83 SETDRR 88
SANT_TRF cd11660
Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human ...
 52-89 5.63e-04

Telomere repeat binding factor-like DNA-binding domains of the SANT/myb-like family; Human telomere repeat binding factors, TRF1 and TRF2, function as part of the 6 component shelterin complex. TRF2 binds DNA and recruits RAP1 (via binding to the RAP1 protein c-terminal (RCT)) and TIN2 in the protection of telomeres from DNA repair machinery. Metazoan shelterin consists of 3 DNA binding proteins (TRF2, TRF1, and POT1) and 3 recruited proteins that bind to one or more of these DNA-binding proteins (RAP1, TIN2, TPP1). Schizosaccharomyces pombe TAZ1 is an orthlog and binds RAP1. Human TRF1 and TRF2 bind double-stranded DNA. hTRF2 consists of a basic N-terminus, a TRF homology domain, the RAP1 binding motif (RBM), the TIN2 binding motif (TBM) and a myb-like DNA binding domain, SANT, named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. Tandem copies of the domain bind telomeric DNA tandem repeats as part of the capping complex. The single myb-like domain of TRF-type proteins is similar to the tandem myb_like domains found in yeast RAP1.


Pssm-ID: 212558 [Multi-domain]  Cd Length: 50  Bit Score: 38.32  E-value: 5.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767902101  52 VKWTIEEKELFEQGLAKFGR-RWTKI---SKLIGSRTVLQVK 89
Cdd:cd11660    1 RKWTDEEDEALVEGVEKYGVgNWAKIlkdYFFVNNRTSVDLK 42
Myb_DNA-bind_6 pfam13921
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 54-101 5.34e-03

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 372817 [Multi-domain]  Cd Length: 60  Bit Score: 35.75  E-value: 5.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767902101   54 WTIEEKELFEQGLAKFGRRWTKISKLIGSRTVLQVksyaRQYFKNKVK 101
Cdd:pfam13921   1 WTEEEDEKLLKLVEKYGNDWKQIAKELGRRTPKQC----FDRWRRKLN 44
 
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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