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Conserved domains on  [gi|1907161075|ref|XP_036020782|]
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mismatch repair endonuclease PMS2 isoform X11 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
1-80 9.86e-22

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 95.41  E-value: 9.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161075   1 MNGFGTHTWflkriPNSqyplrNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 80
Cdd:COG4642   182 RHGQGTLTY-----ANG-----DVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKR 251
vATP-synt_E super family cl23750
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 523-570 8.00e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


The actual alignment was detected with superfamily member pfam01991:

Pssm-ID: 419987 [Multi-domain]  Cd Length: 199  Bit Score: 41.21  E-value: 8.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161075 523 AYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNIL--REE-------EARKQ 570
Cdd:pfam01991  28 LVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLeaREEildevfnEAEKK 84
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1-80 9.86e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 95.41  E-value: 9.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161075   1 MNGFGTHTWflkriPNSqyplrNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 80
Cdd:COG4642   182 RHGQGTLTY-----ANG-----DVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKR 251
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 12-80 1.23e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 57.92  E-value: 1.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161075  12 KRIPNSQYplrneYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 80
Cdd:PLN03185    3 LVLSNGDF-----YSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYM 66
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 25-47 4.43e-06

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 43.17  E-value: 4.43e-06
                          10        20
                  ....*....|....*....|...
gi 1907161075  25 YIGEFVNGFRHGQGKFYYASGAM 47
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
23-43 6.54e-05

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.02  E-value: 6.54e-05
                           10        20
                   ....*....|....*....|.
gi 1907161075   23 NEYIGEFVNGFRHGQGKFYYA 43
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYA 21
vATP-synt_E pfam01991
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 523-570 8.00e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


Pssm-ID: 396537 [Multi-domain]  Cd Length: 199  Bit Score: 41.21  E-value: 8.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161075 523 AYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNIL--REE-------EARKQ 570
Cdd:pfam01991  28 LVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLeaREEildevfnEAEKK 84
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 525-565 9.14e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 9.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907161075 525 KREEMLKEKVKENQLQEAELaQQRQIENEELEARLNILREE 565
Cdd:cd22887    29 DLEEELKEKNKANEILNDEL-IALQIENNLLEEKLRKLQEE 68
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1-80 9.86e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 95.41  E-value: 9.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161075   1 MNGFGTHTWflkriPNSqyplrNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 80
Cdd:COG4642   182 RHGQGTLTY-----ANG-----DVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKR 251
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1-78 4.35e-20

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 90.40  E-value: 4.35e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907161075   1 MNGFGTHTWflkriPNsqyplRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSND 78
Cdd:COG4642   159 PHGQGTLTY-----AD-----GDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNG 226
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
2-79 4.92e-20

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 90.40  E-value: 4.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161075   2 NGFGTHTWFLKRIPNSQ----YPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSN 77
Cdd:COG4642   123 DGGGYGGGTADGGRGGGgiytFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKN 202


                  ..
gi 1907161075  78 DH 79
Cdd:COG4642   203 GQ 204
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1-77 5.16e-20

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 90.40  E-value: 5.16e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161075   1 MNGFGTHTWflkriPNSQYplrneYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSN 77
Cdd:COG4642   205 RHGQGTYTY-----ADGDR-----YEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTMTYADGSVYEGEWKN 271
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
18-78 1.16e-12

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 68.44  E-value: 1.16e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907161075  18 QYPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSND 78
Cdd:COG4642   120 EGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNG 180
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 12-80 1.23e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 57.92  E-value: 1.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161075  12 KRIPNSQYplrneYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDHI 80
Cdd:PLN03185    3 LVLSNGDF-----YSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYM 66
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 18-73 1.63e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 57.54  E-value: 1.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907161075  18 QYPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEG 73
Cdd:PLN03185   50 SWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEG 105
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1-73 4.30e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 49.83  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161075   1 MNGFGTHT----------WFLKR---IPNSQYPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKN 67
Cdd:PLN03185   66 MHGSGTYTgtdgttykgrWRLNLkhgLGYQRYPNGDVFEGSWIQGLQEGPGKYTWANGNVYLGDMKGGKMSGKGTLTWVS 145


                  ....*.
gi 1907161075  68 GHVYEG 73
Cdd:PLN03185  146 GDSYEG 151
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 25-47 4.43e-06

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 43.17  E-value: 4.43e-06
                          10        20
                  ....*....|....*....|...
gi 1907161075  25 YIGEFVNGFRHGQGKFYYASGAM 47
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
24-78 3.08e-05

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 44.67  E-value: 3.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161075  24 EYIGEFVNGFRHGQGKFYYASGAM-YEGEWASNKKQGRGRMTFKNGHV-YEGLFSND 78
Cdd:COG2849    80 KSEGTYKNGKLEGEWKEYYENGKLkSEGNYKNGKLHGEWKEYYENGKLkEEGNYKNG 136
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 3-132 5.26e-05

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 46.36  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907161075   3 GFGTHTWflkripnsqyPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFS---NDH 79
Cdd:PLN03185  114 GPGKYTW----------ANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTrglKDG 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907161075  80 IAQFF-------ETEMDYSQSLDRWSDASQRSRQPRGSSV-----------SAVREPETLRKLDGSESRSV 132
Cdd:PLN03185  184 KGVFYpagsrvpAVQEFYLNALRKRGVLPDLRRQNQVLSShnseqlsrgvsSDKLSKGSLLPLEQSRNRNV 254
YwqK COG2849
Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];
24-78 6.27e-05

Antitoxin component YwqK of the YwqJK toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 442097 [Multi-domain]  Cd Length: 163  Bit Score: 43.90  E-value: 6.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161075  24 EYIGEFVNGFRHGQGKFYYASGA-MYEGEWASNKKQGRGRMTFKNGH-VYEGLFSND 78
Cdd:COG2849   104 KSEGNYKNGKLHGEWKEYYENGKlKEEGNYKNGKKDGVWKYYDENGKlVKEEEYKNG 160
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
23-43 6.54e-05

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 40.02  E-value: 6.54e-05
                           10        20
                   ....*....|....*....|.
gi 1907161075   23 NEYIGEFVNGFRHGQGKFYYA 43
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYA 21
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
1-79 8.62e-05

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 44.56  E-value: 8.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907161075   1 MNGFGTHTWFLKRIPNSQYPLRNEYIGEFVNGFRHGQGKFYYASGAMYEGEWASNKKQGRGRMTFKNGHVYEGLFSNDH 79
Cdd:COG4642    80 GGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGK 158
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
46-67 6.41e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.32  E-value: 6.41e-04
                           10        20
                   ....*....|....*....|..
gi 1907161075   46 AMYEGEWASNKKQGRGRMTFKN 67
Cdd:smart00698   1 DRYEGEWRNGKRHGRGVYTYAN 22
vATP-synt_E pfam01991
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
 523-570 8.00e-04

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


Pssm-ID: 396537 [Multi-domain]  Cd Length: 199  Bit Score: 41.21  E-value: 8.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907161075 523 AYKREEMLKEKVKENQLQEAELAQQRQIENEELEARLNIL--REE-------EARKQ 570
Cdd:pfam01991  28 LVQEAEEKIDEIYEKKEKQAEMQKKIIISNAKNEARLKVLeaREEildevfnEAEKK 84
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 48-70 8.36e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 37.00  E-value: 8.36e-04
                          10        20
                  ....*....|....*....|...
gi 1907161075  48 YEGEWASNKKQGRGRMTFKNGHV 70
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 525-565 9.14e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 9.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907161075 525 KREEMLKEKVKENQLQEAELaQQRQIENEELEARLNILREE 565
Cdd:cd22887    29 DLEEELKEKNKANEILNDEL-IALQIENNLLEEKLRKLQEE 68
 
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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