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Conserved domains on  [gi|2024378751|ref|XP_040506979|]
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ankyrin repeat domain-containing protein 60 isoform X6 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 13-85 3.69e-38

ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins; ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


:

Pssm-ID: 340583  Cd Length: 77  Bit Score: 126.24  E-value: 3.69e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024378751  13 IQLRLAETNEIFSLPQCQNDLTLKQLKSDLELLTGIPFHFQRLHYLDEIDLPDDSTFMDNDIVPGGTITMRIW 85
Cdd:cd17063     5 LKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-189 2.89e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 2.89e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELL 189
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
 
Name Accession Description Interval E-value
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 13-85 3.69e-38

ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins; ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340583  Cd Length: 77  Bit Score: 126.24  E-value: 3.69e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024378751  13 IQLRLAETNEIFSLPQCQNDLTLKQLKSDLELLTGIPFHFQRLHYLDEIDLPDDSTFMDNDIVPGGTITMRIW 85
Cdd:cd17063     5 LKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-189 2.89e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 2.89e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELL 189
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
141-190 3.24e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 141 LFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELLM 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 141-190 2.74e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 2.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024378751 141 LFVASHRGHVNTVKFLL-SHGADVRSKTPLGRTALHVAAVMGRCECIELLM 190
Cdd:cd22192    21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM 71
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-190 5.05e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024378751 104 KLVQLGVTEEYAGTSPyaKILGPEQK-KEWVAHRAFVALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGR 182
Cdd:PTZ00322   50 HLEALEATENKDATPD--HNLTTEEViDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGH 127


                  ....*...
gi 2024378751 183 CECIELLM 190
Cdd:PTZ00322  128 VQVVRVLL 135
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 32-73 7.83e-04

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 37.12  E-value: 7.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2024378751  32 DLTLKQLKSDLELLTGIPFHFQRLHYLDeidlPDDSTF--MDND 73
Cdd:pfam14560  22 SLTIEELKEKLELITGTPPSSMRLQLYD----DDDNLVakLDDD 61
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 30-82 3.35e-03

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 34.93  E-value: 3.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024378751   30 QNDLTLKQLKSDLELLTGIPFHFQRLhYLDEIDLPDDSTFMDNDIVPGGTITM 82
Cdd:smart00213  18 KPSDTVSELKEKIAELTGIPPEQQRL-IYKGKVLEDDRTLADYGIQDGSTIHL 69
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-163 6.19e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.33  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|....
gi 2024378751  140 ALFVASHRGHVNTVKFLLSHGADV 163
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 13-85 3.69e-38

ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and similar proteins; ANKRD60 is an uncharacterized ankyrin repeat domain-containing protein which also harbors a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions.


Pssm-ID: 340583  Cd Length: 77  Bit Score: 126.24  E-value: 3.69e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024378751  13 IQLRLAETNEIFSLPQCQNDLTLKQLKSDLELLTGIPFHFQRLHYLDEIDLPDDSTFMDNDIVPGGTITMRIW 85
Cdd:cd17063     5 LKLRLPETEETFTVPNCYPGMKVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-189 2.89e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 2.89e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELL 189
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
141-190 3.24e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 141 LFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELLM 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-195 1.51e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 1.51e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELLMgtEAG 195
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL--EAG 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-190 1.81e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 1.81e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHgADVRSKTpLGRTALHVAAVMGRCECIELLM 190
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-189 1.10e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 1.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELL 189
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-189 1.26e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELL 189
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-195 1.28e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 1.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELLMgtEAG 195
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL--EAG 143
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 141-190 2.74e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 2.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024378751 141 LFVASHRGHVNTVKFLL-SHGADVRSKTPLGRTALHVAAVMGRCECIELLM 190
Cdd:cd22192    21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM 71
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 32-83 1.17e-04

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 38.73  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024378751  32 DLTLKQLKSDLELLTGIPFHFQRLHYLDEIdLPDDSTFMDNDIVPGGTITMR 83
Cdd:cd17039    18 DDTVADLKEKIEEKTGIPVEQQRLIYNGKE-LKDDKTLSDYGIKDGSTIHLV 68
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-190 5.05e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024378751 104 KLVQLGVTEEYAGTSPyaKILGPEQK-KEWVAHRAFVALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGR 182
Cdd:PTZ00322   50 HLEALEATENKDATPD--HNLTTEEViDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGH 127


                  ....*...
gi 2024378751 183 CECIELLM 190
Cdd:PTZ00322  128 VQVVRVLL 135
Ubiquitin_2 pfam14560
Ubiquitin-like domain; This entry contains ubiquitin-like domains.
 32-73 7.83e-04

Ubiquitin-like domain; This entry contains ubiquitin-like domains.


Pssm-ID: 405277  Cd Length: 83  Bit Score: 37.12  E-value: 7.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2024378751  32 DLTLKQLKSDLELLTGIPFHFQRLHYLDeidlPDDSTF--MDND 73
Cdd:pfam14560  22 SLTIEELKEKLELITGTPPSSMRLQLYD----DDDNLVakLDDD 61
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 140-188 1.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 1.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAvmgRCECIEL 188
Cdd:PHA03100  111 LYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL---ESNKIDL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 139-179 1.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2024378751 139 VALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAV 179
Cdd:PHA03095  156 LAVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQ 196
Ubl_TBCB cd01789
ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins; ...
 32-73 1.81e-03

ubiquitin-like (Ubl) domain found in tubulin-folding cofactor B (TBCB) and similar proteins; TBCB, also termed cytoskeleton-associated protein 1, or cytoskeleton-associated protein CKAPI, or tubulin-specific chaperone B, is one of protein cofactors A through E that is required for the folding of tubulins prior to their incorporation into microtubules and heterodimer assembly. TBCB comprises an N-terminal ubiquitin-like (Ubl) domain and a C-terminal cytoskeleton-associated protein with glycine-rich segment (CAP-Gly) domain. The Ubl domain of TBCB is essential for proper folding and assembly of tubulin alpha. It has a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. TBC-A through E are necessary for the biogenesis of microtubules and for cell viability.


Pssm-ID: 340487  Cd Length: 80  Bit Score: 36.01  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2024378751  32 DLTLKQLKSDLELLTGIPFHFQRLHYLDEiDLPDDSTFMDND 73
Cdd:cd01789    22 SLTIGELKEKLELITGTPPSSMKLQLYDE-DGKLIGTLDDDD 62
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-191 2.41e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.96  E-value: 2.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024378751 141 LFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVAAVMGRCECIELLMG 191
Cdd:PTZ00322  119 LHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-166 2.53e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 35.86  E-value: 2.53e-03
                          10        20
                  ....*....|....*....|....*..
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSK 166
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVK 90
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
 30-82 3.35e-03

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 34.93  E-value: 3.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024378751   30 QNDLTLKQLKSDLELLTGIPFHFQRLhYLDEIDLPDDSTFMDNDIVPGGTITM 82
Cdd:smart00213  18 KPSDTVSELKEKIAELTGIPPEQQRL-IYKGKVLEDDRTLADYGIQDGSTIHL 69
Ubl2_ANKUB1 cd17051
ubiquitin-like (Ubl) domain 2 found in Ankyrin repeat and ubiquitin domain-containing 1 ...
 32-90 3.75e-03

ubiquitin-like (Ubl) domain 2 found in Ankyrin repeat and ubiquitin domain-containing 1 (ANKUB1) and similar proteins; ANKUB1 is an uncharacterized protein with two tandem ubiquitin-like (Ubl) domains located at the N-terminal of Ankyrin repeats (ANK). The Ubl domain may have an adaptor role in ubiquitin(Ub)-signaling by mediating protein-protein interaction. Ubl proteins have a beta-grasp Ubl fold and attach to other proteins in a Ubl manner with biochemically distinct roles. The ankyrin repeats have been identified in numerous proteins with diverse functions. The family corresponds to the second Ubl domain.


Pssm-ID: 340571  Cd Length: 83  Bit Score: 34.93  E-value: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024378751  32 DLTLKQLKSDLELLTGIPFHFQRLHYLDEIDLPDDSTFMDNDIVPGGTITMRIWkqDGW 90
Cdd:cd17051    27 TTTVSQLRSIISRKTGLPVSVFRLVTPDGTEMYDCNLLDDYGIDIGTTLRLETW--DGW 83
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-176 3.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 37.31  E-value: 3.90e-03
                          10        20
                  ....*....|....*....|....*..
gi 2024378751 150 VNTVKFLLSHGADVRSKTPLGRTALHV 176
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLHV 123
Ubl2_FAT10 cd17053
ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 ...
 19-82 3.93e-03

ubiquitin-like (Ubl) domain 2 found in leukocyte antigen F (HLA-F) adjacent transcript 10 (FAT10) and similar proteins; FAT10, also termed ubiquitin D (UBD), or diubiquitin, is a cytokine-inducible ubiquitin-like (Ubl) modifer that is highly expressed in the thymus, and targets substrates covalently for 26S proteasomal degradation. It is also associated with cancer development, antigen processing and antimicrobial defense, chromosomal stability and cell cycle regulation. FAT10 is presented on immune cells and under the inflammatory conditions, is synergistically induced by interferon gamma (IFNgamma) and tumor necrosis factor (TNFalpha) in the non-immune (liver parenchymal) cells. FAT10 contains two Ubl domains. The family corresponds to the second Ubl domain of FAT10. Some family members contain only one Ubl domain.


Pssm-ID: 340573  Cd Length: 71  Bit Score: 34.63  E-value: 3.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024378751  19 ETNEIFSLpQCQNDLTLKQLKSDLELLTGIPFHFQRLHYlDEIDL-PDDSTFMDNDIVPGGTITM 82
Cdd:cd17053     8 LTGTVHTL-QVSRSTTVAQVKAMIEDQSGVPPNEQILVY-NGKRLeDGDKTLGEYGIKTGDTLYL 70
Ubl_OTU1 cd17059
ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 ...
 11-81 5.03e-03

ubiquitin-like (Ubl) domain found in ubiquitin thioesterase OTU1 and similar proteins; OTU1 (EC 3.4.19.12), also termed YOD1, or DUBA-8, or HIV-1-induced protease 7 (HIN-7), or OTU domain-containing protein 2 (OTUD2), is a p97-associated deubiquitinylase that functions as a key player in endoplasmic reticulum-associated degradation (ERAD). Its deubiquitinylase activity is also required for negatively regulating cholera toxin A1 (CTA1) retro-translocation. OTU1 contains a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a C2H2-type zinc finger, and an OTU domain.


Pssm-ID: 340579  Cd Length: 75  Bit Score: 34.49  E-value: 5.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024378751  11 LKIQLRLAETNEIFSLPQcqNDLTLKQLKSDLELLTGIPFHFQRLHY---LDEIDLPDDSTFMDNDIV-PGGTIT 81
Cdd:cd17059     1 MRLRVRSKGGQHVLSLLT--DTSTVGELQDRIAALTGIPPSSQKILYgfpPKPLDLSDEEASLESLGIqSGDTLI 73
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-163 6.19e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.33  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|....
gi 2024378751  140 ALFVASHRGHVNTVKFLLSHGADV 163
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-177 7.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.47  E-value: 7.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2024378751 140 ALFVASHRGHVNTVKFLLSHGADVRSKTPLGRTALHVA 177
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ubl_UBFD1 cd17047
ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar ...
 32-77 8.97e-03

ubiquitin-like (Ubl) domain found in ubiquitin domain-containing protein UBFD1 and similar proteins; UBFD1, also termed ubiquitin-binding protein homolog (UBPH), is a polyubiquitin binding protein containing a conserved ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. It may play a role as nuclear factor-kappaB (NF-kappaB) regulator.


Pssm-ID: 340567  Cd Length: 70  Bit Score: 33.76  E-value: 8.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2024378751  32 DLTLKQLKSDLELLTGIPFHFQRLHY--LdeidLPDDSTFMDNDIVPG 77
Cdd:cd17047    19 DSTIAELKEHIETLTGVPPAMQKLMYkgL----LKDDKTLRELKVTKG 62
 
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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