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Conserved domains on  [gi|767926668|ref|XP_011511100|]
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protein ANKUB1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl2_ANKUB1 cd17051
ubiquitin-like (Ubl) domain 2 found in Ankyrin repeat and ubiquitin domain-containing 1 ...
 31-113 6.73e-48

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: 160.12  E-value: 6.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668  31 EDKPTLYVFNAVTQDTMPVMESISLLDKTVSDLRTLVTLRCGLPVSVYCLRTPRGLEMYDCNTLKDYQTDIGTTLRLDVW 110
Cdd:cd17051    1 EIKPVLYVYCVFNQETIPIMEKINVLTTTVSQLRSIISRKTGLPVSVFRLVTPDGTEMYDCNLLDDYGIDIGTTLRLETW 80


                 ...
gi 767926668 111 DGW 113
Cdd:cd17051   81 DGW 83
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
 1-30 8.97e-12

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17050:

Pssm-ID: 475130  Cd Length: 79  Bit Score: 60.78  E-value: 8.97e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 767926668   1 MYAGAALKDSWSLADVGISFCSTLKCFVKE 30
Cdd:cd17050   50 TYAGADLQDSWVLSDIGIPPGSTIRCLLRE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-247 1.07e-07

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.73  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668  147 LYIAAFCGYIELTEWALKQGARPHeavgvhpyrawcheaLHADVSKCPIHAAAEAGQLLILKAFVNYSVLCLECKnaaGQ 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------------LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GR 62

                          90       100
                  ....*....|....*....|.
gi 767926668  227 TPLTIVFKHKHKDCVLYLLSK 247
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEK 83
 
Name Accession Description Interval E-value
Ubl2_ANKUB1 cd17051
ubiquitin-like (Ubl) domain 2 found in Ankyrin repeat and ubiquitin domain-containing 1 ...
 31-113 6.73e-48

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: 160.12  E-value: 6.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668  31 EDKPTLYVFNAVTQDTMPVMESISLLDKTVSDLRTLVTLRCGLPVSVYCLRTPRGLEMYDCNTLKDYQTDIGTTLRLDVW 110
Cdd:cd17051    1 EIKPVLYVYCVFNQETIPIMEKINVLTTTVSQLRSIISRKTGLPVSVFRLVTPDGTEMYDCNLLDDYGIDIGTTLRLETW 80


                 ...
gi 767926668 111 DGW 113
Cdd:cd17051   81 DGW 83
Ubl1_ANKUB1 cd17050
ubiquitin-like (Ubl) domain 1 found in Ankyrin repeat and ubiquitin domain-containing 1 ...
 1-30 8.97e-12

ubiquitin-like (Ubl) domain 1 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 first Ubl domain.


Pssm-ID: 340570  Cd Length: 79  Bit Score: 60.78  E-value: 8.97e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 767926668   1 MYAGAALKDSWSLADVGISFCSTLKCFVKE 30
Cdd:cd17050   50 TYAGADLQDSWVLSDIGIPPGSTIRCLLRE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-247 1.07e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.73  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668  147 LYIAAFCGYIELTEWALKQGARPHeavgvhpyrawcheaLHADVSKCPIHAAAEAGQLLILKAFVNYSVLCLECKnaaGQ 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------------LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GR 62

                          90       100
                  ....*....|....*....|.
gi 767926668  227 TPLTIVFKHKHKDCVLYLLSK 247
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-247 1.24e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668 146 ALYIAAFCGYIELTEWALKQGARPHEAvgvhpyrawchealhADVSKCPIHAAAEAGQLLILKAFVNYSVLcLECKNAAG 225
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNAR---------------DNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDG 219

                         90       100
                 ....*....|....*....|..
gi 767926668 226 QTPLTIVFKHKHKDCVLYLLSK 247
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
Ubl2_ANKUB1 cd17051
ubiquitin-like (Ubl) domain 2 found in Ankyrin repeat and ubiquitin domain-containing 1 ...
 31-113 6.73e-48

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: 160.12  E-value: 6.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668  31 EDKPTLYVFNAVTQDTMPVMESISLLDKTVSDLRTLVTLRCGLPVSVYCLRTPRGLEMYDCNTLKDYQTDIGTTLRLDVW 110
Cdd:cd17051    1 EIKPVLYVYCVFNQETIPIMEKINVLTTTVSQLRSIISRKTGLPVSVFRLVTPDGTEMYDCNLLDDYGIDIGTTLRLETW 80


                 ...
gi 767926668 111 DGW 113
Cdd:cd17051   81 DGW 83
Ubl1_ANKUB1 cd17050
ubiquitin-like (Ubl) domain 1 found in Ankyrin repeat and ubiquitin domain-containing 1 ...
 1-30 8.97e-12

ubiquitin-like (Ubl) domain 1 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 first Ubl domain.


Pssm-ID: 340570  Cd Length: 79  Bit Score: 60.78  E-value: 8.97e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 767926668   1 MYAGAALKDSWSLADVGISFCSTLKCFVKE 30
Cdd:cd17050   50 TYAGADLQDSWVLSDIGIPPGSTIRCLLRE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-247 1.07e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.73  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668  147 LYIAAFCGYIELTEWALKQGARPHeavgvhpyrawcheaLHADVSKCPIHAAAEAGQLLILKAFVNYSVLCLECKnaaGQ 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------------LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GR 62

                          90       100
                  ....*....|....*....|.
gi 767926668  227 TPLTIVFKHKHKDCVLYLLSK 247
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
194-245 1.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767926668  194 PIHAAAEAGQLLILKAFVNYSVlCLECKNAAGQTPLTIVFKHKHKDCVLYLL 245
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-247 1.24e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668 146 ALYIAAFCGYIELTEWALKQGARPHEAvgvhpyrawchealhADVSKCPIHAAAEAGQLLILKAFVNYSVLcLECKNAAG 225
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNAR---------------DNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDG 219

                         90       100
                 ....*....|....*....|..
gi 767926668 226 QTPLTIVFKHKHKDCVLYLLSK 247
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
146-247 5.36e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 41.86  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767926668 146 ALYIAAFCGYIELTEWALKQGARPHeavgvhpYRAWCHEAlhadvskcPIHAAAEAGQLLILKAFVNYSVLcLECKNAAG 225
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVN-------ARDKDGET--------PLHLAAYNGNLEIVKLLLEAGAD-VNAQDNDG 153

                         90       100
                 ....*....|....*....|..
gi 767926668 226 QTPLTIVFKHKHKDCVLYLLSK 247
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
195-248 6.14e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 6.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767926668  195 IHAAAEAGQLLILKAFVNYSVLClECKNAAGQTPLTIVFKHKHKDCVLYLLSKM 248
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEHA 53
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
 57-107 1.53e-03

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: 37.19  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767926668  57 DKTVSDLRTLVTLRCGLPVSVYCLRTpRGLEMYDCNTLKDYQTDIGTTLRL 107
Cdd:cd17039   18 DDTVADLKEKIEEKTGIPVEQQRLIY-NGKELKDDKTLSDYGIKDGSTIHL 67
Ubl_ANKRD60 cd17063
ubiquitin-like (Ubl) domain found in ankyrin repeat domain-containing protein 60 (ANKRD60) and ...
 35-110 6.17e-03

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: 35.72  E-value: 6.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767926668  35 TLYVFNAVTQDTMPVMESISLLdkTVSDLRTLVTLRCGLPVSVYCLRTPRGLEMYDCNTLKDYQTDIGTTLRLDVW 110
Cdd:cd17063    4 SLKLRLPETEETFTVPNCYPGM--KVKELKSRLELVTGIPSHLQRLSYLDEGDLMDDSTLKYNDIVPGATITLRVW 77
 
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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