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Conserved domains on  [gi|42572849|ref|NP_974521|]
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hypothetical protein (DUF1644) [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1644 super family cl20347
Protein of unknown function (DUF1644); This family consists of sequences found in a number of ...
 47-186 2.90e-85

Protein of unknown function (DUF1644); This family consists of sequences found in a number of hypothetical plant proteins of unknown function. The region of interest contains nine highly conserved cysteine residues and is approximately 160 amino acids in length, and is probably a zinc-binding domain.


The actual alignment was detected with superfamily member pfam07800:

Pssm-ID: 462269  Cd Length: 164  Bit Score: 251.73  E-value: 2.90e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572849    47 VTCPVCLEVPHNSVVLLCSSYHKGCRPYMCATGNRFSNCLEQYKKAYAK----------------------DEKSDKPPE 104
Cdd:pfam07800   3 ATCPICMEHPHNAVLLLCSSHDKGCRPYMCDTSYRHSNCLDRFKKAYGKsssstsqssssastnnsssnvvSSSKEESSE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572849   105 LLCPLCRGQVKGWTVVEKERKYLNSKKRSCMNDECLFYGSYRQLKKHVKENHPRAKPRAIDPVLEAKWKKLEVERERSDV 184
Cdd:pfam07800  83 LKCPLCRGQVKGWTVVEEARKYLNAKKRSCSEESCSFSGNYKELRKHARLEHPLARPSEVDPSRQRDWRRLERQRELGDV 162


                  ..
gi 42572849   185 IS 186
Cdd:pfam07800 163 LS 164
 
Name Accession Description Interval E-value
DUF1644 pfam07800
Protein of unknown function (DUF1644); This family consists of sequences found in a number of ...
 47-186 2.90e-85

Protein of unknown function (DUF1644); This family consists of sequences found in a number of hypothetical plant proteins of unknown function. The region of interest contains nine highly conserved cysteine residues and is approximately 160 amino acids in length, and is probably a zinc-binding domain.


Pssm-ID: 462269  Cd Length: 164  Bit Score: 251.73  E-value: 2.90e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572849    47 VTCPVCLEVPHNSVVLLCSSYHKGCRPYMCATGNRFSNCLEQYKKAYAK----------------------DEKSDKPPE 104
Cdd:pfam07800   3 ATCPICMEHPHNAVLLLCSSHDKGCRPYMCDTSYRHSNCLDRFKKAYGKsssstsqssssastnnsssnvvSSSKEESSE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572849   105 LLCPLCRGQVKGWTVVEKERKYLNSKKRSCMNDECLFYGSYRQLKKHVKENHPRAKPRAIDPVLEAKWKKLEVERERSDV 184
Cdd:pfam07800  83 LKCPLCRGQVKGWTVVEEARKYLNAKKRSCSEESCSFSGNYKELRKHARLEHPLARPSEVDPSRQRDWRRLERQRELGDV 162


                  ..
gi 42572849   185 IS 186
Cdd:pfam07800 163 LS 164
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
 49-115 8.64e-04

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 36.51  E-value: 8.64e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572849  49 CPVCLEVPHNSVVLLCSsyHKGCRPymcatgnrfsnCLEQYKkayakdeKSDKPpelLCPLCRGQVK 115
Cdd:cd16509   6 CAICLDSLTNPVITPCA--HVFCRR-----------CICEVI-------QREKA---KCPMCRAPLS 49
 
Name Accession Description Interval E-value
DUF1644 pfam07800
Protein of unknown function (DUF1644); This family consists of sequences found in a number of ...
 47-186 2.90e-85

Protein of unknown function (DUF1644); This family consists of sequences found in a number of hypothetical plant proteins of unknown function. The region of interest contains nine highly conserved cysteine residues and is approximately 160 amino acids in length, and is probably a zinc-binding domain.


Pssm-ID: 462269  Cd Length: 164  Bit Score: 251.73  E-value: 2.90e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572849    47 VTCPVCLEVPHNSVVLLCSSYHKGCRPYMCATGNRFSNCLEQYKKAYAK----------------------DEKSDKPPE 104
Cdd:pfam07800   3 ATCPICMEHPHNAVLLLCSSHDKGCRPYMCDTSYRHSNCLDRFKKAYGKsssstsqssssastnnsssnvvSSSKEESSE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42572849   105 LLCPLCRGQVKGWTVVEKERKYLNSKKRSCMNDECLFYGSYRQLKKHVKENHPRAKPRAIDPVLEAKWKKLEVERERSDV 184
Cdd:pfam07800  83 LKCPLCRGQVKGWTVVEEARKYLNAKKRSCSEESCSFSGNYKELRKHARLEHPLARPSEVDPSRQRDWRRLERQRELGDV 162


                  ..
gi 42572849   185 IS 186
Cdd:pfam07800 163 LS 164
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
 49-115 8.64e-04

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 36.51  E-value: 8.64e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42572849  49 CPVCLEVPHNSVVLLCSsyHKGCRPymcatgnrfsnCLEQYKkayakdeKSDKPpelLCPLCRGQVK 115
Cdd:cd16509   6 CAICLDSLTNPVITPCA--HVFCRR-----------CICEVI-------QREKA---KCPMCRAPLS 49
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
 47-111 2.86e-03

RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase and is highly related to MID1 that associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1.


Pssm-ID: 438412 [Multi-domain]  Cd Length: 70  Bit Score: 35.73  E-value: 2.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42572849  47 VTCPVCLEVPHNSVVLLCSsyHKGCrpYMCATGNRFSNCleqykkayAKDEKSDKPPELLCPLCR 111
Cdd:cd16754   8 LTCPICLELFEDPLLLPCA--HSLC--FSCAHRILTSGC--------ASGESIEPPSAFQCPTCR 60
 
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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