U.S. flag

An official website of the United States government

Links from Protein

Items: 18

1.

SelB C-terminal domain-containing protein

Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding [1]. [1]. 12145214. Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. Selmer M, Su XD;. EMBO J. 2002;21:4145-4153. (from Pfam)

GO Terms:
Biological Process:
selenocysteine incorporation (GO:0001514)
Molecular Function:
RNA binding (GO:0003723)
Molecular Function:
translation elongation factor activity (GO:0003746)
Molecular Function:
GTP binding (GO:0005525)
Cellular Component:
cytoplasm (GO:0005737)
Date:
2024-10-16
Family Accession:
NF020672.5
Method:
HMM
2.

EutP/PduV family microcompartment system protein

Members of this family function in ethanolamine and propanediol degradation pathways [1-3]. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments [4]. [1]. 15516577. Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica. Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR;. J Bacteriol. 2004;186:7635-7644. [2]. 10464203. The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. Kofoid E, Rappleye C, Stojiljkovic I, Roth J;. J Bacteriol 1999;181:5317-5329. [3]. 10498708. The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation. Bobik TA, Havemann GD, Busch RJ, Williams DS, Aldrich HC;. J Bacteriol. 1999;181:5967-5975. [4]. 20417607. Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement. Parsons JB, Frank S, Bhella D, Liang M, Prentice MB, Mulvihill DP, Warren MJ;. Mol Cell. 2010;38:305-315. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
biogenic amine metabolic process (GO:0006576)
Date:
2024-10-16
Family Accession:
NF022128.5
Method:
HMM
3.

GTPase

This HMM identifies the P-loop-containing domain of large numbers of GTPases with ribosome-associated functions, including many involved in ribosome maturation (Der, Era, etc), ribosome rescue (HflX), and protein translation (InfB, Tuf, PrfC).

GO Terms:
Molecular Function:
GTP binding (GO:0005525)
Date:
2024-10-16
Family Accession:
NF014036.5
Method:
HMM
4.

ADP-ribosylation factor-like protein

Pfam combines a number of different Prosite families together 3D Structure reference. [1]. 7990966. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Amor JC, Harrison DH, Kahn RA, Ringe D;. Nature 1994;372:704-708. Mini review. [2]. 7759471. Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes. Moss J, Vaughan M;. J. Biol. Chem. 1995;270:12327-12330. [3]. 7770914. Arf proteins: the membrane traffic police?. Boman AL, Kahn RA;. Trends Biochem Sci 1995;20:147-150. [4]. 1899243. Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C;. J Biol Chem 1991;266:2606-2614. (from Pfam)

GO Terms:
Molecular Function:
GTPase activity (GO:0003924)
Molecular Function:
GTP binding (GO:0005525)
Date:
2024-10-16
Family Accession:
NF012255.5
Method:
HMM
5.

GTP-binding protein

This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains. Cryoelectron microscopy structure. [1]. 9311785. Visualization of elongation factor Tu on the Escherichia coli ribosome. Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W, van Heel M;. Nature 1997;389:403-406. (from Pfam)

GO Terms:
Molecular Function:
GTPase activity (GO:0003924)
Molecular Function:
GTP binding (GO:0005525)
Date:
2024-10-16
Family Accession:
NF012239.5
Method:
HMM
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.

selenocysteine-specific translation elongation factor

selenocysteine-specific translation elongation factor binds GTP and GDP and transfers selenocysteinyl-tRNA to the ribosome

Date:
2021-10-11
Family Accession:
11461714
Method:
Sparcle
17.

selenocysteine-specific translation elongation factor

In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This HMM describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes.

Gene:
selB
GO Terms:
Biological Process:
selenocysteine incorporation (GO:0001514)
Molecular Function:
RNA binding (GO:0003723)
Molecular Function:
translation elongation factor activity (GO:0003746)
Molecular Function:
GTPase activity (GO:0003924)
Molecular Function:
GTP binding (GO:0005525)
Cellular Component:
cytoplasm (GO:0005737)
Date:
2024-05-14
Family Accession:
TIGR00475.1
Method:
HMM
18.

GTP-binding protein

Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once. This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model.

GO Terms:
Molecular Function:
GTP binding (GO:0005525)
Date:
2022-03-28
Family Accession:
TIGR00231.1
Method:
HMM

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center
External link. Please review our privacy policy.