Q46455 (SELB_MOOTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Selenocysteine-specific elongation factor

Alternative name(s):
SelB translation factor

Gene names

Name:

selB

Organism

Moorella thermoacetica (Clostridium thermoaceticum)

Taxonomic identifier

1525 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteraceae › Moorella group › Moorella

Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the GTP-binding elongation factor family. SelB subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC selenocysteine incorporation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 634

634

Selenocysteine-specific elongation factor

PRO_0000091476

Regions

Nucleotide binding

10 – 17

8

GTP By similarity

Nucleotide binding

60 – 64

5

GTP By similarity

Nucleotide binding

115 – 118

4

GTP By similarity

Secondary structure

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634

Helix Strand Turn

Details...

Helix

379 – 389

11

Helix

396 – 403

8

Helix

407 – 419

13

Beta strand

423 – 428

6

Beta strand

431 – 436

6

Helix

437 – 457

21

Helix

466 – 473

8

Beta strand

475 – 477

3

Helix

479 – 491

13

Beta strand

494 – 497

4

Beta strand

499 – 504

6

Helix

513 – 529

17

Helix

536 – 542

7

Helix

547 – 559

13

Beta strand

562 – 569

8

Beta strand

571 – 573

3

Helix

574 – 588

15

Helix

595 – 602

8

Helix

606 – 618

13

Beta strand

621 – 625

5

Beta strand

628 – 631

4

Sequences

	Sequence		Length	Mass (Da)
	Q46455 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 626F9E8A693A8296	FASTA	634	70,666
	10 20 30 40 50 60 MDYIVVGTAG HVDHGKTVLV KALTGVDTDR LKEEKERGIS IELGFAPLTL PSGRQLGLVD 70 80 90 100 110 120 VPGHERFIRQ MLAGVGGMDL VMLVVAADEG VMPQTREHLA IIDLLQIKKG IIVITKIDLV 130 140 150 160 170 180 EADWLELVRE EVRQAVKGTV LEDAPLVEVS ALTGEGIAEL REQLDALAAV TPPRPAAGRV 190 200 210 220 230 240 RLPIDRVFSV TGFGTVVTGT LWSGTIKVGD ELEVQPEGLK TRARNLQVHG RTVKEARAGQ 250 260 270 280 290 300 RVAVNLAGIE TEAVHRGSSL LTPGFLTPTY RLDASFKLLN GARPLANRDR VHFYLGTSEA 310 320 330 340 350 360 LGRVVLLDRD ELNGGEEALI QLLMEKPVVA SREDRFILRS YSPMETIGGG IIIDPVPPKH 370 380 390 400 410 420 RRFQPEVLVS LQRRLEGSPE KILAQIIQEH REGLDWQEAA TRASLSLEET RKLLQSMAAA 430 440 450 460 470 480 GQVTLLRVEN DLYAISTERY QAWWQAVTRA LEEFHSRYPL RPGLAREELR SRYFSRLPAR 490 500 510 520 530 540 VYQALLEEWS REGRLQLAAN TVALAGFTPS FSETQKKLLK DLEDKYRVSR WQPPSFKEVA 550 560 570 580 590 600 GSFNLDPSEL EELLHYLVRE GVLVKINDEF YWHRQALGEA REVIKNLAST GPFGLAEARD 610 620 630 ALGSSRKYVL PLLEYLDQVK FTRRVGDKRV VVGN

References

[1]	"Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB." Kromayer M., Wilting R., Tormay P., Boeck A. J. Mol. Biol. 262:413-420(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 521.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X99830 Genomic DNA. Translation: CAA68147.1.
Y14814 Genomic DNA. Translation: CAA75097.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LVA	X-ray	2.12	A	377-634	[»]
1WSU	X-ray	2.30	A/B/C/D	512-634	[»]
2PLY	X-ray	2.60	A/B	377-634	[»]
2UWM	X-ray	2.31	A/B	377-634	[»]
2V9V	X-ray	1.10	A	377-511	[»]

ProteinModelPortal

Q46455.

SMR

Q46455. Positions 377-634.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29313N.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.10.10. 4 hits.

InterPro

IPR000795. EF_GTP-bd_dom.
IPR015189. Elong_fac_SelB-wing-hlx_typ-1.
IPR015190. Elong_fac_SelB-wing-hlx_typ-2.
IPR015191. Elong_fac_SelB-wing-hlx_typ-3.
IPR005225. Small_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR009000. Transl_elong_init/rib_B-barrel.
IPR004535. Transl_elong_SelB.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF09105. SelB-wing_1. 1 hit.
PF09106. SelB-wing_2. 1 hit.
PF09107. SelB-wing_3. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.

TIGRFAMs

TIGR00475. selB. 1 hit.
TIGR00231. small_GTP. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q46455.

Entry information

Entry name

SELB_MOOTH

Accession

Primary (citable) accession number: Q46455

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program