O02193 (MOF_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Males-absent on the first protein
EC=2.3.1.-

Alternative name(s):
Putative acetyl transferase MOF

Gene names

Name:	mof
ORF Names:	CG3025

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	827 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable histone acetyltransferase that plays a direct role in the specific histone acetylation associated with dosage compensation. Dosage compensation insures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes. May be directly involved in the acetylation of histone 4 at 'Lys-16' on the X chromosome of males. Ref.1
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	dosage compensation, by hyperactivation of X chromosome Non-traceable author statement. Source: FlyBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	X chromosome located dosage compensation complex, transcription activating Inferred from direct assay. Source: FlyBase transcription factor complex Inferred from direct assay. Source: FlyBase
Molecular function	chromatin binding Inferred from direct assay. Source: FlyBase histone acetyltransferase activity (H4-K16 specific) Traceable author statement. Source: FlyBase mRNA binding Traceable author statement. Source: FlyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 827

827

Males-absent on the first protein

PRO_0000051563

Regions

Zinc finger

572 – 594

23

C2HC-type

Region

688 – 694

7

Acetyl-CoA binding By similarity

Compositional bias

93 – 116

24

Ser-rich

Compositional bias

135 – 141

7

Poly-Gln

Compositional bias

212 – 314

103

Pro-rich

Compositional bias

340 – 346

7

Poly-Glu

Compositional bias

466 – 472

7

Poly-Ala

Sites

Active site

680

1

Nucleophile By similarity

Binding site

718

1

Acetyl-CoA By similarity

Natural variations

Natural variant

5

1

E → V in strain: Congo 159, Congo 194 and Congo 216. Ref.2

Natural variant

48

1

A → S in strain: Africa-1 and Africa-5. Ref.2

Natural variant

119

1

D → E in strain: Congo 216. Ref.2

Natural variant

156

1

G → D in strain: Congo 8, Congo 13, Congo 194 and Mof.820A.s. Ref.2 Ref.6

Natural variant

202

1

G → C in strain: Africa-0. Ref.2

Natural variant

254

1

A → V in strain: Congo 194. Ref.2

Natural variant

384

1

F → Y in strain: Africa-0, Africa-3, Africa-4, Congo 194 and Mof.591A.s. Ref.2 Ref.6

Experimental info

Mutagenesis

691

1

G → E: Males fail to metamorphose and hatch. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

827

Helix Strand Turn

Details...

Beta strand

383 – 386

4

Beta strand

392 – 401

10

Turn

403 – 405

3

Beta strand

411 – 415

5

Beta strand

417 – 419

3

Turn

421 – 423

3

Beta strand

425 – 428

4

Turn

429 – 431

3

Beta strand

432 – 434

3

Helix

436 – 440

5

Turn

441 – 443

3

Sequences

	Sequence		Length	Mass (Da)
	O02193 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 8B9C5E87E3B01317	FASTA	827	92,657
	10 20 30 40 50 60 MSEAELEQTP SAGHVQEQPI EEEHEPEQEP TDAYTIGGPP RTPVEDAAAE LSASLDVSGS 70 80 90 100 110 120 DQSAEQSLDL SGVQAEAAAE SEPPAKRQHR DISPISEDST PASSTSTSST RSSSSSRYDD 130 140 150 160 170 180 VSEAEEAPPE PEPEQPQQQQ QEEKKEDGQD QVKSPGPVEL EAQEPAQPQK QKEVVDQEIE 190 200 210 220 230 240 TEDEPSSDTV ICVADINPYG SGSNIDDFVM DPDAPPNAII TEVVTIPAPL HLKGTQQLGL 250 260 270 280 290 300 PLAAPPPPPP PPAAEQVPET PASPTDDGEE PPAVYLSPYI RSRYMQESTP GLPTRLAPRD 310 320 330 340 350 360 PRQRNMPPPA VVLPIQTVLS ANVEAISDDS SETSSSDDDE EEEEDEDDAL TMEHDNTSRE 370 380 390 400 410 420 TVITTGDPLM QKIDISENPD KIYFIRREDG TVHRGQVLQS RTTENAAAPD EYYVHYVGLN 430 440 450 460 470 480 RRLDGWVGRH RISDNADDLG GITVLPAPPL APDQPSTSRE MLAQQAAAAA AASSERQKRA 490 500 510 520 530 540 ANKDYYLSYC ENSRYDYSDR KMTRYQKRRY DEINHVQKSH AELTATQAAL EKEHESITKI 550 560 570 580 590 600 KYIDKLQFGN YEIDTWYFSP FPEEYGKART LYVCEYCLKY MRFRSSYAYH LHECDRRRPP 610 620 630 640 650 660 GREIYRKGNI SIYEVNGKEE SLYCQLLCLM AKLFLDHKVL YFDMDPFLFY ILCETDKEGS 670 680 690 700 710 720 HIVGYFSKEK KSLENYNVAC ILVLPPHQRK GFGKLLIAFS YELSRKEGVI GSPEKPLSDL 730 740 750 760 770 780 GRLSYRSYWA YTLLELMKTR CAPEQITIKE LSEMSGITHD DIIYTLQSMK MIKYWKGQNV 790 800 810 820 ICVTSKTIQD HLQLPQFKQP KLTIDTDYLV WSPQTAAAVV RAPGNSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila." Hilfiker A., Hilfiker-Kleiner D., Pannuti A., Lucchesi J.C. EMBO J. 16:2054-2060(1997) [PubMed: 9155031] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF GLY-691.
[2]	"Species-specific positive selection of the male-specific lethal complex that participates in dosage compensation in Drosophila." Rodriguez M.A., Vermaak D., Bayes J.J., Malik H.S. Proc. Natl. Acad. Sci. U.S.A. 104:15412-15417(2007) [PubMed: 17878295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-5; SER-48; GLU-119; ASP-156; CYS-202; VAL-254 AND TYR-384. Strain: Africa-1, Africa-3, Africa-4, Africa-5, Africa-7, Amherst, Congo 13, Congo 159, Congo 194, Congo 216 and Congo 8.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Pervasive and largely lineage-specific adaptive protein evolution in the dosage compensation complex of Drosophila melanogaster." Levine M.T., Holloway A.K., Arshad U., Begun D.J. Genetics 177:1959-1962(2007) [PubMed: 18039888] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-827, VARIANTS ASP-156 AND TYR-384. Strain: Mof.591A.s, Mof.639A.s, Mof.732A.s, Mof.774A.s, Mof.799A.s, Mof.820A.s, Mof.852A.s and Mof.859A.s.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U71219 Genomic DNA. Translation: AAC47507.1.
EF630368 Genomic DNA. Translation: ABU97211.1.
EF630369 Genomic DNA. Translation: ABU97212.1.
EF630370 Genomic DNA. Translation: ABU97213.1.
EF630371 Genomic DNA. Translation: ABU97214.1.
EF630372 Genomic DNA. Translation: ABU97215.1.
EF630373 Genomic DNA. Translation: ABU97216.1.
EF630374 Genomic DNA. Translation: ABU97217.1.
EF630375 Genomic DNA. Translation: ABU97218.1.
EF630376 Genomic DNA. Translation: ABU97219.1.
EF630377 Genomic DNA. Translation: ABU97220.1.
EF630378 Genomic DNA. Translation: ABU97221.1.
EF630379 Genomic DNA. Translation: ABU97222.1.
AE014298 Genomic DNA. Translation: AAF46095.1.
AY102685 mRNA. Translation: AAM27514.1.
EU167134 Genomic DNA. Translation: ABV82526.1.
EU167135 Genomic DNA. Translation: ABV82527.1.
EU167136 Genomic DNA. Translation: ABV82528.1.
EU167137 Genomic DNA. Translation: ABV82529.1.
EU167138 Genomic DNA. Translation: ABV82530.1.
EU167139 Genomic DNA. Translation: ABV82531.1.
EU167140 Genomic DNA. Translation: ABV82532.1.
EU167141 Genomic DNA. Translation: ABV82533.1.

RefSeq

NP_511051.1. NM_078496.2.

UniGene

Dm.2952.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BUD	NMR	-	A	367-454	[»]

ProteinModelPortal

O02193.

SMR

O02193. Positions 366-534, 540-813.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46346N.

STRING

O02193.

Proteomic databases

PRIDE

O02193.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0070829; FBpp0070794; FBgn0014340.

GeneID

31518.

KEGG

dme:Dmel_CG3025.

NMPDR

fig|7227.3.peg.16647.

Organism-specific databases

CTD

31518.

FlyBase

FBgn0014340. mof.

Phylogenomic databases

eggNOG

inNOG04829.

GeneTree

EMGT00050000000694.

InParanoid

O02193.

OMA

SGITHDD.

OrthoDB

EOG41RN8V.

PhylomeDB

O02193.

Gene expression databases

Bgee

O02193.

GermOnline

CG3025. Drosophila melanogaster.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.

KO

K11308.

Pfam

PF01853. MOZ_SAS. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF54160. Chromodomain-like. 1 hit.

ProtoNet

Search...

Other

NextBio

774017.

Entry information

Entry name

MOF_DROME

Accession

Primary (citable) accession number: O02193
Secondary accession number(s): A8B845 , A8B850, A8B854, A8B859, A8B879, A8B889, A8B895, A8B8A1, A8ILB7, A8ILC1, A8ILC8, A8ILD1, A8ILD6, A8ILE1, A8ILE5, Q9W463

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project