GenomeNet

Database: UniProt
Entry: F6SRE9_MONDO
LinkDB: F6SRE9_MONDO
Original site: F6SRE9_MONDO 
ID   F6SRE9_MONDO            Unreviewed;       419 AA.
AC   F6SRE9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Acyl-coenzyme A amino acid N-acyltransferase 2-like {ECO:0000313|Ensembl:ENSMODP00000017999.2};
GN   Name=LOC100017693 {ECO:0000313|Ensembl:ENSMODP00000017999.2};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000017999.2, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000017999.2, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000017999.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00006538}.
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DR   RefSeq; XP_007499711.1; XM_007499649.2.
DR   RefSeq; XP_007499713.1; XM_007499651.2.
DR   RefSeq; XP_016279779.1; XM_016424293.1.
DR   RefSeq; XP_016279780.1; XM_016424294.1.
DR   RefSeq; XP_016279781.1; XM_016424295.1.
DR   AlphaFoldDB; F6SRE9; -.
DR   STRING; 13616.ENSMODP00000017999; -.
DR   MEROPS; S09.A50; -.
DR   Ensembl; ENSMODT00000018330.3; ENSMODP00000017999.2; ENSMODG00000014400.3.
DR   GeneID; 100017693; -.
DR   KEGG; mdo:100017693; -.
DR   eggNOG; ENOG502QQ8Z; Eukaryota.
DR   GeneTree; ENSGT01010000222336; -.
DR   HOGENOM; CLU_029849_4_0_1; -.
DR   InParanoid; F6SRE9; -.
DR   OMA; RPFLWGG; -.
DR   TreeFam; TF314911; -.
DR   Proteomes; UP000002280; Chromosome 6.
DR   Bgee; ENSMODG00000014400; Expressed in spermatid and 7 other cell types or tissues.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.2240; Acyl-CoA thioester hydrolase/BAAT N-terminal domain; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR   InterPro; IPR014940; BAAT_C.
DR   InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR   InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR   PANTHER; PTHR10824:SF1; ACYL-COENZYME A AMINO ACID N-ACYLTRANSFERASE 1-RELATED; 1.
DR   PANTHER; PTHR10824; ACYL-COENZYME A THIOESTERASE-RELATED; 1.
DR   Pfam; PF08840; BAAT_C; 1.
DR   Pfam; PF04775; Bile_Hydr_Trans; 1.
DR   PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280}.
FT   DOMAIN          14..142
FT                   /note="Acyl-CoA thioester hydrolase/bile acid-CoA amino
FT                   acid N-acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04775"
FT   DOMAIN          205..413
FT                   /note="BAAT/Acyl-CoA thioester hydrolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08840"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
FT   ACT_SITE        328
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
FT   ACT_SITE        362
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016521-1"
SQ   SEQUENCE   419 AA;  46418 MW;  6836BB87071B68CA CRC64;
     MVQLIVTPET ALADEPICIR ATGLNPFQVV TFTASLTDEK GKLFQSRAFY KANEAGNVDL
     DQAAALGGDY VGVHPMGLFW SLKPVNPFRR LLKQDVMNSP FYIQLDIFDS LLLEDSPKIH
     PKASQMIERW FSGPGLQRIP VRNGRVRGAF FLPPGEGPFP GVIDLFGGIG GLIEFRASLL
     ASHGFGVLAL AYFAYEDLPR SLLEVDLEYF EEAANMLLHH PQIQRSGIGV ISVCKGAEIG
     LAMAIHLEQV AATICINGTN AVHETPCKYR DLVISPIPHQ KEYTQIHVSG ALNFRRIKGD
     PRDEVNQQSV LPVEKARGHI LFIVGEKDEC LNSKAYAEQA MEQLKSHGRS NGTLLSYPGA
     GHLIEPPYSP LCFASWNPFL SRPFLWGGDI RSHAAAQEHS WREIQKFLRC HLAPSRSKL
//
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