ID A0A091E212_FUKDA Unreviewed; 986 AA.
AC A0A091E212;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acyl-CoA synthetase family member 4 {ECO:0000313|EMBL:KFO37382.1};
GN ORFNames=H920_01207 {ECO:0000313|EMBL:KFO37382.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO37382.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO37382.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO37382.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; KN120907; KFO37382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091E212; -.
DR STRING; 885580.ENSFDAP00000015777; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG4649; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.480; -; 1.
DR Gene3D; 2.40.128.630; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR44394; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44394:SF1; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR Pfam; PF13570; PQQ_3; 2.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 442..519
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 986 AA; 110685 MW; 6AA982BDF18C97F8 CRC64;
MTLQELVHRA ASLHLDKTAV CFDECNNQPP VYYTYKTVIS AASELSHFLQ LHCDFQRIRE
IGLYCQPGIN LPSWILGILQ VPAAYAPIDP DSPPSLSTHF MKKCNLKYIL VEKKQLNKFR
SSHETLLNYD TLTVEHNDLV LVRLHWKNVE VNLMLNDEKE DYERENHMSS KNSNEEKELM
DARCKDCLAY VLHTSGTTGI PKIVRVPHVC VLPNVQHFQE LFDITPEDVL FMAAPLTFDP
SVVEIFVALS SGASLLIVPT SVKILPSKLA PVLFTHHRVT VLQLTSMFLS LEGGKNRVCF
LDDEVTVPLG TMRATGDFVT LKGGEIFFLG RKDSQIKRHG KRLNIELVQQ TAEELQQVES
CAVTWYNQEK LILFIVSKDD VVKDDIFKEL QKRLPNHAIP DELVLIDTLP FTSHGKVDVS
ELNKIYLDYV NLKTENKFEG KEDLWEKLQC LWKSILSLPE DLLKVPDESL FLNNGGDSLK
SIRLLSEIEQ LVGTPVPGLL EIILKSSILE IYNYILQTVF AVEDPTFTKT YATKRKLSDT
DEEEASGKSL HQKSAWPFSN KEIYAFISLS RGSQILSVNT STSLTELGHH PLAHSPDLIS
QTDIKNLKSL NPPPVIKKSK GPNCVKKVFE EGNLVTKAEK MEICVRWRSD TGKCVDASPL
VVIPAGDDSS ITVYIGSHSH RMKAVDLCSG KVKWEQILGD RIESSACVSM CGNFIVVGCY
NGLVYVLKSN SGEKYWMFTT EDTVKSSATA DPTTGLIYIG SHDQRVYALD IYKKKCVWKI
QCEGAVFSSP CLSLNPHHLY CATLRGLLLA VDPATGNTIW KHSCGKPLFS SPRCCRQYIC
IGCVDGNLLC FTHSGEQVWQ YSTSGPIFSS PCILASEQEI FFGSHDCFIY CCNMKGHLQW
KFETTSRVYA TPFAFHNHNS NSELLLAAAS TDGKLWILGS ESGQLQSVYE LPGEIFSSPV
IWESLLIIGC RNNYIYCLDL LISNQK
//