ID A0A091DLA0_FUKDA Unreviewed; 1066 AA.
AC A0A091DLA0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acyl-CoA synthetase family member 3, mitochondrial {ECO:0000313|EMBL:KFO31867.1};
GN ORFNames=H920_06758 {ECO:0000313|EMBL:KFO31867.1};
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:KFO31867.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO31867.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO31867.1};
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; KN122240; KFO31867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DLA0; -.
DR STRING; 885580.ENSFDAP00000020273; -.
DR eggNOG; KOG1176; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11304; Cadherin_repeat; 4.
DR CDD; cd05941; MCS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 4.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
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; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027:SF300; CADHERIN-15; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00028; Cadherin; 4.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF49313; Cadherin-like; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS00232; CADHERIN_1; 1.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 650..731
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 732..839
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 854..954
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 955..1041
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 1042..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 117384 MW; F96DAAC7C326B4FD CRC64;
MLPRVTLPFR QLVCAVASCC RAPGGHRGLH FLHTAPTACS DGAAPVFTKA LAFGDRIALF
DQHGRHTYRD LYHHSLRLSL EICRLRGCLD GDLQDERVSF LCSNDVSYVV AQWASWMSGG
IAVPLFWKHP EAQLEYFIQD SRSSVVLASP EHVPLVGPVA ERLGVPLLPL PPDVYRGAVG
EPAAKPAQER KWQDRGAMIL YTSGTTGRPK GVLSTHRNLT ATVTGLVHAW AWTRDDVILH
VLPLHHMHGV VNKLLCPLWV GATCVMLPEF SAQQVWEKFL SPETPWVNVF MAVPTVFSKL
LDYYDQHFTQ PHVQDFVRAV CKERIRLMVS GSAALPTPLL ERWKSATGHT LLERYGMTEV
GMALSSPLSG ARLPGSVGTP LPQVEVRIIS ESPQRDGCPY TVHAEGDAQG TKVTPGLEEK
EGELLVRGPS VFREYWDKPE ETKSTFTPDG WFRTGDTAVF KDGSYWIRGR TSVDIIKTGG
YKVSALEVER QLLAHPSISD VAVIGVPDVT WGQRVTAVVA LQAGHSLSHS DLKEWARPST
VQAADYGPVP CAQPCSAQAE LSRRRFLAPY AVPSGLLLVE EIPRNQMGKI NKKDLSLGLS
WGVPGRPSTL YPWRRLPARG RVRRAWVIPP ISVSENYKGL PYMLVQIRSD KRQPGGVIYS
IQGPGVDEEP LGLFSVEKFS GRVFLNAELD REKTASYRLK VFALDRGGSV LEEPTDLEIL
VVDQNDNRPA FVQEVFTGRV LEGAAPGTYV TRAEATDADD PDTANAALHY SILAQGSPEL
FSIHERTGEI RTVHVGLDRE VVTVYNLTLQ VADMSGEGLT STASAIISVD DINDNAPEFT
SDKFSMEATE AISGVDVGRL EVEDRDLPGS PNWVANFTIL EGDPRGHFDI RTDPRTNEGV
LSVVKPLDYE SCARYELRVS VQNEAPLQAA SPQAQRGQAT VSIRVQDVNE APVFPENPLR
TSVAEGAPPG TFVATFSAQD PDTVQLQRVS YSKDYDPEDW LQVNGASGRI QTRRVLSPAS
PFLKDGWYRA IVLALDDGEQ PASRGRWGWS THKHTPRTMT PRTGCR
//