ID A0A5D2WG38_GOSMU Unreviewed; 569 AA.
AC A0A5D2WG38;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 10.
DE RecName: Full=Macro domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=E1A91_A13G089300v1 {ECO:0000313|EMBL:TYJ00484.1};
OS Gossypium mustelinum (Cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=34275 {ECO:0000313|EMBL:TYJ00484.1, ECO:0000313|Proteomes:UP000323597};
RN [1] {ECO:0000313|EMBL:TYJ00484.1, ECO:0000313|Proteomes:UP000323597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1408120.09 {ECO:0000313|EMBL:TYJ00484.1};
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De L., Hulse-Kemp A., Ding M.,
RA Ye W., Kirkbride R., Jenkins J., Plott C., Lovell J., Lin Y.-M., Vaughn R.,
RA Liu B., Li W., Simpson S., Scheffler B., Saski C., Grover C., Hu G.,
RA Conover J., Carlson J., Shu S., Boston L., Williams M., Peterson D.,
RA Mcgee K., Jones D., Wendel J., Stelly D., Grimwood J., Schmutz J.;
RT "WGS assembly of Gossypium mustelinum.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GDAP2 family.
CC {ECO:0000256|ARBA:ARBA00008355}.
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DR EMBL; CM017648; TYJ00484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D2WG38; -.
DR Proteomes; UP000323597; Chromosome a13.
DR CDD; cd02905; Macro_GDAP2-like; 1.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035793; Macro_GDAP2.
DR PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR11106:SF72; GANGLIOSIDE-INDUCED DIFFERENTIATION-ASSOCIATED PROTEIN 2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000323597}.
FT DOMAIN 71..251
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 394..543
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 42..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 64098 MW; B80CD9E57557A356 CRC64;
MYRPVATAAA TGGVPTDNGD YVVTLDQVPR WNDAEIRSSL EYENEDPSFS KSFLSDPLTS
HGEESGTNGL ASRFPVDHEI NSKIYLWRGQ PWNLEVDAVV NSTNENMDEV HSSQGLHAAA
GPGLAEECAT LGGCRTGMAK VTNAYDLPAR RVIHTVGPKY AVKYHSAAEN ALSHCYRSCL
ELLIENGLRS IAMGCIYTEA KNYPREPAAH VAIRTVRRLL EKQKDKITAV VFCTSTSSDT
EIYKRLLPLY LPRDKHEEAV AISKLPADVG DENGETIIHE RKIRIKPLPK KVIPKPSQSP
AEVPASDVGL VQRSVPVQIL EYRNSSYLDT YLDPAFMSLM KDPDQRRQEQ WEKTAQAQGG
WNCAKMLGFG DIGGPPLSAA EEYSLHSRYL AKANSLNLSE IAEMKILYRG GVDSEGRPVM
VVVGAHFLLR CLELERFILY VVKEFEPLIQ KPYTIVYFHS AASLQVQPDL GWMRRLQQIL
GRKHQRNLHA IYVLHPTFHL KTAIFALQMF VDKVVWKKVV YVDRLLQLFK YVPREQLTIP
DFVFQHDIEV NGGKGLIVDP RTKYIYHRP
//
