ID M7BVZ9_CHEMY Unreviewed; 1302 AA.
AC M7BVZ9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Protein FAM40A {ECO:0000313|EMBL:EMP32292.1};
DE Flags: Fragment;
GN ORFNames=UY3_10504 {ECO:0000313|EMBL:EMP32292.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP32292.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the STRIP family.
CC {ECO:0000256|ARBA:ARBA00007062}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000256|ARBA:ARBA00007122}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB540908; EMP32292.1; -; Genomic_DNA.
DR STRING; 8469.M7BVZ9; -.
DR eggNOG; KOG3680; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR040185; Far11/STRP.
DR InterPro; IPR021819; Far11/STRP_C.
DR InterPro; IPR012486; Far11/STRP_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR PANTHER; PTHR13239; PROTEIN REQUIRED FOR HYPHAL ANASTOMOSIS HAM-2; 1.
DR PANTHER; PTHR13239:SF7; STRIATIN-INTERACTING PROTEIN 1; 1.
DR Pfam; PF05221; AdoHcyase; 1.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR Pfam; PF11882; DUF3402; 2.
DR Pfam; PF07923; N1221; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SMART; SM01293; DUF3402; 1.
DR SMART; SM01292; N1221; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 249..412
FT /note="S-adenosyl-L-homocysteine hydrolase NAD binding"
FT /evidence="ECO:0000259|SMART:SM00997"
FT DOMAIN 530..828
FT /note="Far11/STRP N-terminal"
FT /evidence="ECO:0000259|SMART:SM01292"
FT DOMAIN 925..1282
FT /note="Far11/STRP C-terminal"
FT /evidence="ECO:0000259|SMART:SM01293"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP32292.1"
SQ SEQUENCE 1302 AA; 147955 MW; 7AA25DC86E980476 CRC64;
QIQFADDMQE FSKFPTKTGR RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK
GSSNFCVKNI KQAEFGRREI EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV
LIETLCALGA QCRWSACNIY STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG
WQANMILDDG GDLTHWVYKK YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND
SVTKQKFDNL YCCRESILDG LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVNIT
EIDPICALQA CMDGFRVVKL NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS
NTEIDVTSLR TPELTWERVR SQVDHVIWPD GKRVVLLAEA LALIELYNAP EGRYKQDVYL
LPKKMDEYVA SLHLPSFDAH LTELTDDQAK YLGLNKNGPF KPNYYRQCSS CHTAWGEGSV
SLVQNRPPDS LKEFCTELQP SIKFPEGWTL YPCGSSCGKH RSNQKGYSES PDLEFEYADT
DRWSAELSEL YSYTEGPEFQ LNRKCFEEDF RVHVLDKKWT ELDSNQHRTH AMRLLDGLEV
TAREKRLKVA RAILYVAQGT FGECGSEAEV QAWMRYNIFL LLEVGTFNAL VELLNMEIDN
SAACSSAVRK PAISLADSTD LRVLLNIMYL IVETVRQEAE GDKVEWKTIR QTFRAELGAP
LYNNEPFSVM LFGMVTKFCS GHAPHFPMKK VLLLLWKTAL CTLGGFEELQ AMKAEKREIL
GLPSLPEDSI KVIRNMRAAS PPASASDLIE QQQKRGRREH KALIKQDNLD AFNERDPYKA
DDSREEEEEN DDDSSLEGET FPLERDEVMP PPIQHPPTDR FACPKGLPWA PKVREKDIEM
FLESSRSKFI GYTLGSDTNT VVGLPRPIHE SIRTLKLHKY TSIAEVQVQM EEEYLRSPLS
GGEEEVEQVP TETLYQGLLP SLPQYMIALL KILLAAAPTS KAKTDSINIL ADVLPEEMPT
TVLQSMKLGV DVNRHKEIIV KAISAVLLLL LKHFKLNHVY QFEYMAQHLV FANCIPLILK
FFNQNIMSYI TAKNSISVLD YPYCVVHELP ELTAESLEAG DNNQFCWRNL FSCINLLRIL
NKLTKWKHSR TMMLVVFKSA PILKRALKVK QAMMQLYVLK LLKVQTKYLG RQWRKSNMKT
MSAIYQKVRH RLNDDWAYGN DLDARPWDFQ AEECALRASI ERFNSRRYDR AHSNPDFLPV
DNCLQSVLGQ RVELPEDFQM NYDLWLEREV FSRPISWEEL LQ
//
