ID A0A1V8UUD6_9PEZI Unreviewed; 987 AA.
AC A0A1V8UUD6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A51_04984 {ECO:0000313|EMBL:OQO27299.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO27299.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO27299.1}.
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DR EMBL; NAEU01000170; OQO27299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UUD6; -.
DR STRING; 1974281.A0A1V8UUD6; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01293; Bact_CD; 1.
DR CDD; cd05911; Firefly_Luc_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
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; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR24096:SF389; 4-COUMARATE--COA LIGASE-LIKE 1; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 41..394
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 447..826
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 885..966
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 987 AA; 109073 MW; DA44D829F5DED29B CRC64;
MRVINARLRD HIGLCDIVVA NEKISSIKEH DSETVPVGDE IYDPKGYLTV PQFCENHIHL
DYANTAGVPR DNQSGTLFEA IEIWRDRKEA GLTRPEEIKH NALLAVRSCV EHGVGFIRSH
ADVTDPDLIA LKVLLELRDE VKEWCEIQVV AFPQNGIIAF PHGKELMEKA MSMGADVVGG
IPHLEPTYED GVESLKFIFD LAQKHNAMVD VHCDEIDDPE SRFVDIMAAE TTKRGMQGRV
TVSHAVAMGY YPPGYLARLL PKLVESEVGF AIAPRENLQL QGRDFGAPTP RGVAPIRMLA
DRGISVAFSQ DSICDPWYPI GNGNPMLNMD SGLHVGHMLT AQYIDRCLDF ISYNPAANMG
LQDRYGLDEG KSASFLILGA TTDREALRIQ PRVLLSVHKA MVFFPPIWAP ELPKVPTDIT
IEQFMLDEEH GRHPHRHSRN PFTDGLSGKT YSLPEVKQRV DFVARALVEE LGFKVNEGSE
WDKVVGLFSV NTIDYLTVCW AVHKIGGVLT AASAAYSAPD LEYQLKHSGA KAVFTCATLL
ETTKEACAKS GIPENRIYIL PLPEKAALGA TAPGLKTVDD FIARGAKLPE LEKLRFGPND
GAERTAFLCY SSGTSGLPKG VMISHRNVIA NVLQMYTYEE PGRSKLKPEA GQPKYTENCL
GLLPYSHIYG LVVVTHTGVY RGDGVIVLPK YDFEQLLKSI QDFKIAMLYL VPPMIIHITK
AANIVKKYDL SHVKAIFTGA APLGAETAED LQRMFPDWSI KQGYGMTETC TVVCTSATHD
IWFGSSGSLL PGYKARIVTV EGVECTGYDQ PGELWVSTPS NTLGYLKNEK ATKETFTIED
DGERYTRTGD EAVVRVSPGG NEHIFIVDRI KELIKVKGMQ VAPAELEAVL LTHPAVNDCV
VIGIPSEREG EVPKAFVVKA PGSIEESDSL LKRDICKHVE KLKSNHKWLR GGVEFIDVVP
KSPSGKILRR MIRDQEKAKM KKQGARL
//