ID A0A0J8RXR3_COCIT Unreviewed; 779 AA.
AC A0A0J8RXR3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=AMP deaminase 3 {ECO:0000313|EMBL:KMU89371.1};
GN ORFNames=CIHG_07177 {ECO:0000313|EMBL:KMU89371.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU89371.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000256|ARBA:ARBA00006676}.
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DR EMBL; DS017012; KMU89371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RXR3; -.
DR STRING; 396776.A0A0J8RXR3; -.
DR VEuPathDB; FungiDB:CIHG_07177; -.
DR eggNOG; KOG1096; Eukaryota.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0003876; F:AMP deaminase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0032264; P:IMP salvage; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.800.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR01429; AMP_deaminase; 1.
DR PANTHER; PTHR11359; AMP DEAMINASE; 1.
DR PANTHER; PTHR11359:SF0; AMP DEAMINASE; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88270 MW; 73BAC7BED3E0F6FC CRC64;
MAEPCRDQAF EPSRWKMPDP HEDATTYESD DKNGIATQDL SSDSANGDGE QSHENMDGTP
DDIDPTNSGG SPILPRDRQR RTATYDYAYE KSVSHAEAKL FYQRHQLAYR PAEGDTPQSP
SLPSRASGAP PSSSFELDSP TRTASAASRL SNQGQFLPPP SQHITSTPLA TTTLRRDSLA
AANQSARGYS LHHAPLHENE SRLLASQGIH GAGAGFGVGQ GAGGFVANDD AITAELGVIC
HKIQSLLDTR RKYIKLSMQR SEDNPRDDPS WIIYPPPPEP AWGDYGEPTG ANSMANSMVI
PTENDGVEND GIPPSPARKR RKPGQNIGED FDMDDLLPLP EASSMVFKLD ESSVYQVYDT
KEACELGQPI VQVPSLRDFY MDLDTIIDVS TDGPIKSFAF KRLSYLEGKF QLHALLNEYQ
EIADSKKVPH RDFYNVRKVD THVHHSACMN QKHLLRFIKS KMKKSPDEVV LFRDGKHLTL
REVFESINLT AYDLSIDTLD MHAHTDSFHR FDKFNLKYNP IGESRLREIF LKTDNYIKGR
YLAEITKEVI SDLESSKYQM AEWRISIYGR SMDEWDKLAA WVVDNKLFSP NIRWLIQVPR
LYDVYKSNGI VEDFDAIIQN VFQPLFEVTQ DPNSHPKLHV FLQRVVGFDS VDDESKAERR
LYRKFPIPKQ WNTKQNPPYS YWIYFMFANM ASLNTWRKRR GFNTFVLRPH CGEAGDPDHL
ASAFLCCFGI SHGILLRKVP LLQYLFYLDQ IGIAMSPLSN NALFLTYERN PFATIFKRG
//