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Database: UniProt
Entry: A0A0J8RXR3_COCIT
LinkDB: A0A0J8RXR3_COCIT
Original site: A0A0J8RXR3_COCIT 
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
//
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