ID A0A420XXU7_9PEZI Unreviewed; 1391 AA.
AC A0A420XXU7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=IMP-specific 5'-nucleotidase 1 {ECO:0000256|ARBA:ARBA00015544};
DE EC=3.1.3.99 {ECO:0000256|ARBA:ARBA00012894};
GN ORFNames=DL546_000985 {ECO:0000313|EMBL:RKU40485.1};
OS Coniochaeta pulveracea.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU40485.1, ECO:0000313|Proteomes:UP000275385};
RN [1] {ECO:0000313|EMBL:RKU40485.1, ECO:0000313|Proteomes:UP000275385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAB683 {ECO:0000313|EMBL:RKU40485.1,
RC ECO:0000313|Proteomes:UP000275385};
RA Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053; EC=3.1.3.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000433};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the ISN1 family.
CC {ECO:0000256|ARBA:ARBA00005307}.
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:RKU40485.1}.
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DR EMBL; QVQW01000101; RKU40485.1; -; Genomic_DNA.
DR STRING; 177199.A0A420XXU7; -.
DR Proteomes; UP000275385; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006190; P:inosine salvage; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd21675; SMP_TEX2; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR009453; ISN1.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR28213; IMP-SPECIFIC 5'-NUCLEOTIDASE 1; 1.
DR PANTHER; PTHR28213:SF1; IMP-SPECIFIC 5'-NUCLEOTIDASE 1; 1.
DR Pfam; PF06437; ISN1; 1.
DR Pfam; PF10296; MMM1; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 281..472
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 543..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1391 AA; 152974 MW; DDEAF0DA1D571C08 CRC64;
MSSWTAFLLT YLFGGITFLP LVVLTVLIHA HFTFPVHKDD TAPRTEAAQN EIVQPGDDIA
GLKAAQRDET KTWAANADND VAAGYFGVSR EYTPMGINAK PIERSTPVGS TTVTAPSPSV
YQSMYRSLFD RKQLSNPLDG QNSSQRPKRV GNVFYLVLRH GHLMLFDDDE QLEVRHVISL
AHHDVSLYSG GDTTPEGELF IKRNAICLSR RSDSPIVGAD TRLSKPFYLF SENTSAKEDF
YFALLRSQQQ SAVADGAVPA PLNFDIKHII SLVQKLHSSE EHQQTRWLNA MIGRVFLGLY
KTKDMENLIR EKLTKKISRV NRPSFLSNIT IQGIDTGEAA PYFTNLRLKD LTVEGECGME
ADVRYTGKCR LEVAATARIE LGSRLKAREV SLVLAVVINK LEGHMLFKIK PPPSNRIWFS
FQSMPKLDMT IEPIVSSRQI TYNVILRQIE NRIKEVIAET LVLPFWDDVP FFRTEHKRWR
GGIFDGDDEV ASSPDPETAL AQVGDVDDVD EYEQNGAEET GVGQPLKAKS HSLPVIEALP
KHNGFFGRKK GEQRSNGSLA SSASASATSV DTKQENVPER RAMRRSSFMG SAAPTTGTDV
TNVEAVKPAS ASSPPSRSIS VLQDLSASPP ATDTVSNPAT DPYRPYITSR SSKSSQSSLS
SREVTDSEKD ADNQDAKELE KTPVARHGAA SSAESHDDSS SQSPTVSMKG SIRSQTGLLA
RNLLGRKDYP SADATGHPSS PPTMTEREQQ RKNAIAAVTN VAASAKRWGL NALQRNNDGP
KHGGSREHEP PLDLKQPMGR GRPLPPPGTP LPMPERKTKT APAPMLRRKP VLAPQPDHHH
GDTELGHSAH PTPPPLPKRR SQLVTESSHE AGDVGMLVVA APVESEPTTP VAATQPNQQR
SNYFQPCMQD VDDTPDTEID EGHDNQRGPA RRSGLDLVSP TRVTSQDTVS TPGSGSARDP
AEGQETAPDG DYSAWVDNVN TSQSEWIKGL LAVPFVLYSQ PTGVFEGKAG TGDLQIKARE
EAHRRYSEIF RDVEVMIDDY IHHQRDENPL PSKLQLLVPT IGPFFTRLPL EAGFKYQDRK
RYISSRRFVS PSFNDIRLIL NSAQIMAVTT YGALQLATFD GDVTLYDDGQ SLEPDSPVIP
RMLNLLRQNV RIGIVTAAGY TTAERYYSRL HGLLDAMSVS EGLTSAQRQN LIIMGGEANY
LFEYSPSSPH LLAPVSRERW LTPEMASWAE DDISQLLDVA EAALRDCVKN LNLPAVVLRK
DRAVGIVAQP PEIRIPRESL EETVLVVQKI LEMSDIGRSR RVPFCAFNGG RDVFVDIGDK
SWGVAVCQRW FGGEGNMIRA ESTLHVGDQF LSAGANDFRA RSVGTTAWIA SPAETVELLD
ELADLMGKKL S
//
