ID U1I237_ENDPU Unreviewed; 1079 AA.
AC U1I237;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERF76024.1};
GN ORFNames=EPUS_09452 {ECO:0000313|EMBL:ERF76024.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF76024.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KE720786; ERF76024.1; -; Genomic_DNA.
DR RefSeq; XP_007786643.1; XM_007788453.1.
DR AlphaFoldDB; U1I237; -.
DR GeneID; 19244256; -.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_003599_0_0_1; -.
DR OMA; NMAWVEA; -.
DR OrthoDB; 2477520at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015693; P:magnesium ion transport; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR PANTHER; PTHR24171; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 39-RELATED; 1.
DR PANTHER; PTHR24171:SF9; L-ASPARAGINASE; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01544; CorA; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144083; Magnesium transport protein CorA, transmembrane region; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 5.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 918..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 38..70
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 71..103
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 181..213
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 214..246
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 247..269
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 411..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 122923 MW; 81D02D69DEE56488 CRC64;
MSENFLRIGL MRSAEKGRIA ATQYLLREGA KTDVVAANRL SPLLRAVEHN HVGIVQLLLD
HGASTETADK KGRTALMTAA WKNHWHILQL LLSRGANVHA KDLKKRNILH NLAADKQCDW
GEDVLGLLLK LDICIDGREA QDNLGRSPLH WACATGKKRF AEKLLSRPRH PGANVNATEI
RSKTSLHIAA AHDRDDLVEL LLTYHADVNA RSDGGWTPLH NACEKGSEKI VRMLLQAGAE
INSKLLNGMT ALHLAAQGGH ADVVKCLLEC KDVNLTTRDT FGSTPLLRAA QFRRKDIVQL
LAPYNHVEAL SEDALGACNG FDATIVDFGN YHNENQVKRR TVYELLYGRD PKDSNKHAIS
TLPFNVKATR FRWIHLPANN MVWVEALLTK IFIEEGAGDV EGFKALEKSF SHQHRGQRTH
SHFMRPLSQS TPRAPRQDED DETEQMTPSV VVNGATKEDK VPETPVRISK SGSDQSNCAA
HIGLKNHATG SHNETKGKRR VKRGTDAPKS EQGRKSSLQL ANSIVRSRRS PGSPSRKDFM
HFAKSNIYTF MPYLHFETDT RRQEMQEAIR HAETLKARPA LTKARTYDEM LLRAHLSASN
TSLHVRRTLD QFFYHNIDTQ SRDCDQVVYR YQTKGRDQEY PRIDPKVFMV DQLWMWTLGK
DLIVTSFPQR WQQPKNDPLN VLDNIIEDIN SKTREPVKSV YDLAMIITGR CCGAFDRHRM
GDADYQFLDM FESSIGSATD RETTLFNEFN DASVQASEWL KHHRRPNRFS RNLGSSAEKE
DKFKFEDHNR RPLFVDKLLD IGQEIKLLTE IKDIRDELNM IRMVLQYQLQ VLPDLQEAIF
DIFKEEHRSH QEIKKHIKDQ QKIVDVHIKD LDRMDRQAER IYDSITDLLD LKQKHANAFE
ARFARDQAAG TARQGQTIMV FTIVTIIFLP LSFIAAFFAI DIQEFPRNVD GSQRLHLSYV
AQYMFGIGFA ISIPLVLIAL SLDDIGDLYR EAIRRLRRKR LGRERQPPQI DDAGRAVGVL
KMEQASTVAR SVGGSMETSW VGSLLPVARR TTGESERSRR RFIFRNSVDT ERRDGLRLH
//
