ID G8C080_TETPH Unreviewed; 1276 AA.
AC G8C080;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=IPT/TIG domain-containing protein {ECO:0000259|SMART:SM00429};
GN Name=TPHA0L02060 {ECO:0000313|EMBL:CCE65558.1};
GN OrderedLocusNames=TPHA_0L02060 {ECO:0000313|EMBL:CCE65558.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65558.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65558.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE612867; CCE65558.1; -; Genomic_DNA.
DR RefSeq; XP_003687992.1; XM_003687944.1.
DR AlphaFoldDB; G8C080; -.
DR STRING; 1071381.G8C080; -.
DR GeneID; 11531817; -.
DR KEGG; tpf:TPHA_0L02060; -.
DR eggNOG; KOG3836; Eukaryota.
DR HOGENOM; CLU_004311_0_0_1; -.
DR OMA; CIARQKF; -.
DR OrthoDB; 2901153at2759; -.
DR Proteomes; UP000005666; Chromosome 12.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00102; IPT; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1201..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 685..776
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|SMART:SM00429"
FT REPEAT 870..902
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 903..935
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 394..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 143407 MW; 26B1D3DBB5FF8969 CRC64;
MAEVNRESGN PIVRKNEIFD VLDEFLYPNS SPSNSKGNKF NNNNNIMKSN VNDFDEEIFN
AFIKTDSLDF RQHDDHNDYR DVTKVKAEAD AGTGVTLDQY NDTKVYEHGY SLNAENHSFM
ATNGDEKQDD DGITTTTTMD NDGTHKKTKS SITNTQNIYE ILIENTVSFG ERDVSVSSNL
DSHDTLASLK NAEEKLNKIN ELVNMDENLL PNKLIISKLP HQCRVENQIN ISIQIEPPLT
KQHILHLSSN NVAKNKLFLS KDIDNYPKNF LDEIVFLESF LLCSETNKIA NVCPMCINRE
QRRASRRKSG LCDNILWCQN ENRSALIFNS KQILPISSVA KHLQAFKLTA RMVCYSRHHK
SSKGFKILFI LKNLHGDLLA KSISDSILIM DKKPSSSMNG ESNKNKSATS SNFKTNASLS
PSNDKKNKHS KTYSNSNTDL SMDIDSNMDT DAYYSTNLSE ASTNYASMSD AQYNTNQIVQ
PYTHNTSLPN VNDPNAMMLP SQNNEYDSNN HNGNSMFNFT SPQTHIPSHN RVPSQSQLPP
QLNSQQQLLM LNSFMQQSGM PIIPSPTSMS EDGLDQNKSR SIKTASSTQI AARRNEYING
SARPKRQRSD IADTKYHSDN MNHSPLSWIN NSNNSNNNQF NQTLQNNANQ PVNAAAFTNR
TTDNNMPMVN TVSQNSNDNN IKMNLPLIQR AIPSQGPITG GIEITLLGSN FRNGLTIKFG
DNVTLSTQCW SDSTMVTYLP PAATAGQVFI IAEDPKYPNQ FVNQSNSNKN AVFTYLDDTD
RQLIELALQI VGLKMNGKLE DARNIAKRIV GNDENSPNIS PANGSAASTG NSNYSKYSSQ
LEGSYSDEQL IVKVINSLNA TSNLSMCDSN GRTLLHLAAL KGYEQLVMTL IKYGARIDEK
DMFGYTPLHF ACVNGEYKII AFLLKCKADL TIKAKNGVHA RDVYMVNHGN DEISSDDYNR
VIKMFDSLEK GSKLEFNNSS SGDFDLDSLH SLEYDIEPSI TVNSRGKTHK GPTTVAVSVS
EDSGYEVSDG ESFITNDSDL SSMNSESRDF INTENNGNNV FNIERSTSKK LREANELEEN
TEITNDESKG TETENNSVNY ADRNNDSLWN RMLNRINDDL PKYEDLFPGF THPSKAKQQT
TSMMDEEQAV TMNKTKDMSV LSSNTDDLSQ TSSEDEDDAI QIRLNRFFQQ QRETTFQNDK
MLWFFWFPLS IILISTYFFI KFGSIDDSKL YSFSFEIVDR FRKSLAKLML GNDRMKAAFK
EQLSNFQNTG IHVPVM
//