ID A0A2S4L6T2_9HYPO Unreviewed; 1224 AA.
AC A0A2S4L6T2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Sorting nexin-12 {ECO:0000313|EMBL:POR38111.1};
GN ORFNames=TPAR_01687 {ECO:0000313|EMBL:POR38111.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR38111.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR38111.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR38111.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:POR38111.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PKSG01000167; POR38111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4L6T2; -.
DR STRING; 94208.A0A2S4L6T2; -.
DR OrthoDB; 5392990at2759; -.
DR Proteomes; UP000237481; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd06876; PX_MDM1p; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR013937; Sorting_nexin_C.
DR PANTHER; PTHR22775; SORTING NEXIN; 1.
DR PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000237481};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..287
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 413..552
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 873..991
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..864
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 608..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1224 AA; 137138 MW; CF4084B418ED9F77 CRC64;
MALKRRDVAL AAVAAFVAWG YAVSWFSVLR WAGYAFVGGA VVAVLGLVAA LLLTSRRPNY
TSSRPSGVSF LGARRWRAEV EALRLRQAYV KPALELGSPR VARAVDGLLD LILRDFVRTW
YSYISRNPLF PNEVDRSVRL ALASLLEPLR QKDLADIVTS RLVPILTAHF RDFYDAERSV
RGRKLNRSVT ESEELDLAIA SKFRDGRLHP AASLSFPDTK MVQQDYLRSL VTRIMPKVLT
ENMLSSRAVS TLVREIVGCA VLSPILQLLS DPDTWNQLME NYGRSMLQDR STVRKLRAAL
DQHASPTPRS GKPAVAPRLA PGDSERKFEK FIRGIRKVNN LSDARRFRSE VASQLKRDSL
QENQDPVYLR RLEMGKRLLD QRVNHLAAGG ERRAPPRPVI PASASTSRLQ NASLVELLRD
PSGLSYFMEY MDRQHLMSLV QFWLVVDGFR NPLEDDGPEE EQPSSNLPMW TESDRMDLQQ
IHQAYLSKPE LKAPEASKRE VRQFLQAGKS ATPAQYHNAR RSILKAQSVV LQEMQNRYFQ
AFRNSDLYYK CLASQESSNT SVPPPPAPSG HLEQQQHPPM QRAAPSYQSK PKPLARLVPP
SGAAARRSGS ASDLQSLNGN GQGNGLDALA TSRRSLDENS PNPLFDDDDL DHDGMLDSVQ
SLDQDASGQP VPDTQVVQAV EEALSNILDD DRPQTAEDLR ASLFGAEDNE PSFMSAHDND
SNRGSIDAGR SSILGKESEK PSLSSLGLVS AASRIGVFVD DDLFDDEDKT LADEVEEGDD
GVAPADDDEV HEAAPGDLGL AEAITVLTND IERLVAQEAV VDSLTRKAEL TNNTSELRIL
RKSKASLQRE IRRKELQRQQ YVVQESDNSL YGRSTIKIKS IQVGREEDGR EFALYVVEVQ
RNAGEQMPAA SWIVTRRYSE FHDLHQKLRS RYPSVRNLDF PRRRMVMKFQ SEFLRKRRAA
LEKYLRELLL LPDVCRSREL RAFLSQSVIA QGQDILDRED KKDMMTRLYD SVADGMDDIL
GNIPVLDQIS VAGQNLIAAA TSQLNSMPLN VNEETFPAAE AEAELNAFEN KELEPFIKPI
CDIFLEVFEL NRGNNWLRGR AVVVVLQQLL GGTIERKVRD NIKMLVQDES ILRYLGMVTD
NLWPNGELQQ DWKPRGAAER KKTRTEASLM LATLVPDLAG NVVGRVNAQA ASRRIFATFN
NARLNAHLVF TMLDEIVAVL FDED
//