ID F2PSZ6_TRIEC Unreviewed; 914 AA.
AC F2PSZ6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Ubiquitin-protein ligase Sel1/Ubx2 {ECO:0000313|EMBL:EGE05014.1};
GN ORFNames=TEQG_03856 {ECO:0000313|EMBL:EGE05014.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the sel-1 family.
CC {ECO:0000256|ARBA:ARBA00038101}.
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; DS995736; EGE05014.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PSZ6; -.
DR VEuPathDB; FungiDB:TEQG_03856; -.
DR eggNOG; KOG1550; Eukaryota.
DR HOGENOM; CLU_007931_0_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11102:SF147; FIBRONECTIN TYPE-II DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR Pfam; PF08238; Sel1; 8.
DR SMART; SM00671; SEL1; 10.
DR SUPFAM; SSF81901; HCP-like; 3.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EGE05014.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 840..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 868..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 102265 MW; 5F6BCF392111BBFC CRC64;
MTNDDNSQRL LLATQLRAFR ALQYVGHDQF DYDTLQRLTD IINYINEGIS TTANLYHAYT
NPRSIRWIMA NRMLCLQAIT AGARNLREDL TNRESNPTDL PLPGSLDVEN PVARARGNNG
REYSIDQPVV ETALNILRKI KVPTKKYERP SGIFGHASYY GRELFYLLFM NAPSSDQLSS
SRFTKKNGKL VEAVRLLEGA ARKNNSDATF LLAEMNFYGN YTHPRDFSKA FRYYEALATL
TGNSTAQYML GFMYATGIGG VVERDQGKAL LYHTFAARGG NTRSQMTLAY RRYIGIGAAP
DCDQAVYWYK KVADKAIAWY RSGPPGGVNW RREAFRWADE EGGVYGEGAS VSSAGYNAMR
DVHSSADASL DDVLEYLDLM AKKGDTKATF GLGKLYYEGS RQLERSYKKA MMYFVVVARK
YWTKDGSINP SHPPGIDKIA AQSAAHIGLM FLRGEGTEQN FQKAKVWFTR GRANGDAMCQ
HYLGLMYLHG YGVEQDVMKA ASYFKAAAEQ DNYYSKTRLG ALFLDQGDVV TASIYFEAAA
RHGGMEALYY LAGIADRGLG GQRHCGVATA YYKIVSEKAE GIHSAFAEAN DAYEIGDKEL
ALIISTMAAE QGYESAQANV AYLLDEKRSV LSLDPILPWI RGGRSSLLRN AALGFIYWAR
SAKQANIDSM VKLGDYYFEG YGTKKDVSRA LTCYHSAAEG HSAQAFWNLG WMYENGLHVE
QDFPMAKRYY DLALETNQEA YFPVTLSLLR LRARNFWNKV IRGKANTINA EPDVNTPRTF
KEWISHFINY NEEEEAYQRA LRQQAAADPD AILDEAGHAH AQDQDLNYYD EDALDFDDGI
LESLIIIGLV ATLVLLLHFR QQRAARRAQE ANNANNQQQN QGADGAGNAA EDRGFFPRPD
DPNFAAWVAG GLGR
//
