ID A0A0F4Z0P9_TALEM Unreviewed; 1741 AA.
AC A0A0F4Z0P9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Vacuolar protein sorting protein (VPS11) {ECO:0000313|EMBL:KKA24089.1};
GN ORFNames=T310_1901 {ECO:0000313|EMBL:KKA24089.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA24089.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA24089.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA24089.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA24089.1}.
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DR EMBL; LASV01000075; KKA24089.1; -; Genomic_DNA.
DR RefSeq; XP_013330701.1; XM_013475247.1.
DR STRING; 1408163.A0A0F4Z0P9; -.
DR GeneID; 25314252; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProt.
DR GO; GO:0099023; C:vesicle tethering complex; IEA:UniProt.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR Pfam; PF17122; zf-C3H2C3; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 1201..1354
FT /note="CHCR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT DOMAIN 1651..1688
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 110..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1741 AA; 192868 MW; B56C5A00694021A3 CRC64;
MPLRRPTSPL ILEELSTNDS DIDDVLGSDD ELDESTRAAK RRRIEKLGES YLQGKPLFIA
SASLRGPFDD GWVNPWKKQR KQWRDSLSNL KKINSCAKTA PVEGRVIPET DVKKRCTEEP
SATMGRGNQP GEIVRKRSTV FPGPETDNHG GSEVSNPREA SVASGASSNA RKKQRRSLPW
IENTTASTES GPNSSDRTFK SDWLRKSNMT INVRDVDPPK SPTPLYAGRR DRVKEIAKKS
SQTATSPTSS RNIPSWPADL CGAKRKPSPR DSSNASHASG LSPQRDARGA VQPPIVDEAD
ASRPQGKSIA PALQHAVADP AENRSRRSSV YIVPPSSHLP EFRYRRPKNP VQPEEFSSSP
SKWTRAADGD VSGMTGPQRE ISVQEAKELP SSARGSSNQK HDSICPNDHG RRPDSTRLRA
SIGPGAEPSG SRNLASNSTG SEQIPSAQVV PGNQGLSDRM ISLHSTELHG ERGTQNDRED
DDAQISTQAA LLLAQKSFQD DLTTPKCGIQ PKSAASHPDH QSTANRITPF SHINTTPERH
SDNVPMTART ERFQALNTQA MIDAVTPFTF STSKKSEPWM EPGSGLTKTL SSLKRRKKTC
FALSSSPPRS VSSSSDGGLQ QQDAPAHAIP GKNVEASQIA ATGFDQVETE NSVQGSSHAL
QLTLSGSTPT TEQQDGQGLL GGMDSFNINQ VIQDAGSWLQ QSWEVEKELR RCSGQSAQSS
STQTQRAATT FVLIKTFMSV LMFNLPADWL GTSDKHGWDN CLAPRGAPSN TVSTPPGALR
QPIFNPRAYH CCSWRGFKAN GSDFVKQWKT FNFFEVSQVK LPEESSSVFN DDVACLCTGS
DNLFLGTNDG VVHIVSSSFK VVRSFKAHDA GSIRHMKQVE GTSLLVTIAE DLPNEPVLKV
WALDEIGKKT GAPRCLSTLS VQNGRRPFPV SAFAALDDLS QLAVGFANGS VAIIRGDLIN
DRGARQRIVF ESEEPITGLE TQRGHTTILY IATTNRILTL TIAGRGQGQP ARVLEDAGCG
LGCMALEKET GDILIAREDA IHTYGPRGRG PSYAFDSPKS SLNLFRGYVA LVCPPKTSKS
DSLRRLGVSQ VDDIFNTSTF TLLDTDLKFI AHSEVLVSPA KSVFTIWGDL FLITIDGKIY
RYHEKSLQQK LEILYQRNLY ILAINLAQKA GVDTLQQNVI FRKYGDYLYQ KGDYDTAMQQ
YLRAIDNTEP SQVIRKFLDT QRIHNLIEYL EELHDHERAT ADHTTLLLNC YAKLKDTSKL
DSFIKAPGEL KFDLETAIAM CRQGGYFEQA AYLATKHGEH DMKLLLSIWN WELMWNKAYP
NLMKYARVLL GHCPRETTQL FIDYYTGRYR PKKEAELPVK TETQSGSAVQ NLAALLPLPY
VGTGGTKAQP SEAQVTSEEK SLDVTPTYEI PKPRTAFSAF VDHPDEFITF LEALIKQESL
KKEDKIDLYT TLFEMYLDTA KRKKDASERQ EWENKAKKLI EGKDIPISTS NVLLLSDLSN
FREGTTLVRE QEGLRSDIFR SYTAAKDTQG VIKALRKYGP EEPQLYIDAL AYFTSSPKIL
EEAGDELNAV LRKIDEDGLM APLQVIQALS NNAVVTMGMI KKYLSDNIER ERKEISTNRR
LISSYSSETE SKKKEIEELG TKPVVFQARR CMSCGGSLEL PVVHFLCKHS FHQRCLDRTD
EDAECPVCAP QHATIKAIRK RQVESADQHD LFNSELHRSR DRFGLISEFF GRGVMRPQKT
E
//