ID A0A162QJK6_MUCCL Unreviewed; 946 AA.
AC A0A162QJK6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Vacuolar protein sorting-associated protein 41 {ECO:0000256|PIRNR:PIRNR028921};
GN ORFNames=MUCCIDRAFT_148109 {ECO:0000313|EMBL:OAD00029.1};
OS Mucor lusitanicus CBS 277.49.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD00029.1, ECO:0000313|Proteomes:UP000077051};
RN [1] {ECO:0000313|EMBL:OAD00029.1, ECO:0000313|Proteomes:UP000077051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD00029.1,
RC ECO:0000313|Proteomes:UP000077051};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for vacuolar assembly and vacuolar traffic.
CC {ECO:0000256|PIRNR:PIRNR028921}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000256|ARBA:ARBA00004132}. Vacuole
CC {ECO:0000256|PIRNR:PIRNR028921}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the VPS41 family.
CC {ECO:0000256|ARBA:ARBA00009582, ECO:0000256|PIRNR:PIRNR028921}.
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:OAD00029.1}.
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DR EMBL; AMYB01000007; OAD00029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162QJK6; -.
DR STRING; 747725.A0A162QJK6; -.
DR VEuPathDB; FungiDB:QYA_148109; -.
DR OrthoDB; 8838at2759; -.
DR Proteomes; UP000077051; Unassembled WGS sequence.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-UniRule.
DR GO; GO:0034058; P:endosomal vesicle fusion; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR016902; VPS41.
DR InterPro; IPR045111; Vps41/Vps8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR PANTHER; PTHR12616:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 41 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR PIRSF; PIRSF028921; VPS41; 1.
DR SMART; SM00299; CLH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Protein transport {ECO:0000256|PIRNR:PIRNR028921};
KW Reference proteome {ECO:0000313|Proteomes:UP000077051};
KW Transport {ECO:0000256|PIRNR:PIRNR028921};
KW Vacuole {ECO:0000256|PIRNR:PIRNR028921};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT REPEAT 102..143
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 834..907
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 109043 MW; 8A0A4CAF19A9AA32 CRC64;
MSVDSKKQDT VLSDDDKPYD SDQEEYDEDE EYDEEDEDET DEDDDSLDEP KLRYRRVGAS
VKELLDKDTA STLRVSDRFV ALGTHWGAVH ILDFEGNVIK SFRSHAATVN DISIDKSDEF
VASASDDGKV FIYALYTPEI QSFNYKRPVK SVALDPDYAR KSTRQFVSGG MAEQLIMSEK
GWLGHKDIIL HANEGPIYAI RWRNNFIAWA NDTGVKIYDT TTNVRITYID RPDGSPRADL
YKCRMCWKND TTLLIGWADT VKVAVIKPRA NPAQGQPAHY VEITTMFQTD YIISGIAPFN
DTLMLLSYLL EEEEEEKDAD NPSFQRKRLA SKPELHIINA DNEEISADVL ALHGFEHYQA
NDYVLDFLME EDMFYVMGPK DLIAARSRDQ DDHIEWLLEH ERFGEALQAV RATTTSKKFN
ADQIGQTYLN WLMAEKKFDQ AAEECSDILK HDQLLWEDWV FKFTEVGELK AIAPYIPIKD
PQLSSTVYEI ALAWFLKSDH VALRNTIRKW PRTHYNLSNV IVAVEDVMKK DKHDEVLLEC
LADLYTYNSQ PDKAIEYNLR LRRPNAFELI QEYNMFDAVK DKAVLLMEFD QHLLEKEGET
KSKPSKMPAV QLLVKNTDAI PPEKVVKQLR RHRQFLHIYL DALFDRDHQL GYEFHDLQVE
LYAEFDYPKL LEFLRASHYI SLEKAYKICE QRDLVPEMVF ILGRMGNNKK ALMLIIERLE
DVQRAIDFAK EQKDDDLWED LLTYSMDKPN FIRGLLENVG TDIEPLRLIK RIPDHLEIPG
LKDALLKILQ DYNLQMSLHE GCEKILVSDS VFLADKMYKA QKRGVNCNPE DMVCNICEEP
VFDETNVEDI PNSIIFFCRH AYHQQCLINQ SSVEQLQQDN NPGSLTSKVN QSALLKSTQN
MACPLCREQA AGGNAFVNRM KTQRRGVKRS PQSPTAGSIR SFGTVH
//
