ID A0A319ESN4_ASPSB Unreviewed; 705 AA.
AC A0A319ESN4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Transport protein particle component-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO78DRAFT_304837 {ECO:0000313|EMBL:PYI10895.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI10895.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI10895.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI10895.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.
CC {ECO:0000256|ARBA:ARBA00006218}.
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DR EMBL; KZ826320; PYI10895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ESN4; -.
DR STRING; 1448318.A0A319ESN4; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd16792; SP-RING_Siz-like; 1.
DR CDD; cd14944; TRAPPC6A_Trs33; 1.
DR Gene3D; 2.60.120.780; PINIT domain; 1.
DR Gene3D; 3.30.1380.20; Trafficking protein particle complex subunit 3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR007194; TRAPP_component.
DR InterPro; IPR037992; TRAPPC6/Trs33.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF97; SUPPRESSOR OF VARIEGATION 2-10, ISOFORM I; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF04051; TRAPP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 17..51
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 76..241
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 270..355
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 77..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 78457 MW; 6999078DF900C7A0 CRC64;
MASAGQFSDT QNLVALVKTL TNAQLKDILR NEGLAVSGVK ASLQLRIIDF IERLSQAGQV
EQYDNLRQFI YATARRPVPT PSTTQSIPNQ HFQPHPVSQP LSTQQRPSPL SIQMPSQGLT
PVREQTRDSV ELKVVLTPNV AARLQADPNL RVMVYCAADT GLNQYTKSDI AFPHQVELKA
NLDEVKANLR GLKNKPGTTR PADVTQYIRK KPGYPNNIVM TYALTQKASR FFVLVNLVQR
HPVEELVVEL KRRKTISKEQ VLREMRNKAG DSDIVATSSV LSLKCPLSTL RIEVPCRSVI
CTHNQCFDAS SFLQLQEQAP TWSCPVCSKA TSFESLQIDQ YVDDILRLTS LDVEQVIIEP
DGRWSSPNHE ESSKTGGFTP TTDDDDELIE IREPGVTPIK QESLSAPTFL VHRTPTQSRE
PSTASSAAHL STNKRNAAQV IDLTGSDEDE DTPIRPTKRP AFNSMSRPSP RQDFCNPYNG
GFLNRDIQLS SQPGSEYPSQ ANKHFVRVDI GTTFAMSFDT PASPLNASDP HARLLGASCL
DFLLIELVPM AERMAKELAS GDNLPDDEEI RETAFFRLES LGYRVGQGLA ERRFSRDRPR
FADNLDIIKF LCKDLWTILF KKQVDNLKTN HRGVYVLTDN SFRPFARMST SVRGEAVSMA
QAYLWFPCGV IRGALSNLGI TTTVQAESAE LPGATFQIKT VNPKP
//
