ID A0A319AA13_ASPLB Unreviewed; 702 AA.
AC A0A319AA13;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Transport protein particle component-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO96DRAFT_433655 {ECO:0000313|EMBL:PYH56836.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH56836.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH56836.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH56836.1,
RC ECO:0000313|Proteomes:UP000247441};
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 (DEC-2016) 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; KZ821348; PYH56836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319AA13; -.
DR OrthoDB; 20246at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000247441; 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; IPR036361; SAP_dom_sf.
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 SUPFAM; SSF68906; SAP domain; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
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..239
FT /note="PINIT"
FT /evidence="ECO:0000259|PROSITE:PS51466"
FT DOMAIN 268..353
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 360..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 78109 MW; 299693DBFBFF9052 CRC64;
MASTGQFSDT QSLVALVKTL TNAQLKDILR NEGLAVSGVK ASLQLRIIDY IERLNQGGHV
EQYDDLRKFI YATARRPIPM SPTTQAVPGQ HYQPHTVNQP LHTQHRPSPL SIPMPPHGQT
SVREQTRDSV ELKVILTPTV AARLQADPNI RVMVYCAADT GLNQYTKSDI AFPHQVELKA
NLDEVKANLR GLKNKPGTTR PADVTQYIRK KPGYPNNIVL TYALTQKRFF VLVNLVQRHP
VEELVDELKR RKTISKEQVL REMRSKAGDS DIVATSSVMS LKCPLSTLRI EVPCRSVICT
HNQCFDASSF LQLQEQAPTW SCPVCSKATS FESLQIDQYV DDILRSTSLD VEQVIIEPDG
RWSSPTQEDS AKVGGYTPAT DDDDELIEIR EPGVTPIKRE SFPPPSFFVH QTPTQSREPS
ATSSAAYLST NKRNAAQVID LTGSDEEDDA PVRPVKRPAF NQMNRPSSQQ DFCNPYSGGY
ANGDIQLPSQ PSSDFLNHAG SSTTVVTLTP FTMSLDTPAS SLSASDPHAR LLGASCLDFL
LIELVPMAER LAKELASEEK LPDDEEIRET TFFRLESLGY RVGQGLAERR FSRDRPRFAD
NLDIIKFLCK DLWTILFKKQ VDNLKTNHRG VYVLTDNSFR PFARMSTSVR SEAVSMAQAY
LWFPCGVIRG ALSNLGITTT VQAESTELPG ATFQIKTVNP KP
//
