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Database: UniProt
Entry: K2RND2_MACPH
LinkDB: K2RND2_MACPH
Original site: K2RND2_MACPH 
ID   K2RND2_MACPH            Unreviewed;       582 AA.
AC   K2RND2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=DNA-binding SAP {ECO:0000313|EMBL:EKG16213.1};
GN   ORFNames=MPH_06650 {ECO:0000313|EMBL:EKG16213.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG16213.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG16213.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG16213.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- SIMILARITY: Belongs to the PIAS family.
CC       {ECO:0000256|ARBA:ARBA00005383}.
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:EKG16213.1}.
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DR   EMBL; AHHD01000284; EKG16213.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RND2; -.
DR   STRING; 1126212.K2RND2; -.
DR   VEuPathDB; FungiDB:MPH_06650; -.
DR   eggNOG; KOG2169; Eukaryota.
DR   HOGENOM; CLU_020537_1_0_1; -.
DR   InParanoid; K2RND2; -.
DR   OrthoDB; 20246at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.780; PINIT domain; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR023321; PINIT.
DR   InterPro; IPR038654; PINIT_sf.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR004181; Znf_MIZ.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10782:SF4; TONALLI, ISOFORM E; 1.
DR   PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14324; PINIT; 1.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF02891; zf-MIZ; 1.
DR   SMART; SM00513; SAP; 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   DNA-binding {ECO:0000313|EMBL:EKG16213.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129};
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          18..52
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          115..271
FT                   /note="PINIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51466"
FT   DOMAIN          298..379
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          377..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  64530 MW;  18B879227C5226B5 CRC64;
     MASGQSLQQQ ASSLHPRLKT LINNDLKEIC RSEDLPVSGV KAALQERIIQ LLNQFVQRGD
     ANAIQRLRYR IYNHGQTPPA TPHQPQIPDY PDSVSPVNSV TLPNHHRPAA VMNLPPRPRA
     PLYQPRFSFK SSPFYDIDEA LAPTIELQVL PNNRTSTSAS VQLSTEVAAR LKADSSMRVM
     LFSAADPVLA PYAAADIAFP HQLEVRVNGD EVKSNFKGLK NKPGSTRPAD ITDLVRKIPN
     YNNSLQVTYA LTQKASGERK FHMVVYLVRK HSVAELSQRI SQVFSKERVI NEMISRARDE
     DIVIESQVVS LRDPVAGIRI SMPCRSTVCS HNECFDAISF LQLQEQAPTW NCPICNKTIS
     YEALAVDRYM QDVLDKTSSS TDQARLYPDG TWSPGTADKT KTGATSLNRS TNGVSAPPQD
     DSDDDLVEIV APPSMKKEES MTPLHNVNTP PVSSREPSAA SAVPGSNRGK RKQEVIDLTL
     SDDDEPPRPA KRTNSAYSTP NSLPDRPFRL PPLAHNAYPT HPTAPVTPSD YRQDQTANRP
     PSSLGPAMAS RPRHSVNGTF STPNNHHYYD SNQHWYNSNR TR
//
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