ID U6JVY6_9EIME Unreviewed; 1227 AA.
AC U6JVY6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Protein inhibitor of activated STAT protein, putative {ECO:0000313|EMBL:CDJ28222.1};
GN ORFNames=EMH_0000480 {ECO:0000313|EMBL:CDJ28222.1};
OS Eimeria mitis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=44415 {ECO:0000313|EMBL:CDJ28222.1};
RN [1] {ECO:0000313|EMBL:CDJ28222.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ28222.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ28222.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ28222.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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}.
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DR EMBL; HG681084; CDJ28222.1; -; Genomic_DNA.
DR RefSeq; XP_013350796.1; XM_013495342.1.
DR AlphaFoldDB; U6JVY6; -.
DR EnsemblProtists; CDJ28222; CDJ28222; EMH_0000480.
DR GeneID; 25375156; -.
DR VEuPathDB; ToxoDB:EMH_0000480; -.
DR OrthoDB; 20246at2759; -.
DR UniPathway; UPA00886; -.
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 CDD; cd16650; SP-RING_PIAS-like; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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 7..41
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 354..441
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 57..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1095..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 133063 MW; 99CBD64FCD0B640C CRC64;
MRTLEELHCH TVAELSAACR ALGLPVKGLK KDLVGRLMAF EKTRGPLPPE VLHRRPLQRQ
RHPPPPLQPQ QQQQQHVSPR QVYIQPGGPM EETSAANYHQ RAKHHFLQYQ QQQQLLLQQH
QHLQHQHLQQ QQHLHQQQRH GGVPPASQAA SQAASQGATR HYPGPQRPRN ALSSSHTRGA
GATGRECICG DRLSPQQQQL LMQQQQPLIS CPVCGARCHR VCYGLSEDRN PADFICGACH
LKLMDPFYPP LEESVAAPSW EHKRRDTPIV ITQYLRSGMN QVDINTTNFT PDPKLFFIAV
FLVDTKTPEA LEASVVQQHT VAIAAAKERV QRLLHGQQQK QEQQQQQQQD DADSDEEVQC
LEVGRRLKLT CPVTFTRIEI PCRGRFCMHL QCYDLSGYLL VSRSTKAFNS RWRCPQCHLT
VLPSDLQVDG FFQLLLSQTK EEDLEVELQA DLSFRVLSDE ELKAESKRAE QQRQLAAEAL
LKPKGEETET TGKVAFEVVD MLSDSDAEDT AAAAPSSSGA AGVATATPAA SGEAVAACQD
PPGAPREGSA AETLQRPVAA AGSSNSSSSS NSSSGASDEE DEGPLMKRQR RMDSLSMDAN
NQQREVLCLS DSSDDEQQPQ QQQQQLQQQQ QQQHNVAGPA VNDGQGGGGA RHTSNEQLLP
SQHSQQQQQS SQSQQLQQLP PQSQQQQPTQ SQQQLQQPTQ SQLQHLQQQH PDGSGGELNA
PIALDSDSDE EEQQQQPSQQ QQQWQQSSQQ QTQHSQPPQQ QASQQQQQSL LPRAPCDEGG
TQKADAAGEG TVAQHPGGSS SSSSSNSGSS TAGSHGSNSS TSSNCSKARG GGDSSVSAVG
PPSGGDAASA AISSNSRSNS GEMAQQDMPL GFVTEAAALL EEIDWSADGG QPEAGQAQAA
STPAAAADSA ASPAAAPGAA AAAVTDAATV AAAQAAAAAP APAASAAEDA VALRKAAAAA
AAFAAAAAAA ANYAQADRGG TGSQPTAADG SSQSQQQHQQ QQLLQQQPLI SEEGLLALRQ
RCQQEILLRQ HEAIIRQQQQ QHKLQLQQHQ GQLLLLQQNR YAAMQTQQLM LQQQQQQQQQ
QQGAVQPVGA PWFLNNLLSG APGSSGPATP RSWPGGQQQL QVEQQQMPQQ QQMPQQQQMP
QQQQIPQQHQ MSQQQEVPAQ LQQQPQQQQV PHHIQLAARL PQLLNMRNIP SSAQATVRHL
LTTAQEHADE FSRQQQQQQP HHRSLQN
//
