ID U6GCE7_EIMAC Unreviewed; 1217 AA.
AC U6GCE7;
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:CDI77815.1};
GN ORFNames=EAH_00027200 {ECO:0000313|EMBL:CDI77815.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI77815.1};
RN [1] {ECO:0000313|EMBL:CDI77815.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI77815.1};
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:CDI77815.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI77815.1};
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; HG670746; CDI77815.1; -; Genomic_DNA.
DR RefSeq; XP_013251887.1; XM_013396433.1.
DR AlphaFoldDB; U6GCE7; -.
DR EnsemblProtists; CDI77815; CDI77815; EAH_00027200.
DR GeneID; 25270790; -.
DR VEuPathDB; ToxoDB:EAH_00027200; -.
DR OMA; EIVIRCC; -.
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); 1.
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; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 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; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 413..500
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 58..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..410
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 133400 MW; 0CAE27AB0AE683F6 CRC64;
MRTLEELHCH TVAELSAACR ALGLPVKGLK KDLVSRLMAF EKTRGPLPPE VLHRRPLQRQ
RHPQPPLRQQ QQQQHVSPRQ VYIQPGGPME EPSAANYHQR AKHHFLQYQQ HQQLLLQQHQ
HLQHQHLQQH QNVQQEQRHG GVLPPSQPAS QAASQAATRH YSGPQRPRNA LASSHTRKEC
ICGDRLSPQQ QQQLLQQQQP LIGCAVCGAR CNQRDSTNKE VSALLLMLLR CMLLQHRVCY
GLSEDRNPAD FICGACHLKL MDPFYPPAQV FALSPLEDSL AVSLDATDIK GWRAQGKEIV
IRCCQAQTPK HIQTWPRTVE VFVNGRITQY LRSGLNQVEV KTTNFTPDPK LFFIALLLVD
TKTPEALEAS VVQQHTLPLD AAKERVQRLL QGQQQKQEQQ QKQEQKQQED VDSDEEVQCL
EVGRRLKLTC PVTFTRIEIP CRGRFCLHLQ CYDLSGYLLV SRSTKAFNSR WRCPQCHLTV
LPSDLQVDGF FQLLLAQTKE EDIEVELQAA LLVLRWDAGG GSNWEISDSE AEDAPAAAAA
AGSAAAAAAS GEAAAPCQDS AGAPREVAAA GFPRRPPAAS GSSSSNSSSG ASDEEEDGPL
TKRQRRLDPS PGSASNQQRE VFCLSDSSDD EQSHQQQQSG ASTSASNGPT GDRERHTSNE
QLQSSQHSQQ QQQHPSQSQL LPESQQQPTQ CQQQLQQATQ SQQQQLQHQK SDGGGGEVNA
PIALDSDTDE EEKQRQKPSQ QQQQWQRSSQ QQPPQQQPTQ LQPSQQQQPQ QALFPKAPRE
DGAAQRASES LSDAVAAREG TSAQHATSSS SCSDSGGSST GSQGSNSSSS SNSSKGRGGG
DSSMCAPALA SSGAVASGAL SNSSRSSSRS SGETAQDMPL GFASEAAALL EEIDWSADGV
KPDAGQSHAA STPAVAAESA AAAAAAAVPP AATVGAAPTA DDAAPLKKAG AGAAAMPANY
TQADQGGNES QAATAEGSSQ LQEEQQMQKQ QQQQLLQQQQ QQQQLQYHQQ QQQQQPFITE
QGLLALQQRC QQEILLRQRE ALLRQQQQQH KLQLEHQQGQ LLLLQQNSFS ALQRHRLLLQ
QQQQQQQTAV QSIGAPWFLN TLVPGAADNS SPATPRSWHG GAQQPQVQQQ QIPQQQQLPQ
QQEVPAQPQL QQQQQQQVPH HIQLAARLPQ LFNMRNIPSS AQATVRHLLT TAQGQAEEFA
RQQQQQQQQQ QHRSLQN
//
