ID A0A0V0X0G0_9BILA Unreviewed; 1248 AA.
AC A0A0V0X0G0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Anaphase-promoting complex subunit 11 {ECO:0000256|ARBA:ARBA00013928};
DE AltName: Full=PAX transactivation activation domain-interacting protein {ECO:0000256|ARBA:ARBA00030146};
DE AltName: Full=PAX-interacting protein 1 {ECO:0000256|ARBA:ARBA00023858};
DE Flags: Fragment;
GN Name=Paxip1 {ECO:0000313|EMBL:KRX81421.1};
GN ORFNames=T06_879 {ECO:0000313|EMBL:KRX81421.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81421.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81421.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81421.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
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:KRX81421.1}.
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DR EMBL; JYDK01000031; KRX81421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0X0G0; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR GO; GO:0000931; C:gamma-tubulin ring complex; IEA:InterPro.
DR GO; GO:0097602; F:cullin family protein binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0033566; P:gamma-tubulin complex localization; IEA:InterPro.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd17711; BRCT_PAXIP1_rpt3; 1.
DR CDD; cd14524; PTPMT1; 1.
DR CDD; cd16456; RING-H2_APC11; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 4.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR022214; MZT1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR044596; PTPMT1-like.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23196; PAX TRANSCRIPTION ACTIVATION DOMAIN INTERACTING PROTEIN; 1.
DR PANTHER; PTHR23196:SF37; PAX-INTERACTING PROTEIN 1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF12554; MOZART1; 1.
DR Pfam; PF12738; PTCB-BRCT; 2.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR SMART; SM00292; BRCT; 4.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52113; BRCT domain; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50172; BRCT; 5.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 31..183
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 104..172
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 176..244
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 256..320
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 693..779
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 791..864
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 934..1015
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 1161..1204
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 448..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1248
FT /evidence="ECO:0000313|EMBL:KRX81421.1"
SQ SEQUENCE 1248 AA; 141391 MW; 3C9CEFC8906B20D9 CRC64;
MAMGLLSWAT FYSTLSYNLL RNRLSETDWP WYSKIDETVI LGALPFKSMM NELIDKEHIG
GVVCLTEPHE IEHRWAAAKD DWEARGVSYF WLPIRDFWYS TSLENVREAV KFIEECEQSG
KKVYVHCKAG RSRSAMIVMC YLMQKHGWYS TAAHALLKSK RPRIVLWHDH WLTIEQYAKT
FQLKVYLVPR TVEESRAEKV RKILTENGAR LSSYLTDSVS ILIADHPDSS EVGEARDIYD
IPVVAMSRHD ANILWSIIVS LGGECERVLT SRTTHLISFL ISGNKYRIAS VNDSIRIVIP
QWVVDCAEAG ELLSVEQYHP SNFVQENSAD ENDMKAEQEI QNLAATLKME AQQHHVAMHQ
QQQHAGMNVS SPAPGVSPAC GFNPSVDRCY QLSPEMGANS PYQQMGPRIS PQQRFWYSNN
VQPPFPVQHQ TQMHGSPQQM QMIRPQQMPV SRRQSDTPLM SPSGNGSPLG SPNPTFISHS
QQQYSASPMQ AHHQQQNSFG GGYQHEMQLV GAPQRQVYMP QQNQLHQNHG QLIQQQQPRF
SDSTPPNYSS AAEYAGNAAV QLQQAKKMSL QQQQETTPID ASLHRQQFVP TTRINQGSFP
NSNQIQMQAH CQLRHGFQRV SYPGYALPLQ TSTPATISLP SGQRPTVPSY PQPYQVMQVA
GSQIPNERFQ SRNFQQPYSP RMGTTSLKES RIPPELCLVG CVFLIVDYER TLDQKEVSDW
RIVINLHGGD VEIMYSTKCT HVVCESLRHP VVQQALRDNK RCVTAQWLND VIMNKKLLPP
WKAIHFPSFF GDNKPCKGKI VAVSGFPVKE RSCLKQMILA IGAHYTAYFS RHNHLLVAKT
YCGPKVMKAA EWKIPVVNLQ WLTEVFFGQT TALQNINNAK YHQFVPKELS LQPNFDPFRI
DTATAMPILS PPPADADIQK RCAELAKCGK NVAEVRICFT GLYQAEVNHL EKKVLWLGGK
VVQLVSECTH LITADLKRTR KLLEGISLGR YIVSPIWIRQ SYKQQQFIGT QFVVIACDND
LHICQALLDA GVVQFAYRRA ENVGKCSKKH LPQNPLFVID DADLGGLHRI AKLLKVDLDR
ESLAICVRLI EAGVDPERLA IVVLRKMHEQ EQQQEEENNP DDSTVTGLKV TILNWNLIST
WQWDTQDPLC GICRNSFDFP CPDCKVQYDQ CPIAWGECTH CFHEHCIIQW HSTQADVKDC
PMCRQPWVKS ADVTETPPRT PESLAAFNLS PSTGIAFVDE SSKATILY
//
