ID A0A0V0RXB2_9BILA Unreviewed; 1527 AA.
AC A0A0V0RXB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 35.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=NFI1 {ECO:0000313|EMBL:KRX19133.1};
GN ORFNames=T07_3083 {ECO:0000313|EMBL:KRX19133.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX19133.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX19133.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX19133.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:KRX19133.1}.
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DR EMBL; JYDL01000063; KRX19133.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00181; EGF; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1527
FT /note="protein-serine/threonine phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006868148"
FT TRANSMEM 887..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1084..1104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 221..259
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 333..371
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 652..825
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1323..1481
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT SITE 1389
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT SITE 1427
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT DISULFID 229..246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1527 AA; 174358 MW; 7AEFF2BD94DE4E81 CRC64;
MIKPTISLYV RLTLIAWMCA RCLQFSTADN TGHLNQWRTL LSSRSRLVST EHHFHCSRPD
PFLNYQFEII TRSYTGRLGT IYVEQMSSNG TPFRLELFLQ HRKFHLQLVV DNHPLATLQH
ALTDFSDGYP HHISVTLGCS TGELGLSVDD ELVQTVLVDH HHHFNPITAP LDHLKVQIKF
GYDSNPSMKY IPAIVGCIRG SIFNNESEIE SHSSDVENGC VDHCKTNPCR NVARDRCVNL
FGNLRCNCLY SGFQGMRCES QGVPIRPIDS NFKNYSFSSF PGFVGCLKNF YVDFTNVLWL
SKVAGQKQLI SNEQLAYGCG EIPTLWSYKF VVNHSACDTR RCRHHSSCID DGKNGARCSC
ATIPYVGSLC QFFYVHCTMD DELNHGWTIV EHNFEESMQI RSVWAKDTTY IISYSFPTYT
WFRSATMYGN FSTLISEKNA CFCYANKTCA KAGRCNCDGN DLNSHVDAGY LVNHQAGLIE
MTFIQHRPRK GWANVALGPL ECRGSDLEEA IQFFGSGTII EESSWKGTNL EIWFKTTNSE
KAILINQEAD DGRFFRILLN KGTVVDFQFD FNIRRDQNYG MKTVTLEDLM NVGSSYTSNE
WNRIKVENID SEIFFVFNRK QAFYKLADNE QLDRTTFDKP LMIGGNINEQ SDVSFQRKDN
GFIMYRDLQQ NPLVEQIVLS FRTDQESGLL LYAHDQFYNF IQLHLWESNR LSLTVNSDRE
VKQCTAIGKT SKTVIPPRPP VPPNNISNYT LTYVGGLPSQ AFYNGRKKRQ AVYATKLQNY
LGCMRGLRIG SDDVDLKKAG ERTTDSQRRF RLYSINNEDV HLSPCGLTIE TLQPLTTSAS
LTMPAWDRLL ETRIYADNIE LEDVSTTHLT TPLNENDFAE KSDGESAGIA VGFIIFISVV
VVLVFAVLLW RKVQRKSYIT HEIYEDEDDF SELDDGKFQN QRCCCHQPET AEEHESGGLN
AATDYSSSQC VNNVSPPDEM DKLNDDSQDI VISPKNFGSY ECSSGDLKYM DENVNRLSRE
YPPAAPLQQN QIADQEQQHN RRLVAVSPPK LEVLNNHVPV AWISIRLLLA VLMLDWPAPD
VVNLTSLCAV VWCSFSTCLT WNWTCMATNI CHWKNLKFGP FCRVRLGRVR IVNNYRRPVA
GRPVRTALAL GRRSPMVVHV KGRGRRHVGR RGLHLEPGRQ LDRWHRYEDR RSGIIFYWQR
SCRRRLRRKP RRRRYVQATS AAANNNNNNN NTNNTAGPVR VLWPFFQNRR TTTKKNRCEV
VERKLRVPKV FRGLFCCFGL KPVESAAPLQ SEFQNSHFTS RHSENNVHAS SSERLLLPPV
HPSDVNKKCL IVDLDETLVH SSFKPVKNPD FVIPVEIDGV VHQVYVLKRP YVDEFLQQIS
ANFECILFTA SLAKYADPVA DLLDRWGVFR SRLFREACVF HKGNYVKDLN RLGRDLKHVL
IVDNSPASYA FHPDNAVPVQ SWFDDLHDTE LLDLLPLLDK LATADNVYTV LKGSNRRSTS
PVLYHYSECN GAYDPLGVIA QVEQKPL
//
