ID A0A0V0S4Q9_9BILA Unreviewed; 2417 AA.
AC A0A0V0S4Q9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
GN Name=MPP5 {ECO:0000313|EMBL:KRX21673.1};
GN ORFNames=T07_7339 {ECO:0000313|EMBL:KRX21673.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21673.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX21673.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX21673.1};
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 -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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:KRX21673.1}.
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DR EMBL; JYDL01000037; KRX21673.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR CDD; cd19856; DSRM_Kanadaptin; 1.
DR CDD; cd22677; FHA_Kanadaptin; 1.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 2.
DR CDD; cd12036; SH3_MPP5; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.12760; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR035601; MPP5_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR PANTHER; PTHR23122:SF14; PROTEIN PALS1; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 103..166
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 368..424
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 491..571
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 586..658
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 727..909
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1069..1124
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1820..2041
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1389..1416
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1219..1237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2417 AA; 275565 MW; F834EDA38185BF3D CRC64;
MRLRPAKASQ TDNIFQQRRS TTSSPIADYF GWWSNKGQAM SIEISDQWSQ VASYIQTESI
TFHTFKRCRK STRHIDTCPT VDLQSDAYKK EAIISKQAVL NLEIMLKDNE NRLGFSMDNN
CRPMVINHVT HGSPAYRHGI RVGDEIIEIN GDNVEKMNTN QLVQLVHQCF PSRVVLLKVR
RNIIGGELLL MNSTDVAQTN LDCSQATMQR GIVVNAKKQP PVHIDQIAFP LSTTKATMTA
ASSTESCSEE ADSRLERLKR YGQDLQKRKD NEERHAKEEK LLRNSLRGSK KLNALKKTST
QTIPLVNVLD DIFLVDNNNH DYDKLNSKNN TVSIVANVDQ YSPSQMVSEE AISCAVKFLS
QSEKQNYLGK SSPSAMDCLS EVTRQLGDSI SDAAAELQTV LDKPYFKTLL AVHDQTVEFI
DRTPTTDGSQ SWRLSGCLGL LETMLTGEKG GDNLRIIRLI RDVLKFKFTR RLDSPTCGHF
APPPERLKPD KVNFKKKTGA ATGATVKNDG EAIVIGRIIR GGVAEKTNLL HEGDEIIEVN
GVDLRGKTVH EVCDLLCNLF GELTFIIVAS RRSDTAVDNN NAIAPKGVKH VRALFDYNPE
EDVYLPCREL GLGFNKGDIL HVISTQDPNW WQAYREGEDS AQTLAGLIPS VSFQIERENY
IRELTTDSGK DSCAKHRAGL LFCAKYPKTN WFRFKLGRSF DLKMEPFEKE IPTYEEVSLY
LSRTGRRRPI VLVGPPHVGC FELRQRLLEN EKDKFDGTIS HTTRLRRFNE RDGFHYHFVS
RQEFEEDVLA RKFVEWGEYQ KHLYGTSFVE IRRVIERGKT CVLTLKPQSI RAIRNSDLMP
FVVFISPPSL ERMKLNQRRQ ANPTLKDDEL KAIVTEAKEA EEKYGHYFDL VVVNYDLEHS
YQELRTAINR LETEPQWVPS FWLKNPSLFN GRKYLLMLTT MSSEKGCNLQ EASRCNQTDS
ECFKVPFPVA PVGETESSVK ISESVDTKFQ NSTSVTLDDH STEHLSPPPP TATSNDIQNE
NKTIAERNAS SLPYKIPAWS GHPEELLYSF EVLKQGCMIG KIDLNKPYIS FGRAEYVDVQ
LEHPSISRCH AVFQYRAVGE SHQLGWYIFD VGSTHGTFLN KEKIPPFMYM RVKVGHMIAF
GSSTRFYILQ GPEWDEEPES EFTVTELKQR VERQKALIDA SRKWKDVVES KAGSLQEEFH
DSPALDRGID WGLSDYGEDD HEQQEDSEGE ESEDGEDIDF EHLEQREQYY KDDPKKVLKK
FFDREGHELV YDCSEKGPTF RRTWCCRIEL PIETSTGKPV FAEAVVSGAK KDAIFQCALE
ACRLLDAHDV LRKSSQIGRG RKKKDWKSND YYDSDEDEFL DRTGEIERKR AFRYEREMKM
NTSSKVDNYN TLMQKLESLD ADIERTKIQL KLLAAEAEKG AEVAVQPGRD SLDEFLANMT
RCDLQNVKVK QSQLRTRLGA LEKQRARTAL LVKVAKPAEM PAFKRLLVDK PSDCGPTRTQ
NVLVGRMGGF GRKEQMVLPV FVQKLPESTS DKFVEEVEEE EEEGGRGGEA KKEEKQDEVK
MGKSTKTLPP ELDKKPLNEE KPTSSKRPFI EEDEQESAAN TDQPSERRFK RSFVFPYGTG
PEEENFSEWL PPENMDESGE FCETENVSFE NVHSDDLAEV CCSTALSGSN LLKRKLSGDQ
LENTEPYEKR CSSGKIINET MKEMEFKEGP GFGIQDQGMA VPHSDHHTLP DWEMEKMEII
EEVKWFPPSP SPLALDLKLD EKCIKIGRRV KDSRQEDSYF KKNILNDLLL AKSELHNIKD
WRLRSARSRA NPFESIKSAI FQNRAAIKLA NLDALVDFQL TDPKDADGNS IVPNVAEYPE
LFYFADVCSG PGGFTEYVLW KRGWNAHGFG MTLRNDCDFR LDKFTASSPV MFEAFYGEDG
IDGDGDITKG NNLESFSNFV LKNTDQKGVH LFMADGGFSV VGEEILQEVL SKRIYLCQSL
CGLLVLRKGG TFLCKFFDTF TPFTVDLICL LWHCFDKLTL HKPHSSRPGN SEKYVIGIGF
RGNCKQISDY LIKANLMFDT FKADEDIRQL LPSNFVQEAN EFMSHFMEIN EQLSARQISF
LKKYKTFSEN RTLRDNRQQL IREYCLNLWK IPDESAKNFT QSAEMIFKLL SPRNASWLLE
KRTKVDASWL QRLNIVQHLV VASFGEATVL IAGGNNLYYF HEKEWKEFDC VEAYLPNNTV
IFGSFTPCYS TAASSSSCSI ESNNVKLTEK VSLFRIIDAA WLGDVNVENF PYQQRLQLVA
KFCKAIDKRY SIPKALHFEA APLLTPLDVV HLLQHQVKLM SSENGHWILA KQSTVFPDYF
IPVQTLMFVS KMKFANPFDD SSKEKNNSNF QNFREMFVDR IAVQFYENDA DSCLNGDILE
NGRISCLQTF QNAVQKA
//
