ID A0A0V1CXG3_TRIBR Unreviewed; 2970 AA.
AC A0A0V1CXG3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
GN Name=MPP5 {ECO:0000313|EMBL:KRY53912.1};
GN ORFNames=T03_15817 {ECO:0000313|EMBL:KRY53912.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53912.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53912.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53912.1};
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:KRY53912.1}.
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DR EMBL; JYDI01000077; KRY53912.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CXG3; -.
DR Proteomes; UP000054653; 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:UP000054653};
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 378..434
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 466..546
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 561..633
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 702..885
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1038..1093
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 1796..2017
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 960..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2754..2797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1366..1393
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1188..1206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2761..2775
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2970 AA; 338609 MW; D7A9DFA69EF13ECE CRC64;
MRLRPAKASQ TDNILQQRRS TTSSPVADYF GWWSNRGQAM SIEISDQWSQ VASYIQTESI
TFHTFKRSRK STRHIDTCPT VDLQSDAYKK EAIISKQAVL NLEIMLKDNE NRLGFSMDNN
CRPMVINHVT HGSPAYRHGI RVGDEIIEIN GDNVEKMNTN QLVQLVHQCF PSRVVLLKVR
RNIIGGELLL MNSTDVAQTN LDCSQATMQR GIVVNAKKQP PVHIDQIAFP LSTTKATMTA
ASSTESCSEE ADSRLERLKR YGQDLQKRKD NEERHAKEEK LLRNSLRGSK KLNALKKTST
QTIPLVNGSE NEAFSADKKR NTCWMTFSSL TIITMTMISL IRRIILSRLW LMSTSIHLHK
WFLKKLSVAR QPEKQNYLGK SSPSAMDCLT EITRQLGDSI SDAAAELQTV LDKPYFKTLL
AVHDQTVEFI DRTPTTDGSQ SWRLSGCLGL LETMLTGEKG GDNLRIIRLI RDGDLPLGAT
VKNDGEAIVI GRIIRGGVAE KTNLLHEGDE IIEVNGVDLR GKTVHEVCDL LCNLFGELTF
IIVASRRSDT AVDNNNAIAP KGVKHVRALF DYNPEEDVYL PCRELGLGFN KGDILHVIST
QDPNWWQAYR EGEDSAQTLA GLIPSVSFQI ERENYIRELT TDSGKDSCAK HRAGLLFCAK
YPKTNWFRFK LGRSFDLKME PFEKEIPTYE EVSLYLSRTG RRRPIVLVGP PHVGCFELRQ
RLLENEKDKF DGTISHTTRL RRFNERDGFH YHFVSRQEFE EDVLARKFVE WGEYQKHLYG
TSFVEIRRVI ERGKTCVLTL KPQVSIRAIR NSDLMPFVVF ISPPSLERMK LNQRRQANPT
LKDDELKAIV TEAKEAEEKY GHYFDLVVVN YDLEHSYQEL RTAINRLETE PQWVPSFWLK
NPSLFNGRTM SSEKGCNLQE ASRCNQTDSE CFKVPFPVAP VGETESSVKI SESVDTKFQN
STSVTLDDHS TEHFSPPPPT ATSNDIQNEN KTIAERNASS LPYKIPAWSG HPEELLYSFE
VLKQGCMIGK IDLNKPYISF GRAEYVDVQL EHPSISRCHA VFQYRAVGES HQLGWYIFDF
GSTHGTFLNK EKIPPFMYMR VKVGHMIAFG SSTRFYILQG PEWDEEPESE FTVTELKQRV
ERQKALIDTS RKGKDVVESK AGSLQAEFHD SPALDRGIDW GLSDYGEDDH EQQEDSEGEE
SEDGEDIDFE HLEQREQYYK DDPKKVLKKF FDREGHELVY DCSEKGPTFR RTWCCRIEYC
NSNVQRLPIE TSTGKPVFAE AVVSGAKKDA IFQCALEACR LLDAHDVLRK SSQIGRGRKK
KDWKSNDYYD SDEDEFLDRT GEIERKRAFR YEREMKMNTR SKVDNYNTLM QKLESLDADI
ERTKIQLKLL AAEAEKGGEV AVQPGRDSLD EFLANMTRCD LQNVKVKQSQ LRTRLGALEK
QRARTALLVK VAKPAEMPAF KRLLVDKPSD CGPTRTQNVL VGRMGGFGRK EQMVLPVFVQ
KLPESTSDKF VEEVEEEEEG GGGGEEEKKE EKQDEVKMGK STKTLPELDK KPLNEEKPTS
SKRPFIEEDE QESAANADQP SERRFKRSFV FPYGTGPEEE NFSEWLPPEN MDESAEFCEI
ENVSFENVHS DDLAEVCCST ASSGSNLLKR KLSGDQLENT EPYEKRCSNG KMINETMKEM
EFKEGPEFGI QDQGMAVPHS DHHTLPDWEM EKMEIIEEVK WFPPSPSPLA LDLKLDEKCI
KIGRRVKDSR QEDSYFKKNI LNDLLLAKSE LHNIKDWRLR SARSRANPFE LIKSAIFQNR
AAIKLANLDA LVDFQLTDPK DADGNSIVPN VAEYPELFYF ADVCSGPGGF TEYVLWKRGW
NAHGFGMTLR NDCDFRLDKF TASSPVMFEA FYGEDGINGD GDITKGSNLE SFSNFVLKNT
DQKGVHLFMA DGGFSVVGEE ILQEVLSKRI YLCQSLCGLL VLRKGGTFLC KFFDTFTPFT
VDLICLLWHC FDKLTLHKPH SSRPGNSEKY VIGIGFRGNC KQISDYLIKA NLMFDTFKAD
EDILQLLPSN FVQEANEFMS HFMEINEQLS ARQISFLKKY KTFSENRTLR DNRQQLIREY
CLNLWKIPDE SAKNFTQSAE MIFKLLSPRN ASWLLEKRIK VDASWLQRLN IVQHLVVASF
GEATVLIAGG NNLYYFHEKE WKEFDCVEAY LPNNTVVFGS FTRCYSTAAS SSSCSIESNN
IKLTEKVSLF RIIDAAWLGD VNVENFPYQQ RLQLVAKFCK AIDKRYSIPK ALHFEAAPLL
TPLDVVHLLQ HQVRLMLSEN GHWILAKQST VFPDYFIPVQ TLMFVSKMKF ENPFDDSSKE
KNYSNFQNFR EMFVDRIAVQ FYENDGDSCL NGDILENGRI TVVRAVCPNG ISDEQMLSCL
HPIEESWQRI RSRKVSLDKA MLQVLFLSRV ETRQLCAKLE QARLRCSFDF ARCSSSNDAL
RLVQTGLQFA CEHKNPLWHN CTQAVMRNHG QCVLQLTRRD NPAEQCQSLA EFYTCIQEPL
QAQCGTGAVA ELVKLIDIQS CSLESLLESS AQSDSRQCEK DDREAVDECF EPLENYWRLL
RVKDHKLNTI GFPLYTFRAH ELEYMCDTVH QIKASCTAVQ RCPSRPVVQF ANALLGYACG
SEQDAFFAHF QCVRESIQSA GQCWHYLQGA WEPGFHREVC PRMPAFFRCI LPQLGRKCST
EAISTLVQSI RQYWCDVGTI ADVASAIQDS GIELDDRLAL LAFGSVKSQK KVTEVSVEQQ
VEENREDDDD EEEVDVNEQH HQPADADSSN NEDGCAPTRQ KRVRDCLAPV FERLVHLHRT
HRLENLSLPL YHYGKAEILD LCDLYATAFL QCPFSWFQDC ADDAVVSAAN SLLGYFCSPQ
HINAFHEHYD CLSLVIRNRH ACSKHLLGSA PGQDELDHND DQTPKRGASL SCGRVKQFFN
CARLAVDRGC PQAASNVFKQ SLQQFGCQLD
//
