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Database: UniProt
Entry: A0A0A1UDM6_ENTIV
LinkDB: A0A0A1UDM6_ENTIV
Original site: A0A0A1UDM6_ENTIV 
ID   A0A0A1UDM6_ENTIV        Unreviewed;      2528 AA.
AC   A0A0A1UDM6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   08-NOV-2023, entry version 45.
DE   RecName: Full=DOCKER domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EIN_359320 {ECO:0000313|EMBL:ELP90849.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP90849.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP90849.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP90849.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   EMBL; KB206483; ELP90849.1; -; Genomic_DNA.
DR   RefSeq; XP_004257620.1; XM_004257572.1.
DR   EnsemblProtists; ELP90849; ELP90849; EIN_359320.
DR   GeneID; 14889866; -.
DR   KEGG; eiv:EIN_359320; -.
DR   VEuPathDB; AmoebaDB:EIN_359320; -.
DR   OrthoDB; 23305at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08679; C2_DOCK180_related; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR046769; DOCKER_Lobe_A.
DR   PANTHER; PTHR23317; DEDICATOR OF CYTOKINESIS DOCK; 1.
DR   PANTHER; PTHR23317:SF76; LD20667P; 1.
DR   Pfam; PF06920; DHR-2_Lobe_A; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680}.
FT   DOMAIN          495..671
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          2072..2520
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1131..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1486..1527
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1136..1174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2528 AA;  293773 MW;  F2FD68C436E2857D CRC64;
     MEHQLDTSVL SQIFETDFRK TKVVMATPER GSNPIQKTET SLKILSKFDL YDTENNKELD
     VYQLRKYIEG EWKICLSEES IKYHCGQNFL EKAYKVQRNE FIAFHKYITA NLEEIKKENT
     QSDLEVFESQ FTEDSPVDSQ YKLLDKNCFV IEKLDKFHSI MYPDLIPPEK GDPIHCDMYN
     VIFGKTISIY KKHIPFRSVF TTIPDNFVPK NDNLKKLFSI DSLFQSITNK VGQRRKKAKN
     FFEFFDKKIS HTDFLYSTNL SNARDEDIEV LKKYKKPSVI EMVNIKLPLN IEKLHCRLSF
     YDTNYIKLSA DYCFNVDPSD LQASTLNVPL SSFVMRQEII NKSVAFIVVF QVFKAMDADI
     SFAREVYAND NKRDAKNVKK YSDRVKESAK FFEQKKYQLL MFSSKQILFT GNYELFKLYK
     PPNEVKDIVW MIKECDKWKL CGEWTFKFKA SKKELVHVDG ESEFNNQEHE EKPIFIKSLT
     NLSLQDSEDI FTDYRNFLFC YPTELCLGKE RKRGGCLITV YCRDTDAKFA GEITGNLPVI
     FPNNSSCHVD MQTSLTTTVA TEKVGKFTDE IKLELPFPLT PTHHLLFCVR DIGTDDGVEG
     RPLFAKLPLY ENGRVVENKE YTLRIMKEMN DHYLKTNEYY DQSKMYLKVT INVVSTVYPT
     ERVLTDFLYF NAPVDTVLYP DLYTEMIHFL PSVLHRCLRI LQDRNREEIF SMFKLFKVFD
     VNKNVEEEKK ESFSVYKNKN VVYAINHFVR VKTDENVYNC MFIVASLPII FDRSETNATE
     RLKYIWIIFA LLIKSLIAFY NDHNAFNLPN FHTFCCGEDA KIISANLVKN IDMCSDFIVY
     CSALSFVDPL VVREANLFYA EFIRDFAMLW RHDDTTKLVI SHLDNICKMS RDVIGRSSSS
     FSRLLRLEFI SVLAEGDHIF QLNGPQNLEV KGINKLNDTI AQRHTLMFII LRQFFVLILD
     QDKLISKMAL HELVLLMNKF DLDKSLSSQH DRERFFGMMF PFVLFFLDDS EKINEWRKKD
     CTSDLNDIEC LYMIFFFILK NLEDNLLDQW LVAEYLPSML NTLLVHIRKA LLLFSVFPMQ
     TLPDAPKLYL KELQTLLNSI ETQSAPNIAR SPSPGLSKIG SSLKMHVKNN SQNKRLSSKY
     KKDDDVKEPS TPRVGLDRLK LKKYDDDEEG RRSVSPRGSG SGAAMEYAKM SATPVFSNLS
     CSAGARTITV SSCETADPNV LNMITDVSLI AMDYLEIMIS VLIRDDKTQA MDRIQEIVSD
     VLFKIKTTPS YLVSLYKFIF IVLTTYREFL FLKPNQMCIN LLKNLLSLSN SQEVMERDFA
     NNLLFTFAKT NFIVTGNTVS TIVSAISALS ELNLANVQNV KTSVKGLLEL SSQYHYTFDL
     KLQRCVELLL DEGSRKIEAL QKVQQIYRAI DGGNLDVFIT FVKDCMLVFE DIIEFATTAN
     TTVINGYDVF KSEVGGLLKT NEIFKMVGKW IIFIEHIQLC PKDSFYLFLE EKKKELRNSY
     THLEETIVEL EKLCVTEKEQ MKRFEKQCDE NKTVGNRLFT WVKTNLQVQA IDYDTCEDSQ
     LINIIEDLEK EQNKRVNGIK SHIEKYCQFD EVLKEMGLLV NPLFPVTSQE MGECVKKVLQ
     LHQNRIKLVH QLIHVRTSYD TEYLIYTEKL KHFEKTLETM NSDIAVEISS KPITGHFLED
     SMYRYKMLDD LFSTCSKKLN AKKVKMGGMK PTWEITYNGW EDVISLVLST LELTTNLLEK
     VKQNDYEVIA MKEWYLKETK FNKTIIGVFM WDGMYSALNK VAMKESNDFL EILAGVYEYL
     STHLKDVETR YNECVDILQH LRKKKLPLGF KYLQKKINVK DFEMLAMSTE LYVDQFNEEK
     TLEKSRKEYA DLFVHFFKFT DKLCDDADKM QGLQNTKAVT GNTSITNLST YFKQKDHTID
     PKVLEEISKQ REKLLSFEEQ KIDKLNRYCD LTQITQTVLT RCSLLGLPDK EKEPLKISYN
     AKIPRSVSLP KSNNKLVELK DVLSFFMDSK DCIKLDCFHD LSYGQRDNFN KDLKNVEDDI
     LNVLDSLEDI NTQKRESSDP QLVLQRFEGF AMNYVAAPQL HLTWMTRLAQ QHRDRGQYVE
     AGMCEIHMVL FIHRLLENNT RTVDCSEFVA TFGNFVENTS TAPSSQFTAH FTEEMMIKHI
     SNAADDFEKG NIAWYGLVTA NVLIPYYIEK RTIKELGKTH DYVNRMYSTL VSGNSDHFGR
     DNLAFYYVQF VGKVFGEKLD GKKYIYVSTR NKMPMLIKEI KDVVPKSFKG ERHIISSLDK
     MNEQLAISGD AENQCHIVFS QITPLYEKGK FVQYASKFNF DCLMCDEGKD PTVITNWFKN
     RIVLETNLVL PGVLRRQEVT QKEQFYRMSA IEIAIDEIER KTEDLKFYLD ESFNFLKETD
     DESAKLIVKK TSEILCGSND IGNERLAPKL TVFEKKKLVE FLHIFFYELQ DENINSTVLT
     NLFNASKEAL AVVREAIAVV NETYRNVIVN ETTRSNIENI ERQADRVDYT LDEIENTMKS
     QLGEDDNL
//
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