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Database: UniProt
Entry: A0A0N4UP00_DRAME
LinkDB: A0A0N4UP00_DRAME
Original site: A0A0N4UP00_DRAME 
ID   A0A0N4UP00_DRAME        Unreviewed;      2460 AA.
AC   A0A0N4UP00;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Spectrin alpha chain {ECO:0000313|WBParaSite:DME_0000966601-mRNA-1};
GN   ORFNames=DME_LOCUS10718 {ECO:0000313|EMBL:VDN60745.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000966601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000966601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN60745.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826}.
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DR   EMBL; UYYG01001239; VDN60745.1; -; Genomic_DNA.
DR   STRING; 318479.A0A0N4UP00; -.
DR   WBParaSite; DME_0000966601-mRNA-1; DME_0000966601-mRNA-1; DME_0000966601.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR   CDD; cd00176; SPEC; 11.
DR   Gene3D; 1.20.58.60; -; 18.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR035825; Alpha_Spectrin_SH3.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF422; PH_9 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF08726; EFhand_Ca_insen; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 20.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM01184; efhand_Ca_insen; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 20.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 14.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1020..1079
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          2310..2345
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          2353..2388
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          954..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          344..403
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          767..794
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          916..943
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1196..1223
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1263..1304
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1685..1755
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        956..975
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2460 AA;  285518 MW;  1A35BA4CB8F2A123 CRC64;
     MIESSTAPPE PVLEVPPPQE IKILETADDI QLLSDVGGIG QESSDIISPS EILVSLIVID
     FDYQDFLFFK NRRSEVLGHY AQFKVYAKTK RDRLEDARQF QYFKRDADEL EIWILEKLQT
     ASEESFRDPT NLQAKIQKHE AFEAEVHAHS NAIAQLDKTG SDMIQHDHFA SEIIRKRLDE
     LHALWDQLFF KLKDKGIKLQ QALKLLQFIR QCDDVLYWIR DKEAFVTAED FGMDLEHVEV
     LQRKFEEFLK ELGNHHYRIT EVNQAADKLI EEGHTEQNTI YNKREEVNEA WHRLNTLAAT
     RREGLFGAHQ VQRFNRDIDE TLAWIGEKDA TLSTDDYGRD LNNVQALQRK HEGTERDLAA
     LDAKMNSLAI EADRLAQVHP DRADAISAKM NEAKDQWAAL KRKAQARKDG LDRSYNLHRF
     LADYRDLSSW INDMKAVISA DELAKDVAGA EALLESHQEH KGEIDAREDS FNQTAEAGQR
     LLDEDSEQSD DVREKLGHLA KKKASLLSLW EERRILYEQC MDLQLFYRDT EQAETWMTKQ
     EAFLANDDLG DSLDSVESLL KKHEDFEKSL AAQEEKINAL DEFATKLIQG QHYAADDVSR
     RRALLLERRR HLMQRAAERR RQLENSYRLQ QFDRDCDELL SWIMEKLKTA KDDSYLDPTN
     IRGKLQKHLN YEQELKANKN RLDEINTTGQ SLIEKNHYAA DHIRKRLGEV DGMWDELVDA
     TAKKGAKLKE AGDQQQFNRN VEDVELWLSE LEGQVASEDF GKDLISVQNL QKKLGLLESD
     YNAHQDRIDA IKQQAKTFYD SGHFDAPMIL RKQETLHSRY ENLLDPLNKR KNKLAESLKG
     NQLFRDIDDE LAWIREKEQV AASTNRGRDL IGVQNLIKKQ QALIAEIANH EPQIDAVSAS
     AEQMISQGHF LAPDIRDKLA QLRDNWRNLK AKAEKRRQEL DDSLQAHQYL ADANEAESSM
     REKEPVVGST DYGKDEDSAE SLLKKHRALM SDLEAFKSTI DELRKQASQC RYQEQPGGQL
     GRECVMALYD YTEKSPREVS IKKGDILTLL NSSNKDWWKV EVNDRQGFVP AAYVKKVEPG
     AAQRQSQQVS SIGVKQNEIE DQYQKLLILG ETRRRKLEEA CKGYQLLREA NDLADWIRSR
     EAVAAQQEIG SDLEQVEILQ KKFDDFKGDL KANEIRLQEM NQIATALTSV GQTETAVRIR
     QQIDDLNARW RALEEQTEQR EQQLGSAHEV QRFHRDIDET KDWILEKDDA LDSEDFGRDL
     RSVQALQRKH EGVERDLAAL GDKIKTLDEK ANRLRQTHPE AAEQIYDLQR ELNEQWNRLT
     TKANNRKERL LDSYDYQRFL SDFRDLMQWI AAMNQLVSSD ELANDVTGAE ALLERHQEYR
     TEIDSRAATF QAFEQFGNQL LNSHHYASDN IKQRLNDVNE ARRKLEDAWI HRRHVLDQCL
     ELQLFNRDCE QADTWMSARE AFLNQEDTGD NVESLIKKHE DFDKAIASQQ EKISALRTFA
     NQLINSDHYG KDAVADKRDQ ILQRWDRLKS ALIEKRSKLG ESQTLQQFSR DADEIENWIA
     EKFQVAQEEN YRDPTHIQQK HQKQQAFEAE LAANADRIAT LISAGQNLID GSKCAGSEDA
     VSQRLKALND QWEMLVKTTS EKSYRLKEAN RQKSFMAAVK DLEFWLGEIE GLLASEDYGK
     DLASIENLLK KHQLLEADIA AHADRVAEMN TQADNLLENE QFDRPEINNR RKIINDRYEN
     VKKMANLRRD NLNKAITVHQ FLRDIDDEES WIKEKKLLVS SDDYGRDLTG VQNLRKKHRR
     LDNELASHEP QVFLVREKGL ELANMSNVCA SEIKDRMAAL EKSWDEIKNI TGKRHQKLNE
     SEDFQIFIGK VEEEEAWMNE KQQILSSDNF GENMAGVQGL LKKHDAFEAD LVLHNQRVAQ
     LIKDGQKLID AGNHHSPTIK ARCDQLRNRL DEITELARRR LQKLRDSSAY LQFIWKCDVV
     ESWIAEKEQQ VRSDDFGRDL SSVQILLTKQ EAFDAGLNAF EHEGIQRISE LKDQLVNAQH
     AQTPAIEKRY GNVIMRWQQL LGNSNARRQK LLKMQEQYKQ IEELYLTFAK KASAFNSWFE
     NAEEDLTDPV RCNSLEEISA LREAHAEFHK SLSVAEEDFK QLQHLDKQIK SFNVGPNPYT
     WFTMDALEET WRNLQKIIKE RELELQKEHR RQEDNDKLRR DFARQANAFH HWLTETRAAM
     METSGTLEEQ LELLKRKVAI DVKNNRAQLK KIEDLGALLE EYLILDNRYT EHSTVGLAQA
     WDQLDQLAMR MQHNLEQQIQ ARNQSGVTEE ALREFSMMFK HFDKEKCGRL DHQQFKSCLR
     ALGYDLPMVD EGQPEPEFQR ILDIVDPNRD GYVTLQEYMA FMISKETENI QSSEEIESAF
     RALSKEFRPY VTAEELYANL TPEQAEYCIK RMKPYTDAIS GRSVPGALDY EQFVHTLFQS
//
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