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Database: UniProt
Entry: A0A0V0XNW7_TRIPS
LinkDB: A0A0V0XNW7_TRIPS
Original site: A0A0V0XNW7_TRIPS 
ID   A0A0V0XNW7_TRIPS        Unreviewed;       985 AA.
AC   A0A0V0XNW7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Minor histocompatibility protein HA-1 {ECO:0000313|EMBL:KRX89640.1};
DE   Flags: Fragment;
GN   Name=hmha1 {ECO:0000313|EMBL:KRX89640.1};
GN   ORFNames=T4E_10299 {ECO:0000313|EMBL:KRX89640.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX89640.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX89640.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX89640.1};
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   -!- 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:KRX89640.1}.
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DR   EMBL; JYDU01000191; KRX89640.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XNW7; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd20816; C1_GMIP-like; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR   PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          246..508
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          615..660
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          678..877
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          20..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX89640.1"
SQ   SEQUENCE   985 AA;  111830 MW;  DE3AC5C1F4453DD4 CRC64;
     LPFWHVELTA MSTERELASS LPISSEAVGS DPASEYSAIS SSMDTSAGDM DSELMDSLVR
     DVRRLSETLT ELGIALEQPT GLCAEDSATD ADNNSKEDLN TNWSVNVHQR LCDVLQLIKE
     AIIRYRFLQS NDIFEYLGSL VDVIKGLNFY EESPKNSEAL KNARATLESL QIAVAECVGE
     YLTWEMTQYE SSLNKMSWSA EDVSSLMMQN GDPPVAKRRQ KKELRKQLSV GSEVSTKALS
     LPEKHVESED EILDGLEDGV EIALSRARAW SNYCKELLAF IQRRINLDSE HARAVQKLNA
     NARFAITVEH FLPLKEVYLN NFKIENDFFE NCLDTMKRLY EYKFIKPLEA RKVEIDCKRK
     DLKHTWEKIV KEVETVTIEL KKARHNVVIR ESNYKKAKES TAKSEKMKVD SQKLERRRKL
     QEDALMRREQ ASHDYWSLEQ RLEEKYQEMA KTKTTVLREV RELIYQCDQT TKACTVAYFQ
     ACSGLWALLP MQYQSLADTS RQYIPGTLYK QFVHNLNNFA SEENITGPGE KNKVVSEGDL
     PVIQLNGDPI NSAASPSQRS SMPPSSSPSA ATSVSTCCYS SDDVSSSHRI AALKPLRNKA
     KIFNRPSLLS DAALSHRLQR TRAPTKCCHC DAYTFFQTVQ CTECGLTWHK TCLGNLDVHC
     QLAKQLNINR RRMRIFGVPL QKHLEDNQIS VPFVLKTCIE ELETRGLDVK GLYRVCGVKS
     NIEQICEKFE RQKVELSTVL PTNIASIIKL YLRQLPEPLL THELYHSFVE LANKYPEMKS
     TEQLSISLNI ITDLKRICNM LPSANYRTLK LLCLHLNRVS WFEMENQMSP TNLGIVFGPS
     LLWIDEGLSG TSLKSLLDAP LQTRVAELLI KYAYEIFDED ATEDMKRLCV KRRCKELAEC
     DEADRRQVKS MVPSTSKTAE IDPALVEKGR HSTTPDLLRE TKLSRAKSLQ SSLGIITSVD
     FTDASKANSM QNSLSSLTKT DFNVE
//
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