ID A0A0V1L2Q6_9BILA Unreviewed; 1239 AA.
AC A0A0V1L2Q6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Minor histocompatibility protein HA-1 {ECO:0000313|EMBL:KRZ53573.1};
DE Flags: Fragment;
GN Name=hmha1 {ECO:0000313|EMBL:KRZ53573.1};
GN ORFNames=T02_12478 {ECO:0000313|EMBL:KRZ53573.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ53573.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ53573.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ53573.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ53573.1}.
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DR EMBL; JYDW01000161; KRZ53573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L2Q6; -.
DR STRING; 6335.A0A0V1L2Q6; -.
DR Proteomes; UP000054721; 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 CDD; cd01327; KAZAL_PSTI; 1.
DR Gene3D; 3.30.60.30; -; 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; IPR001060; FCH_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
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; PF00050; Kazal_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00280; KAZAL; 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 SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00282; KAZAL_1; 1.
DR PROSITE; PS51465; KAZAL_2; 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:UP000054721};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 333..595
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 701..746
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 764..963
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1184..1239
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 633..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1239
FT /evidence="ECO:0000313|EMBL:KRZ53573.1"
SQ SEQUENCE 1239 AA; 139903 MW; 1B918B3E23C94DB6 CRC64;
LLTCRFLMRD ALTLRTVTPY RRILVDLCGS TVAPESCPGH ACISSAVCAF CLIFSVYRHS
SNTLKNDIAA PNHQCRIKIP PYLLHSLTHI CTPELTAMST ERELASSLPI SSEALGSDPA
SEYSAISSSM DTSAGDMDSE LMDSLVRDVR RLSETLTELG IALEQPTGLC AEDSATDADN
NSKEDLNTNW SVNVHQRLCD VLQLIKEAII RYRFLQSNDI FEYLGSLVDV IKGLNFYEES
PKNSEALKNA RATLESLQIA VAECVGEYLT WEMTQYESSL NKMSWSAEDV SSLMMQNGDP
PVAKRRQKKE LRKQLSVGSE VSTKALSLPE KHVESEDEIL DGLDDGVEIA LSRARAWSNY
CKELLAFIQR RINLDSEHAR AVQKLNANAR FAITVEHFLP LKEVYLNNFK IENDFFENCL
DTMKRLYEYK FIKPLEARKV EIDCKRKDLK HTWEKIVKEV ETVTIELKKA RHNVVIRESN
YKKAKESTAK SEKMKVDSQK LERRRKLQED ALLRREQASH DYWSLEQRLE EKYQEMAKTK
TTVLREVREL IYQCDQTTKA CTVAYFQACS GLWALLPMQY QSLADTSRQY IPGTLYKQFV
HNLNTFASEE NINGSGEKSK VVSEGDLPVI QVNGDPITSA SSSQRSSMPP SSSPSATTSV
STCCYSSDDV SSSHRIAALK PLRNKAKIFN RPSLLSDAAL SHRLQRTRAP TKCCHCDAYT
FFQTVQCTEC GLTWHKTCLG NLDVHCQLAK QLNINRRRMR IFGVPLQKHL EDNQISVPFV
LKTCIEELET RGLDAKGLYR VCGVKSNIEQ ICEKFERQKV ELSTVLPTNI ASIIKLYLRQ
LPEPLLTHEL YHNFVELANK YPEMKSTEQL SISLNIITDL KRICNMLPSA NYRTLKLLCL
HLNRVSWFEM ENQMSPTNLG IVFGPSLLWI DEGLSGTSLK SLLDAPLQTR VAELLIKYAY
EIFDEDATED MKRLCVKRRC KELAECDEAD RRQVKSMVPS TSKTAEIDPA LVEKGRHSTT
PDLLRETKLV SRAKSLQSSL GIITSVDFTD ASKADSVQNC LSSLSKTDFN DTVQRRQFRF
KVIWGFWKIF QVDKIYGQCR KNDNANVTQM MYKKITTLKK PEVVFLARPT GPGAANQCAS
RAEKDRLHSS SDHFAIPSCT VVMANPKVCL LFALVCCALG MARGEREPNC DHAPDICTRE
YSPLCGTDGK TYSNQCMLCA VKADSKPDLR IASDGPCPK
//
