ID I0XLR7_9LEPT Unreviewed; 802 AA.
AC I0XLR7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=HDIG domain protein {ECO:0000313|EMBL:EID99824.1};
GN ORFNames=LEP1GSC185_2591 {ECO:0000313|EMBL:EID99824.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EID99824.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EID99824.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EID99824.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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:EID99824.1}.
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DR EMBL; AHOO02000013; EID99824.1; -; Genomic_DNA.
DR RefSeq; WP_008592080.1; NZ_AHOO02000013.1.
DR AlphaFoldDB; I0XLR7; -.
DR PATRIC; fig|1049972.3.peg.3480; -.
DR OrthoDB; 9806952at2; -.
DR Proteomes; UP000004889; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR011624; Metal-dep_PHydrolase_7TM_extra.
DR InterPro; IPR011621; Metal-dep_PHydrolase_7TM_intra.
DR NCBIfam; TIGR00277; HDIG; 1.
DR PANTHER; PTHR36442; CYCLIC-DI-AMP PHOSPHODIESTERASE PGPH; 1.
DR PANTHER; PTHR36442:SF1; CYCLIC-DI-AMP PHOSPHODIESTERASE PGPH; 1.
DR Pfam; PF07698; 7TM-7TMR_HD; 1.
DR Pfam; PF07697; 7TMR-HDED; 1.
DR Pfam; PF01966; HD; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 564..726
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
FT REGION 774..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 90861 MW; 81A0DBD5B3FA38D1 CRC64;
MFPLGSLLER GMAWITDTLT KIRPISFVRK FQVILTAITL IIVTWMLAIP FFGQDKINLS
QDGPYSEGKN ALDKVVSTKD IVYEDEEKTK AKRLKAFQSA PNFFDRDYRV LIEVIRPAIQ
EDMEKYREPK PTGEVKTSAE LLAAVPRWKN RSKEELELLL KTPGKSRVRD LVQQYSNLVF
SNFCILRDQP ADYSAIRSAE ARIRNSGASG NKEQISSVEG TLVIPRMYLY RDSATVDALN
RLAAEKLQAT DPQLLSVIQK LALTYLYSNP ACTFNAEETK NQKQAVMDRT EPVSSRINAG
ETIVKAGEII TPDIYQKLLI VNRYATRANI ASIISILLIQ SIFVIIVYAF LKKYNPKRLN
DVSSNVIVFT LIWSLVLWAY LASKAFFSFE NSYDSVFYFA LVIPTGMVCL ILSMIYDEQL
SIAIGFFLSF FVFAASRYNP TSFILAFVMT VVAATYGRKM RKRIDFIKAG FYMALVQMLI
SSSGYLFDSR NYWVAVPSGS HFRDLWESNI FRLYLLCLVN GFVCSTLTQL LLPIYEYVFN
IPTRFKLLEL ADTGHPLLQD LLTKAPSTYT HTFLVAAMSE RAAQNLELDW LLTRVGVYFH
DIGKIPNAGF FVENQHLIPK KENIDKNNPA KAAKIVIDHV LDGIEMAKKA RLPREVIDFI
PEHHGTSTMA FFYHKALAEL SPSQKKKLKK ADFQYPGPKP QRKETAIVMI ADSLEAASRS
LEEVTPEALD ILITKIVNGK LAENQLDECG LTLGDLEVVK HSFKEVLLSS LHSRPKYPKP
EDTKALEEKN KNILGKHTPK SH
//