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Database: UniProt
Entry: A0A1G7PYM9_9EURY
LinkDB: A0A1G7PYM9_9EURY
Original site: A0A1G7PYM9_9EURY 
ID   A0A1G7PYM9_9EURY        Unreviewed;       624 AA.
AC   A0A1G7PYM9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=ATPase, PilT family {ECO:0000313|EMBL:SDF91341.1};
GN   ORFNames=SAMN05216218_11179 {ECO:0000313|EMBL:SDF91341.1};
OS   Halorientalis regularis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorientalis.
OX   NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF91341.1, ECO:0000313|Proteomes:UP000199076};
RN   [1] {ECO:0000313|EMBL:SDF91341.1, ECO:0000313|Proteomes:UP000199076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF91341.1,
RC   ECO:0000313|Proteomes:UP000199076};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNBK01000011; SDF91341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7PYM9; -.
DR   STRING; 660518.SAMN05216218_11179; -.
DR   OrthoDB; 7146at2157; -.
DR   Proteomes; UP000199076; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd09878; PIN_VapC_VirB11L-ATPase-like; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR001482; T2SS/T4SS_dom.
DR   PANTHER; PTHR11603; AAA FAMILY ATPASE; 1.
DR   PANTHER; PTHR11603:SF157; PILT PROTEIN DOMAIN PROTEIN; 1.
DR   Pfam; PF01850; PIN; 1.
DR   Pfam; PF00437; T2SSE; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   4: Predicted;
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT   DOMAIN          1..115
FT                   /note="PIN"
FT                   /evidence="ECO:0000259|SMART:SM00670"
FT   DOMAIN          261..396
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          526..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  67425 MW;  EF21C597A87412CE CRC64;
     MNVVPDTSVV IDGRVSDHVE AGDFAGATIY VPEAVVGELE SQANEGRDSG WDGLTELQAL
     ADLADDGEID LEYVGQRPDA DEIDDAGEGE IDAIIRDTAA EHGATLFTSD IVQSEVATAK
     GITVEYVEPI VEETAVETLT IEQFLDETTM SLHLKTGVPP MAKRGELGEM HYEEIRDEPS
     TEAQLKEWAQ EIENSARASP DGFIELSEPG MTIVQFRDMR IAIASPPFAD GHEITAVRPI
     VKTELDDYEF ADELRERLTD HQRGVLISGA PGAGKSTFAQ AVAEFLADAD FAVKTMEKPR
     DLQVGPNITQ YTELGDEMAK TADSLLMVRP DYTIYDEVRK TDDFEVFADM RLAGVGMIGV
     VHATRAIDSL QRLVGRVELG MIPQVVDTVV YIEEGRVEKV YDVTTEVKVP EGLMEEDLAR
     PVIMIRDFET GQPEYEIYTF NRQVVTVPIG EDSEGGGQDS GVDRIAKQEV EREIRSVAHG
     HVEVDLKGPN TAVVWVEDDD ISQVIGKGGG RISDIENRLG IDIDVRTLSE KPGGASGGTG
     SGGGGDSGGG QPGQIVTPEV TSRHVIVPME GHAGETVEVQ ADGEYLFTAT VSRGGEIQVS
     RGSAIAEELE QAIDRGKTIQ VIPS
//
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