ID   F6D3V0_METPW            Unreviewed;       614 AA.
AC   F6D3V0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=PilT protein domain protein {ECO:0000313|EMBL:AEG18752.1};
GN   OrderedLocusNames=MSWAN_1741 {ECO:0000313|EMBL:AEG18752.1};
OS   Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=868131 {ECO:0000313|EMBL:AEG18752.1, ECO:0000313|Proteomes:UP000009231};
RN   [1] {ECO:0000313|Proteomes:UP000009231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC   {ECO:0000313|Proteomes:UP000009231};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H.,
RA   Imachi H., Zinder S., Liu W., Woyke T.;
RT   "Complete sequence of Methanobacterium sp. SWAN-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG18752.1, ECO:0000313|Proteomes:UP000009231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC   {ECO:0000313|Proteomes:UP000009231};
RX   PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA   Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT   "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT   lacus isolated from northern peatlands.";
RL   Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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DR   EMBL; CP002772; AEG18752.1; -; Genomic_DNA.
DR   RefSeq; WP_013826251.1; NC_015574.1.
DR   AlphaFoldDB; F6D3V0; -.
DR   STRING; 868131.MSWAN_1741; -.
DR   GeneID; 10669251; -.
DR   KEGG; mew:MSWAN_1741; -.
DR   eggNOG; arCOG04116; Archaea.
DR   HOGENOM; CLU_023387_0_0_2; -.
DR   OrthoDB; 7146at2157; -.
DR   Proteomes; UP000009231; Chromosome.
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; IPR004087; KH_dom.
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; SM00322; KH; 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          259..428
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          485..560
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
SQ   SEQUENCE   614 AA;  68642 MW;  AA5731F95672C5C5 CRC64;
     MKIVPDTSVI VDGRITGIVQ VKEYKGCEVI IPEAVISELE NQANKGRETG FNGLEELKEL
     QKLCKEGKLS LTFVGRRPTL EEISLAKGGE IDAMIRNTAG KYHATLITSD RVQKEVAEAQ
     GLDAIYLKQE MVVYTDLEIG KFFDKSTMSI HLKENVVPMA KKGTPGNIKL VKIGSKRLKR
     IEIEKMAREI IERAKSDFRS FIEIEMDGAT VVQFREYRIS IARPPFSDGI EITVVRPVAK
     VSIEDYKLPD KLMDRLRNSA KGILIAGPPG AGKTTFAQAV ADFYSKDIGA IVKTMESPRD
     LQVGDEITQY APLEDDMAKT ADILLLVRPD YTIYDELRKT KDFRIFADMR LAGVGMIGVV
     HSTRPIDAIQ RVISRVELGM IPSIIDTTIF INEGRVAAIY DIALTVKVPT GMVEADLSRP
     VIEVKNFDTG ELAHEIYTYG EQTIVMDIGK TTFEKTPIQK IAEREIINEI KRRIPDAHVE
     VTMKSDKRAT VWIDEKHIPK LIGKKGKTID EVEKHIGISI GVEPLSVNEK KDKTQDNTFP
     IKAELAGNYI VLNFQKDAVG TPFDILVDDE YLFTATVGKK SNIKIKKDIE LANIIINALK
     KNISINARVR QELL
//