ID A0A077ZQ17_TRITR Unreviewed; 1210 AA.
AC A0A077ZQ17;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=DUF4117 and Ftsk gamma and FtsK SpoIIIE domain co ntaining protein {ECO:0000313|EMBL:CDW60850.1};
GN ORFNames=TTRE_0000925301 {ECO:0000313|EMBL:CDW60850.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW60850.1};
RN [1] {ECO:0000313|EMBL:CDW60850.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW60850.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; HG807483; CDW60850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZQ17; -.
DR STRING; 36087.A0A077ZQ17; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR025199; FtsK_4TM.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF13491; FtsK_4TM; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 855..1068
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 232..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 133233 MW; 5777D1BBBC45BAAF CRC64;
MALILTSCGL AAINADDIWY FASGGVIGSL LSTTLQPLLH SSGGTIALLC VWAAGLTLFT
GWSWVTIAEK LGGWILNILT FASNRTRRDD TWVDEDEYED DEEYEDENHG KQHESRRARI
LRGALARRKR LAEKFINPMG RQTDAALFSG KRMDDDEEIT YTARGVAADP DDVLFSGNRA
TQPEYDEYDP LLNGAPITEP VAVAAAATTA TQSWAAPVEP VTQTPPVASV DVPPAQPTVA
WQPVPGPQTG EPVIAPAPEG YPQQSQYAQP AVQYNEPLQQ PVQPQQPYYA PAAEQPAQQP
YYAPAPEQPV AGNAWQAEEQ QSTFAPQSTY QTEQTYQQPA AQEPLYQQPQ PVEQQPVVEP
EPVVEETKPA RPPLYYFEEV EEKRAREREQ LAAWYQPIPE PVKEPEPIKS SLKAPSVAAV
PPVEAAAAVS PLASGVKKAT LATGAAATVA APVFSLANSG GPRPQVKEGI GPQLPRPKRI
RVPTRRELAS YGIKLPSQRA AEEKAREAQR NQYDSGDQYN DDEIDAMQQD ELARQFAQTQ
QQRYGEQYQH DVPVNAEDAD AAAEAELARQ FAQTQQQRYS GEQPAGANPF SLDDFEFSPM
KALLDDGPHE PLFTPIVEPV QQPQQPVAPQ QQYQQPQQPV PPQPQYQQPQ QPVAPQPQYQ
QPQQPVAPQQ QYQQPQQPVA PQQQYQQPQQ PVAPQPQDTL LHPLLMRNGD SRPLHKPTTP
LPSLDLLTPP PSEVEPVDTF ALEQMARLVE ARLADFRIKA DVVNYSPGPV ITRFELNLAP
GVKAARISNL SRDLARSLST VAVRVVEVIP GKPYVGLELP NKKRQTVYLR EVLDNAKFRD
NPSPLTVVLG KDIAGEPVVA DLAKMPHLLV AGTTGSGKSV GVNAMILSML YKAQPEDVRF
IMIDPKMLEL SVYEGIPHLL TEVVTDMKDA ANALRWCVNE MERRYKLMSA LGVRNLAGYN
EKIAEADRMM RPIPDPYWKP GDSMDAQHPV LKKEPYIVVL VDEFADLMMT VGKKVEELIA
RLAQKARAAG IHLVLATQRP SVDVITGLIK ANIPTRIAFT VSSKIDSRTI LDQAGAESLL
GMGDMLYSGP NSTLPVRVHG AFVRDQEVHA VVQDWKARGR PQYVDGITSD SESEGGAGGF
DGAEELDPLF DQAVQFVTEK RKASISGVQR QFRIGYNRAA RIIEQMEAQG IVSEQGHNGN
REVLAPPPFD
//
