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Database: UniProt
Entry: K1WKK7_TRIAC
LinkDB: K1WKK7_TRIAC
Original site: K1WKK7_TRIAC 
ID   K1WKK7_TRIAC            Unreviewed;       866 AA.
AC   K1WKK7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=MMS2 protein {ECO:0000313|EMBL:EKD01834.1};
GN   ORFNames=A1Q2_03897 {ECO:0000313|EMBL:EKD01834.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD01834.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD01834.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD01834.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(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:EKD01834.1}.
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DR   EMBL; AMBO01000310; EKD01834.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1WKK7; -.
DR   STRING; 1220162.K1WKK7; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   HOGENOM; CLU_000688_12_0_1; -.
DR   InParanoid; K1WKK7; -.
DR   OMA; HACHDIK; -.
DR   OrthoDB; 168438at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR   CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 6.10.20.150; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005938; AAA_ATPase_CDC48.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015415; Spast_Vps4_C.
DR   NCBIfam; TIGR01243; CDC48; 1.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 2.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          31..114
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          144..210
FT                   /note="CDC48"
FT                   /evidence="ECO:0000259|SMART:SM01072"
FT   DOMAIN          256..392
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          529..668
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   866 AA;  95083 MW;  F1B44391995BEDB1 CRC64;
     MSDPSQVADA KPTADDSTAT AILRQKKSPN RLMVDESPSD DNSVAVLHPN TMETLGLFRG
     DTIIVRGKRR KDTVLICLSQ DDIEEGKICM NKVARQNCAA KLGDLVHVAP ANGIKYDKRY
     VWLDLGATDV TSIHVLPFSD SVEGLSGNLF DVYLKPYFLE AYRPVRKGDI FQVRGGMRTV
     DFKVIEVDPS PYCIVASDTV IHTEGDALDR EAEEADLNAV GYDDLGGCRK QLAQIRELVE
     LPLRHPQLFK AIGIKPPRGI LMFGPPGTGK TLMARAVANE TGAFFFLING PEIMSKMAGE
     SESNLRKAFE EAEKNSPSII FIDEIDSIAP KRDKTNGEVE RRVVSQLLTL MDGLKARSNV
     VVMAATNRPN SIDPALRRFG RFDREVDIGI PDPTGRLEIL RIHTKNMKLS DDVDLEQIAA
     DTHGYVGADM ASLCSEAAMQ QIREKMDLID LDEDTIDAEV LDSLGVTMEN FRYALGVNNP
     SALRETVVEI PTTTWNDIGG LEKVKRELQE TVSYPVEHPE KFLKYGLSPS KGVLFYGPPG
     TGKTMLAKAI ANECQANFIS IKGPELLTMW FGESEANVRD VFDKARAAAP CVMFFDELDS
     IAKSRGGSGG DAGGASDRVL NQILTEMDGM NAKKNVFIIG ATNRPDQIDP ALLRPGRLDQ
     LIYIPLPDEA SRLSILEATL RKSPVAPGVD LGFLAKSTAG FSGADLTEIC QRAAKLAIRE
     SIESDVRKDR ERREKAEAAG GEGEVDIMDE ENDEDEVPAI TVEHFEEAMK FARRSVSDAD
     IRRYEMFSTS LQQSRGFGNN FKGGAAFQNE ADDDDQTFPL PPVSLLSETT SRMETPDHGS
     RPCPRYCDSQ TAQADTSLPL ATEDEL
//
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