ID A0A0A8KZ28_9SACH Unreviewed; 1508 AA.
AC A0A0A8KZ28;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=WGS project CCBQ000000000 data, contig 00107 {ECO:0000313|EMBL:CDO91788.1};
GN ORFNames=KLDO_g121 {ECO:0000313|EMBL:CDO91788.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO91788.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO91788.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:CDO91788.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCBQ010000004; CDO91788.1; -; Genomic_DNA.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000031516; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 340..552
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1196..1234
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 175410 MW; 03619CE41BC53AC3 CRC64;
MGAFPEGSFV GWELLDKDVE LIEGGIRDFS FDESLQPYES HRKERQGKYG VIPVLNWGLR
YGDFNVSEIT KRVAVTLKWE QNQSRNKGWV QFYHNSRFLG KWDCGASFGQ FKQTVLCVES
KVKEKDDWEE LVHATEEKEK EESGTGNSKR KKRKVALRNK NTYKFPDVKL HPLVMSIDSQ
GNWEVTVQMS LFCVIDDGNN FAEETNRLLT ELFNEKNVEY TAEEAYRREM GSVDEFNHLL
ERHSKQILRE GVQVNVPSML NVKLMPFQME SVDWMLRKEG FYNEPLERIS TVKQLKGFLN
EHVSFGYEFM PINNCFWNKV VGYICPLDTA WNIYEEWLTD QSNERKTKGL LADEMGLGKT
VEMIGLITTN RRDLSHISTT CISSTTKKEI YRAKTNLIVC PVTILEQWID EIHLMFNNNV
SDFKVFHYEG FAKMKHKFNN ESSINLAKRL SEYDVVITSY NVLSAERRYA NFGEVQRPSR
KSTRQHDYSS PLINLEFFRV ILDEVQLLGH VLSYTSQCLQ MVNRIHSWCM SGTPVQSVRS
LQDIFSHLQL HPFQLPEVSE LADNAYYASS ANHSGYNESD HYYGFIYRNW DPTDDWYGYH
GCRLTREEIF DIFPNYNLAI RHLKKDVQDQ IKIPKQVNYL IPVEFNPVER DNYTDLWDSF
LSASGYDSKG RGTCYLDFYN LKMWLDIFRL TCCHASLKFD HDSDIAGYKW RAVDDLKDMD
AVLDTMKQQV SNKISRLQRE NYAIQIHTAQ VKTEAGEDHD TSTSVFQNVI ESITNDLRTV
YGINDFLDLN IETVQSIPVN DISGFRSLLQ LLHQAIYLLA TSYYQLGSKK LQDIENIYDN
EGNHESLTKN DMIKSSKESS ENSNGDVCMK NELVEISNYQ NLEREWYATA KKLRREMLRE
RIADVNAVVS NVRNFFAKES LERKLKLDYI ILDKDNFALP LGETVIYQQI IRLFERINKQ
TEQFNGLIKK LEVLCYETID IQPDDGEDAV KLKDFSEVLR KQNMVKFILD TLERILTNRE
DMLISEYKVT PSDHDNSTVE ADSQLLDDIS KNTVFIDGDS LRLLLNRAED SPVMQNQLLR
SKLSNHTMHD FIECHEADIT RIQKENKNMK IVLERFNDIY DAKVDYFNHL QLISESQPSP
AKEPYAVMKL TVNKGSEELR YEKNCSTISN LRSRRNYLNT LSQLKSTIAK NEAITCAICY
SDVYTGSILK CGHLFCKGCV IHWFQKNSSC PLCKTTMTNS EVYHFKFREN DLQESKDTNN
IVSTLKENGS DKNIHPSKMN GEIGHFSHSI DRDNSFQNTE AIIAHKYSTF SKMNEVNKIV
LKNSWGGKVD QALKLILYIK KQHMENDPSA KSPQIVICSM HPQFFDILGR LLSLHKISFG
RPLRDTPYAA AINIFKKNPE CTCLFLRSRQ EAVGLTLVNA RHLFIMDPIM ESSTEAQALS
RIHRIGQKQE TYVWNFMVRN TVEESIIKFK VELESKRFQQ MEELKKLNSE EVMCVAEKKW
RTLYHWKI
//
