ID A0A0K3CPZ1_RHOTO Unreviewed; 1719 AA.
AC A0A0K3CPZ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=RecF/RecN/SMC N terminal domain-domain containing protein {ECO:0000313|EMBL:PRQ72866.1};
GN Name=FGENESH: predicted gene_9.458 {ECO:0000313|EMBL:CTR09251.1};
GN ORFNames=AAT19DRAFT_16790 {ECO:0000313|EMBL:PRQ72866.1},
GN BN2166_0051120 {ECO:0000313|EMBL:CTR09251.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09251.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR09251.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR09251.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ72866.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ72866.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; CWKI01000009; CTR09251.1; -; Genomic_DNA.
DR EMBL; LCTV02000009; PRQ72866.1; -; Genomic_DNA.
DR STRING; 5286.A0A0K3CPZ1; -.
DR OMA; ECSENIM; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069}.
FT DOMAIN 997..1111
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 718..952
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1162..1399
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1462..1513
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1719
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1719 AA; 190069 MW; C7D0DBB16198F275 CRC64;
MPPRRKQPLE QYDTNAQPAA FSRSSRSSSS TNKHKQALAA AASRRATRKR VSEASTAATE
EDADEAEDSE GENVGFEGDA TEEDEEDEDS EPVKSKRAAA TRVARTVKQE SATGRTRRAP
ASSTATSRRR NVREDTVSTA ASDDEDEDDD KEEEEEPVKA RSARSSRSSR STTTSARSTR
GKKASTPEQP AAPLSPPATP AVGEDDEEDE AEQQDDDDEE EEEEVKPRVS ASKRKKRVSL
APASPVKQPV LPTPEPESSA AEEEDGEDEQ TAQEDEDVED REETPQPPAA AAKSKAKGKR
RAIVQSDEDE QDELAQPAAP AAAQQVAPPS PAPSATPRSR STTPTPAEPA APAVAPAPAP
VAPAKPAPPT ALTASALASI ARQAAIDHAA QAAERAKELL GKPRLVIHQL VLENFKSYKG
RNTIGPFHKA FSAIVGPNGS GKSNTIDALL FVFGFRATKM RQGKFSELIH NSGVAGGAEH
APAAEGDADE DDEDGFFNPE EYDSEEEVEM RKRKGKGKAK GKKTARKAPS YAAAGGCDFA
TVEVWFREIV DSPTSRDDFS VVPHSQLVVA RTVRRDNSTR YTVNGKNATP GEVKQLLLGK
GIDLTHNRFL ILQGEVESIA QMKPKGANDH EEGLLEYLED IIGTAKYKPL IEEASADVER
LGDERAVQMN RVKLVEKEKG ALESRKKAAD AYLHDQLTLV SLQNQLYQRH AHQAGADRVV
YEQQVAEAKA ELDAEMERQK SDRERYDQGV EQYEVTKKNL KEIEDAANGL AKELATFEKA
KVQLTVQKKA ADTKYAKLKK SLEEDKHAAQ QAQSDIRDHA DTLEKLVSSK DRLKAELEEE
QAALTKVMDS LRDKIEGFSV EIEQHQKSLA PWTEQIEAKQ NEVKIATHQL EDVRGKSAQV
VADIERTEQE IEELKEAAKE KAVELKTLQK GRKDILAQID EARQRVQQEK TVEAKHRAVV
NSAREKTAEA KASQKASESK GHVLSAVLKL KEQGRLPGFH GRLGDLGRID DKYDIAVSTA
AASGLESLVV DTRETAEAVF DHLRKHNIGR AACIALDRFG KVDLSPIKTP QGTQRLFDLV
TPKDAIYAPA FRHVLKDTLV APSWDIAHPV STGKVDGQRW RVVTLDGNVA EKSGAAQVGG
SRPIRGKMSS RLAADDVSPQ QLAKLEAEEK TATVKLEQAA EQSKQAEADL KVLEKQLTQA
ESSIPKVEMD LEANKQDAAQ KAELLNELRG QSKPDAGDVK RVAQLEKAIE TLEGELESLR
GKASKFEDKI AALQAKIEEV GGLKLRSQKA KVSDLQDQIR HNESRLVKAK TERAKAEKDH
AKATKAIESN TAKMQELEVE LKDLRRQLAE KEEEAEPIRQ TVEAAQAKVE EGREELGNLK
AELDEQEEAI IEFKKAEAKL RTIYTEQEKL LKETTRIFEH WTAKISSLEM PEFELLGDAD
EEDEDGNRPP EVEEVLRQLE PEEIEQIDVK RLKGEIALLE ERLEKNNADL AVLQEYKRRE
EEFRRRGEEF EAVSREWDGA KTRVTELRNE RLVQFMQGFG IISNKLKEMY QMITLGGNAE
LELYDSADPF SEGILFSVMP PKKSWKNISN LSGGEKTLSS LALVFALHTY KPTPLYFMDE
IDAALDFRNV SIVANYIKTH SENSQFLIIS LRNNMFELAA RLVGIYKVSN QTRSIAIDNK
ELSAVPDVPS VTLEEEEEEE EEEEEEEEEE AGSEDEDDA
//
