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Database: UniProt
Entry: A0A443SB20_9ACAR
LinkDB: A0A443SB20_9ACAR
Original site: A0A443SB20_9ACAR 
ID   A0A443SB20_9ACAR        Unreviewed;       806 AA.
AC   A0A443SB20;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Structural maintenance of chromosomes protein 4-like protein {ECO:0000313|EMBL:RWS24664.1};
GN   ORFNames=B4U80_08894 {ECO:0000313|EMBL:RWS24664.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS24664.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS24664.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS24664.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006005}.
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:RWS24664.1}.
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DR   EMBL; NCKV01004578; RWS24664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443SB20; -.
DR   STRING; 299467.A0A443SB20; -.
DR   EnsemblMetazoa; LDEU007376-RA; LDEU007376-PA; LDEU007376.
DR   VEuPathDB; VectorBase:LDEU007376; -.
DR   Proteomes; UP000288716; 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; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; 1.
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:UP000288716}.
FT   DOMAIN          99..215
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          235..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          13..72
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          277..318
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          343..532
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        239..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  92023 MW;  48BE6737ED6D2D5C CRC64;
     MEKAKLDQFK LKFERNNEEV KEKQSSFKDL KKNIPVTENR LQEINNEVSR IVEQKTRISS
     ELRANNEKLQ EAKNVVNSHT SRNAVVNALM EQKRSGNIEG IFGRLGDLGA IDQKYDVAIS
     TACGSLDNIV TDTMECAQQC VRFLKANNIG SATFIALDKQ TRLESQCRSR IETPENVPRL
     FDLVKINDER VRPAFYFALR DTLVCENLTQ ATRIGLGGRK RWRVVTLRGE LVETSGAMSG
     GGRPSSGKMG SSISGAGVNE EEIREMEGAV NTLKSKFNDI KTREEHLNAE NEKLKRDLEQ
     MKQRLPKLEL ELSEFDKKQS ELKKSINEQE VRTKEAAPDA KKVKELEKKV GALKSDYDKK
     AEEAKAIEVK IKDLNGKIAE IMDKKVGTAK KQVESLNQDI EKVTSAFTKS TVSQKTALRN
     IEKSKSKIET MKKELEDSEA LIVKLKEEMK EIEIKATDIT AKYEECCNER DEVYKKHKEL
     QSELNVLKEK ESRLNSDNLD TKHEVDKLEK VLKDKEAEVN KWHSHIKSLQ LQEIDGQPPP
     EDGLPELTKE QLQCLNSHSV QKEIENMDKE LKKMKPNMAA IAEYRKKQAV YLDRVKELEA
     VTEERDMYKS QFENLRAQRL KEFKDGFTLI TRKLKEMYRT ITLGGDAELE WIDSLDPFSE
     GINFTVRPNK KSWKRITNLS GGEKTLSSLA LIFALHYYKP SPLYVMDEID AALDFRNVSI
     VAHYIKQRTQ NTQFIIISLR NNMYELANRL VGIYKTSNCT KSVTYNPCNK EARKKVVGSS
     VSNGTDIESV VEKQNIPITT TVEMVQ
//
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