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Database: UniProt
Entry: A0A1I7XYB7_9BILA
LinkDB: A0A1I7XYB7_9BILA
Original site: A0A1I7XYB7_9BILA 
ID   A0A1I7XYB7_9BILA        Unreviewed;      1430 AA.
AC   A0A1I7XYB7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Structural maintenance of chromosomes protein 4 {ECO:0000313|WBParaSite:L893_g10853.t1};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g10853.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g10853.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   WBParaSite; L893_g10853.t1; L893_g10853.t1; L893_g10853.
DR   Proteomes; UP000095287; Unplaced.
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; 1.20.58.60; -; 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; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}.
FT   DOMAIN          651..767
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          811..939
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          969..1080
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1214..1251
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..426
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1163
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1430 AA;  162224 MW;  F3A8E13F4C5F99FD CRC64;
     MAPGRRKVDK AEPKPKRGRR SLPDADNEDE DVIMDSDDSL PSPSKKAGAR GAKKKAPVKP
     TPKKTKAKGA QKDTQEEEED ADDFDERRQL LEENINEEDL LNMVIPPPPE AMKEGDANKR
     LMISSIEVEN FKSYYGKQVI GPFHKNFTAI IGPNGSGKSN VIDSLLFVFG YRAAKIRSKK
     VSVLIHNSAA HDNIDRCRVQ VNFQQIIDEP EGKYSVVPGS QFSVARTGFR NNSSQYHYNG
     TPMQFKEVAK ILRNVGIDLI HNRFLILQGE VEQISLMKPK APSPNEDGML EYLEDIIGCA
     RLKVPIEKLT AKCSQLQDQR TTQFSRAKQA EREKEALENP VRDIMQHLRL ENGIALVNSK
     ALYKKMYKKE AQYEEHAPQV DVIKEKIKEN KEQMSELLKL QDEQSKEQKK LQKKLEKAED
     EFSRSKTSQS TMEGEVQLKK KELKRCAEKV EKLKADIKKE DKKLKEYESQ PAKCEQKIEE
     HTEIAEEAKQ EELKYQKMLE ERLVELEGKS KELNERKKAH EAELAAAAKA QDSASSKLLV
     AQQDRKNLVD EGERAHTQLK ELESNIAETE RNLEAKKGEL EKVKTALPGK VQALQESETR
     AREVEERVKK LEAACHPLQA KVMEERSSCS SQSQNRVIAA LMREKEKGTI QGIYGRLGDL
     GGIDKKYDAA ISNCTGVLDN VVVENVEVAQ QCIKFLKEQN IGTVTFLALN KQDRFKGRMK
     LTRATPEGAP RLFDLITVKD EKVLPAFYFC LQDTLFAEDI NAATRIAFTP PRWRVATANG
     EIVETGGTMV GGGSRVVRGK MGATVRVDTS RRRSGESLEE LEQKLKSLKA EIEELERESG
     NLNRQIHSLT RDKEQMERRA KDLDTEIDTL TLRLERLRGS LVEQKEKVKN SKRTEQAVDE
     ATDNVRTLEK DRDEAAATVD KIRSQVEEIN KQLQDFYTEI VGDIQTHFDA ARERKDAALK
     VVSKEQTALN AVSRNLSKSQ KKVAELNKDL ERTEESIVAD EEKIKDLEEQ LEALALKIEE
     LEKVKVEAQE EVNEANEKAK SSNEDEIKLK NEGNMLDKSL KELTEKLTKI RYEIERYKGE
     IAKLTFQYVT FVDRLPAELT APDGTDEILS EAYTIEMEAI KSGKTKKGKA PRVASSSDDP
     EPMETDGEEV PAPESEDEEE EGAPMVSVTT MIGTLEIPAP TKEAMEMLTE EELKFHQVNL
     DKKKVKKNYD FNNLVEYYHK LLKFEKENAE LEEISKKRDA HRDKLKQVKD MRHNEFMDGF
     QKIGSALKEM YQMITLGGDA SLDLVDSLDP FNEGVSFGVR PPKKSWKQIT NLSGGEKTLS
     SLALVFALHH YKPTPLYVMD EIDAALDFRN VSIIGHYIKE KTKNAQFIII SLRNNMFELG
     DRLVGIYKTY DCTKNVCVDP DEVAKAAQDV GEKLRKNRAD RRVLSSRQDV
//
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