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Database: UniProt
Entry: B4NBN8_DROWI
LinkDB: B4NBN8_DROWI
Original site: B4NBN8_DROWI 
ID   B4NBN8_DROWI            Unreviewed;      1237 AA.
AC   B4NBN8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   Name=Dwil\GK11152 {ECO:0000313|EMBL:EDW81202.1};
GN   ORFNames=Dwil_GK11152 {ECO:0000313|EMBL:EDW81202.1};
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW81202.1, ECO:0000313|Proteomes:UP000007798};
RN   [1] {ECO:0000313|EMBL:EDW81202.1, ECO:0000313|Proteomes:UP000007798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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DR   EMBL; CH964232; EDW81202.1; -; Genomic_DNA.
DR   RefSeq; XP_002070216.1; XM_002070180.2.
DR   AlphaFoldDB; B4NBN8; -.
DR   SMR; B4NBN8; -.
DR   STRING; 7260.B4NBN8; -.
DR   EnsemblMetazoa; FBtr0241803; FBpp0240295; FBgn0213163.
DR   GeneID; 6647468; -.
DR   KEGG; dwi:6647468; -.
DR   eggNOG; KOG0018; Eukaryota.
DR   HOGENOM; CLU_001042_0_2_1; -.
DR   InParanoid; B4NBN8; -.
DR   OMA; SYIRDHT; -.
DR   OrthoDB; 231904at2759; -.
DR   PhylomeDB; B4NBN8; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0008278; C:cohesin complex; IEA:EnsemblMetazoa.
DR   GO; GO:0000791; C:euchromatin; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005700; C:polytene chromosome; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0016319; P:mushroom body development; IEA:EnsemblMetazoa.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:EnsemblMetazoa.
DR   GO; GO:0016322; P:neuron remodeling; IEA:EnsemblMetazoa.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03275; ABC_SMC1_euk; 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; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR028468; Smc1_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF12; 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   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007798}.
FT   DOMAIN          534..653
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          405..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          257..291
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          696..954
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1036..1077
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        416..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1237 AA;  142886 MW;  897BC7C52BF72616 CRC64;
     MADEDEDVTR VVAPPSRKPD DDTAFLQFIE MENFKSYRGH IIVGPLKQFN AVIGPNGSGK
     SNFMDAISFV MGEKTSSLRV KRLNDLIHGS SIGKPVSRSC YVTAKFILNH EKHMDFQRAV
     ISGSSEYRIN GESVSSSTYL NKLEKIGINV KAKNFLVFQG AVENIAMKTP KERTALFEEI
     SGSGLLKDDY NRLKNEMIAA EEETQFTYQK KKGIAAERKE AKHEKMEAER YTRLQNEYNE
     KQVEYQLFRL FHVEKDIRKH ITDMEAKQQE VKVVEQRKEA ADEVLREKKK DAGKITRDLA
     KIDQEIREFE TQMNKRRPLY IKAKEKVTHC KKKLVSLQKT LETAREADNA HQQDIRKLEK
     QLSDIETLKK SFEDDIENES QRRGKSVNME EGLVQEYDRL KQEAEATATQ YRSELDSVNR
     EQKSEQDTLD GETNRRASVE ESFKKLTLQR EEAVKRRDKL MDHIKSSQAA LEEQNRIKDE
     LRRDVGSSKE KITEKQRELE NVRDQLGDAK SDKHEDARRK KKQEVVELFK KQVPGVYDRM
     INMCQPTHKR YNVAVTKVLG KFMEAIIVDT EKTARHCIQI LKEQMLEVET FLPLDYLQVK
     PLKERLRNIS EPRNVRLVFD VLKFEPPEIE RAVLFATGNA LVCETPEDAM KVAYEIDRSR
     FDALALDGTF YQKSGLISGG SHDLARKAKR WDEKHMAQLK MQKERLNEEL KELVKKSRKQ
     SELATVESQI KGLENRLKYS MVDLETSKKS IGQYDNQLQD VQRQLDDFGP KISEIERRMQ
     DREEHIQEIK ENMNNVEDKV FAAFCRRLGV KNIRQYEERE LVMQQERARK RAEYEQQIDG
     INTQLDFEKQ KDTRKNVERW ERSVQDEEDA LEGLKTAESR YLKEIDEDKE KMEKFKQEKQ
     AKKQAVDDME EDISKARRDV ANLAKEIHNV SSQMSSIESK IEAKKNERQN ILLQAKTDCI
     AVPLLRGSLD DAVRQSDADN TNTSLAMDNI IEVDYRSLPR ELTKLKDDSA FKKMNEQVQK
     DLQAKLDILE RIQTPNMKAM QKLNAVTEKV QSTNEQFENA RRKAKKAKSA FERVKNERSS
     RFVQCCQHIS DAIDGIYKKL ARNEAAQAYV GPDNPEEPYL DGITYNCVAP GKRFQPMSNL
     SGGEKTIAAL ALLFSTHSYQ PAPFFVLDEI DAALDNTNIG KVASYIRDHA TNLQTIVISL
     KEEFYGHADA LVGITPAEGD CLISNVYIID LTCFEDK
//
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