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Database: UniProt
Entry: B3MGM6_DROAN
LinkDB: B3MGM6_DROAN
Original site: B3MGM6_DROAN 
ID   B3MGM6_DROAN            Unreviewed;      1748 AA.
AC   B3MGM6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV36784.1};
GN   Name=Dana\GF11779 {ECO:0000313|EMBL:EDV36784.1};
GN   Synonyms=dana_GLEANR_11809 {ECO:0000313|EMBL:EDV36784.1};
GN   ORFNames=GF11779 {ECO:0000313|EMBL:EDV36784.1};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV36784.1, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV36784.1, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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   -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000256|PROSITE-
CC       ProRule:PRU00841}.
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00841}.
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DR   EMBL; CH902619; EDV36784.1; -; Genomic_DNA.
DR   RefSeq; XP_001959962.1; XM_001959926.2.
DR   EnsemblMetazoa; FBtr0116479; FBpp0114971; FBgn0088819.
DR   GeneID; 6494641; -.
DR   KEGG; dan:6494641; -.
DR   eggNOG; KOG3654; Eukaryota.
DR   HOGENOM; CLU_003076_0_0_1; -.
DR   OMA; EANHYII; -.
DR   OrthoDB; 2918432at2759; -.
DR   PhylomeDB; B3MGM6; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR   GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 3.10.20.360; CKK domain; 1.
DR   InterPro; IPR032940; CAMSAP.
DR   InterPro; IPR022613; CAMSAP-like_CH_dom.
DR   InterPro; IPR031372; CAMSAP_CC1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR038209; CKK_dom_sf.
DR   InterPro; IPR014797; CKK_domain.
DR   InterPro; IPR011033; PRC_barrel-like_sf.
DR   PANTHER; PTHR21595:SF0; PATRONIN; 1.
DR   PANTHER; PTHR21595; UNCHARACTERIZED; 1.
DR   Pfam; PF17095; CAMSAP_CC1; 1.
DR   Pfam; PF11971; CAMSAP_CH; 1.
DR   Pfam; PF08683; CAMSAP_CKK; 1.
DR   SMART; SM01051; CAMSAP_CKK; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50346; PRC-barrel domain; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51508; CKK; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|PROSITE-
KW   ProRule:PRU00841}; Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT   DOMAIN          156..288
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          1607..1741
FT                   /note="CKK"
FT                   /evidence="ECO:0000259|PROSITE:PS51508"
FT   REGION          332..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          791..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          969..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1097..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1294..1336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1379..1410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1430..1557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          671..705
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          735..769
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        354..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..888
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..940
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1044
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1228..1279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1311..1335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1444..1460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1479..1541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1748 AA;  196855 MW;  9F50A71AA6B13BDB CRC64;
     MDAETQEIRQ ARQRASVKWL LSKAFNNRVP DNLKEPFYRD HENQERLKPQ IIVELGNATL
     YCQTLSNLYS DPNYQSLNHW SILQTLARKG VPVAESSDMP ITETVLIQTN PLRINAHMSV
     IESLMVLYAK EISSGDRVMA AIRRISGSNY QAPPGQSYEQ ALLAWISHAC AALKKRIIKE
     VETGLPDDNG SRLQTPDIPP VRDFQDLCDG ICLALLISYY CPKVVPWTSV RINYLPAVED
     SIHNILLVGN FSQKHLPYSV FHMTPEDVTY MRGSMKLNLV LLLTDLFNLF EIHPAKCVCY
     PGMDGQDVIA RRSLGANEHG ICHRRGLTVQ PVTPIPDLRS DLDTPPVGSP SNRPPFQVPH
     SNSFGGGLNR RSTPPTEYQT VQTNNFDSNH EEAFVVHKSR GITTLASMHS QHQQQQQQQQ
     LHQQQQQQQY QHQQSQLQLQ QQEPLVPARL RQAKEKTNVD SKADERGDYA AAGRPSNWEQ
     SRRPSFAGRR SRRNSSSEDS QLTIENFGGS QDQLNTLGRF DRERDRERKL SNTSIVVEPA
     VAIRSSIADA RGTLQLGYDT DSGSEKQDRE TEKYSMRRQA SVDNVPTVSS HNLSNAGSPL
     PTARHKQHSI DKDYNNSSMM ADGGYSDARS TSGYDPESTP VRKSSTSSMP ASPAAWQLDV
     GDDDMRSLEN ASKLSTIRMK LEEKRRRIEQ DKRKIEMALL RHQEKEDLES CPDVMKWETM
     SNESKRTPDM DPVDLDKYQQ SIAIMNMNLQ DIQQDIHRLA TQQSQMQAQH LQAQQLMQAQ
     QIANMLNQQQ TYGSQQHLAD HHYQQPRPMQ QSFGSSPHLP QAYNYSSRPP SRDPYQQHQQ
     QQQPMAMPQP MQFVNEHGQY MSPPQPAHYM SPQQHQQQPQ SIYSDNGAAY NHSPYGGAPP
     PQYRSSVVYD DYGQPTNHFY LHESSPQPPH PQQQHPQRRT WAHSAAAAAY EQQQHQQMQQ
     PLVDVNAWQT QQQPKQPKQT WMNRPPSSAG APSPGSFVLH QNGAGNGGGG ELQHLFQVQA
     SPQHRGANGV QRQQSLTNLR DNRSPKAPQP MGMPMDLPMQ PEDMMAPQSI CFIGDEEDVD
     ELERNIIESM QSTRISDFVH QQQQQHHQQQ KLQQQQQRLQ GHSGRGSSSE DYDSGEMISN
     KLNITSGNLT YRIPSPSRPS IQANSFQDPR VAAPAAAAPG EDQPPEKGFY ISFDDDQPKR
     PKPPLRAKRS PKKEAPPGSR DSVDQAIKRE SLSQLHNNNN IGIGGEDSNN KTVTRHSVHG
     LNNSNSVKSP GNATYNKYTD EPPIQLRQLA VSGAVSPTGH ERRHLEDVTN QSPHQQHQQP
     PMSPTRLQHS NQAAEAARNK ALVIGVDATN LDPDSVDEME RRKEKIMLLS LQRRQQQEEA
     KARKEIEASQ KREKEREKEE ERARKKEEQM ARRAAILEQH RLKKAIEEAE REGKTLDRPD
     MHVKLQPQSS TSTTPRLRQQ RTTRPRPKTI HVDDASVDIS EASSISSRGK KGSSSNLTGY
     GQLSSNSMKR DYYRGSQDSL TVKESPDDYP STSSTPIGRR GSYKTSREPA GVERGRTLSR
     ISVAKGSTLN FRGRKSNSLM NLCDSGLGRA TPPRRAPSPG MGMGASGPKL YKQPAAKSNR
     GIILNAVEYC VFPGVVNREA KQKVLEKIAR SEAKHFLVLF RDAGCQFRAL YSYVPETDQV
     TKLYGTGPSQ VDEVMFDKFF KYNSGGKCFS QVHTKHLTVT IDAFTIHNSL WQGKRVQLPS
     KKDMALVI
//
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