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Database: UniProt
Entry: A0A498MVL7_LABRO
LinkDB: A0A498MVL7_LABRO
Original site: A0A498MVL7_LABRO 
ID   A0A498MVL7_LABRO        Unreviewed;      2556 AA.
AC   A0A498MVL7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   05-FEB-2025, entry version 19.
DE   SubName: Full=Centromere F {ECO:0000313|EMBL:RXN20675.1};
GN   ORFNames=ROHU_024767 {ECO:0000313|EMBL:RXN20675.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN20675.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN20675.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN20675.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN20675.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:RXN20675.1}.
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DR   EMBL; QBIY01012633; RXN20675.1; -; Genomic_DNA.
DR   STRING; 84645.A0A498MVL7; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0000922; C:spindle pole; IEA:TreeGrafter.
DR   GO; GO:0070840; F:dynein complex binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051310; P:metaphase chromosome alignment; IEA:TreeGrafter.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:TreeGrafter.
DR   GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:TreeGrafter.
DR   Gene3D; 1.10.287.1490; -; 3.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR043513; Cenp-F.
DR   InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR   InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt.
DR   InterPro; IPR018463; Centromere_CenpF_N.
DR   InterPro; IPR025925; PPC89_CLD.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR18874:SF10; CENTROMERE PROTEIN F; 1.
DR   PANTHER; PTHR18874; CMF/LEK/CENP CELL DIVISION-RELATED; 1.
DR   Pfam; PF10490; CENP-F_C_Rb_bdg; 1.
DR   Pfam; PF10473; CENP-F_leu_zip; 2.
DR   Pfam; PF10481; CENP-F_N; 1.
DR   Pfam; PF14197; Cep57_CLD_2; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT   DOMAIN          106..258
FT                   /note="Centromere protein Cenp-F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10481"
FT   DOMAIN          1659..1799
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          1897..1997
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2211..2274
FT                   /note="PPC89 centrosome localisation"
FT                   /evidence="ECO:0000259|Pfam:PF14197"
FT   DOMAIN          2415..2455
FT                   /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT                   /evidence="ECO:0000259|Pfam:PF10490"
FT   REGION          155..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1394..1416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1511..1545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2340..2388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2457..2490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2504..2556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          725..822
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          847..930
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          983..1231
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1270..1332
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1418..1489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1551..1634
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1670..1711
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1754..1837
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1873..2079
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        158..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1515..1524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1525..1536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2355..2372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2461..2481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2504..2516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2556 AA;  292613 MW;  7A5623B4748628C6 CRC64;
     MGSIFAETNV YMLHMMYQAM GVCLYMQDWD GAMKYGEKII QPYSVHYPPY SLNVASMYLK
     LGRLYLGLEK KTQGVKALKK ALAVMDIAHE HARVSLRSNT AFSVNMSWAV EEWKDGLPAK
     ALQKIQEIEA QLDKLKKERQ QKQFQLDSLE ATLQKQRQKM DSEKSEASAL KRENQSLVES
     CEGLEKTRQK LTHDIQTKEQ QVNYLEGQLN SSKKQIDRLE QEIKKYKHDL ERSQTSHASE
     IQQFTTPQKT FATPATPNHW QQDLRSKISE LELRIQAQEK EMKNQINKFS EIQSQLEMAK
     KDLAEKDKLL SKSRDELTKA TGQYEQSVSK CSSLEMKLKQ ELAQLQSSHQ ALDQQFNQVK
     NKMSMEIQQA KKDHNVLQSD MDKVTALKNR LEKDLEELKQ KLLRSEQALQ ASQVKETELK
     KKSDEMQREK NSLSCQLDQG MKRVKQLEDE KQNIEQNLAK NRTMVDDLKV KTQTQSEELT
     ELRKKMDRQS ASSAQELENA KKTLAEIEAK NTKTQAELQK LVHEVELKAS KICAMEKENE
     DLKMTSNSCQ KEVAEIKKEY EALLQWKTEK EQLINNTESN REEMLSKIAD LASDKAKLND
     AQDGLQKRMQ DLENEKICLS GQIDSLKGEL LVKCVELEEK GRVYEELQQQ FSETHQKHNK
     EMDNLKQQIT LMQEQVSELE AKLHQETSKV DGLEKAHGQL LAEYESACDL AKSKDSIIEM
     NKTKIEHLQE TFALQEQELE KFKEEKEMLA KECEDHLVQN KELEQEKLNM ETSLQEVLEK
     IALLESDLKS QKDSNADIQA KYDDLSKVKE DLAEKVSLVE KREKDLVLEV ESLLQKNKSF
     GSLEEQFNSL VSEAEETRSS LEKLKELQVQ TATELGHQKT IAENLVKDIE EERRKASSLE
     HDNAQLKVKQ QEVENKINDL AEKYESLQKS HDIVCQEKEN LLTQVSEMTG ALAERDAMAE
     TIVLTQTELE ASNHLSTTLK NSLESLQKQF DSSVEQNLSL EKNVQGLSEE KALLETSIKE
     LTERHNKETE VHVSEMETHL KKQNSLEEQI SVIEAELQSK CLQARNASEK QEEAALEIVQ
     LKQDFDLSKD QLREVTDSYQ KVAKELEDLK QSASPHEQEI ESLKAALADL KSQEAAKTCE
     VKTLKEKLKE SQSEQAKVLE TLNEKNIKLS KIEVQLEMLQ MDLEDNETCI NSFDAQVEAL
     QGNISVLEAK LGESEAQRSI LQTELESVKE DYAKSALEVS QLSACLEETQ KEQQSSSALV
     AELESLRVTH ETLKVSLEQE NCKLANLEAM YNNLMEQKLK LESNIQELKA DAQNSLKQID
     QLKQANDSLV SQFAEQQTYI AQLQSEKIPA ANSDADTLKK AQTVDDNDQD ICEMPFANTS
     ILPFEEDVAV QGISSPGEHL DSQEETQTSL SSDEDGKHVL LKEQMQNTNR ELEKAIRTME
     EQTGVKIEQL KLQHAEELQR MEQQMLCIRN ELEAKLREEK QHTEILSSQL EATMQQLQEL
     DLASSSLLAT ETSQEMEKMT HEAQENITHQ PEQSDSAPDI SPESEKSLVE LETLKETLRK
     REAELVHLQS QFELLESEMA VRKDLCSDLE GKIREMEGEK TNVTDKLTSG TQENQKMNNH
     IGKLTEEIDS LRLQLQTSTC QLSDVMEMIE SLEMAKGEWS EKFFQTESEL KRVRSEKANL
     EKHILSMEAD IEEIQEQKQK QAADLEAVRR TNCSLEQQLN MTMAEGGRLK EELILCADER
     ESENLSLIKW KEKAELLEKR ESNTRELIKE LEEDIRMGKR QNEATSNQID ALLKEKEQLV
     QQSQNLENTV SLLNEDKKNL LSELNSLKNN ENFASRESEN MSSKIHSLEH ENIRLSQSLE
     SSLLEKGEIA SRLISTQEEV AQMRQGIEKL KVRIESDERK KNHMSQLLKA AQRKADVLQD
     NIERLEREKE LSEQNLEDAV LQAETAKAEL EESLQSENKE FAQRVLEYER CQVELRSSND
     LLLKDFENKQ QELSEENARL QSQIAELQAL SSVKEERDEL KKDKAELQSI IAQLEETTQM
     QSTKIEVLQT SVASLENNIQ QLESQLDAMK LMNTELTEKL NALHESSLHL QTQHQHELCE
     ARERQNALEI NQNLLACQLQ ESQKQIETYK LSLEALTTEK DGLQKNVSDI QESHDVQIKK
     NNRRHEENLK HVQQQHEMER NGLKEEIKAV EEKAAQYLSD LNSFKSQNAD VDSTLKELQN
     KLEHFEKEKA ELDSKIVRLS KEKDSAMSKI NLWMKSCKQL ETEKQALQEE LQQQGQALTD
     SQKQGDAENG DALQEELQEL KEALEEKSRE ADESMDRYCS LMVKVHKLEE TNESLKNQLK
     QLSIQTKTPK TRRSLRSEKS DLENSKPVED KANVPGGKRP RAVDDTPNKA QEALHSITKR
     LKAAATTPKA TLDVDDEDFR PEGLPELVQK GFADIPLGEM SPFIIRRTTV QRCSPRLAAQ
     KTATQQSSVS TEHPVQISRQ TAEGRKSYPV QAPKAIQSNA AVLSPLTNSP QKNSCESLLP
     ASAQKISRRS RSFKKSPEKQ ERVCASPKEN DNCQVQ
//
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