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Database: UniProt
Entry: A0A315V2C2_GAMAF
LinkDB: A0A315V2C2_GAMAF
Original site: A0A315V2C2_GAMAF 
ID   A0A315V2C2_GAMAF        Unreviewed;      2312 AA.
AC   A0A315V2C2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Centromere protein F {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=CCH79_00010547 {ECO:0000313|EMBL:PWA17279.1};
OS   Gambusia affinis (Western mosquitofish) (Heterandria affinis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Gambusia.
OX   NCBI_TaxID=33528 {ECO:0000313|EMBL:PWA17279.1, ECO:0000313|Proteomes:UP000250572};
RN   [1] {ECO:0000313|EMBL:PWA17279.1, ECO:0000313|Proteomes:UP000250572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NE01/NJP1002.9 {ECO:0000313|EMBL:PWA17279.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PWA17279.1};
RX   PubMed=29703783;
RA   Hoffberg S.L., Troendle N.J., Glenn T.C., Mahmud O., Louha S., Chalopin D.,
RA   Bennetzen J.L., Mauricio R.;
RT   "A High-Quality Reference Genome for the Invasive Mosquitofish Gambusia
RT   affinis Using a Chicago Library.";
RL   G3 (Bethesda) 8:1855-1861(2018).
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:PWA17279.1}.
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DR   EMBL; NHOQ01002371; PWA17279.1; -; Genomic_DNA.
DR   STRING; 33528.ENSGAFP00000008272; -.
DR   Proteomes; UP000250572; Unassembled WGS sequence.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:InterPro.
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   Gene3D; 1.10.287.1490; -; 2.
DR   Gene3D; 1.20.5.1000; arf6 gtpase in complex with a specific effector, jip4; 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   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; 1.
DR   Pfam; PF10481; CENP-F_N; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000250572}.
FT   DOMAIN          2..314
FT                   /note="Centromere protein Cenp-F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10481"
FT   DOMAIN          1662..1801
FT                   /note="Centromere protein Cenp-F leucine-rich repeat-
FT                   containing"
FT                   /evidence="ECO:0000259|Pfam:PF10473"
FT   DOMAIN          2196..2240
FT                   /note="Kinetochore protein Cenp-F/LEK1 Rb protein-binding"
FT                   /evidence="ECO:0000259|Pfam:PF10490"
FT   REGION          133..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1415..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1512..1553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2018..2038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2103..2312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          21..125
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          179..206
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          851..888
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          924..1357
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1561..1637
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1666..1714
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1788..1829
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        138..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1448..1462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1512..1529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1530..1546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2119..2142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2143..2161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2164..2180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2285..2301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PWA17279.1"
SQ   SEQUENCE   2312 AA;  263333 MW;  59324DAF7A9B551A CRC64;
     AMSWAVEEWK DGLPGKALQK IQEMEVQLDK LKKERTQKQF QLESLEAALQ KQKQKVDSER
     TEISALKREN QSMIESCDAL EKTRQKVVHD LGVKEQQVSY LEGQLNSCRK TIDRLEQELK
     KWQTCRFSFR HKTELDRSQP AGSSSLSTSS SDLQTFSTPQ KTFATPAPVS ALRQPDSKLN
     ELQEKYNHEV EERKKLESEL KLLQVKLLNQ SSVSHKDIAA RQAGSSIFPW QQQDQVHSLR
     GQDVMETPLK RRGASSLWDA EETPIKPSQR MSSSRTVQSP SGSSQQTEQL KSLNQELRGR
     VSELERNLAA QEKEIRTQTS KLQELQTHLN QTRKELSERD RELVKAGHEQ SQAADRYQQL
     EAKCSMVEQK LKQVSEEMSC QRHNAESCRR ALEQKLKDQE RNSQKELAQL QSSHQALDQQ
     LNQTRTKLTQ EVQQAKKDHN VLLADLEKMR LQKSQMEREI EELKQKLLRS EQGLQATQTK
     EQDLRKKMEE LQKEKNALII QLDRSSRSLT QLEEEKRISE QSLKRSQGLL EDLKAKSEGQ
     AEELKRLQSK LEHQTQTAAR ELEDVKKRLS DAEARNDKSQ NELQNQKQNE ELKSNLRQSR
     DKSQAVKQEH QAVKQELQAV KQELQALLEW KKNKENLINQ TEAVQQELTD KIITLEGKAS
     RLHEANNELQ DKISSMEADK ASLSAHVDAL KGELLLRSTE LEEKDHQNQQ LQLHVSEAAQ
     KHGKDLENAG KQLAQLQGQV KDLESRLQRE ASRAQLAEKR SCELQEEQQA ACDLLRSKDQ
     LLELGLAEVS QLKDGLARSA AQQEAQSDSF VKQKAVLLQQ CEESVSAQAE ETERVKLQAE
     EILQFSHTER INALQEQIVC LEKQVSANQE ATEEVSVLKN KLDVVKQSLG HLNKSLEASE
     KSLSCANETK ADLGVTLSEK VKLITALDDQ INNLIEKLKK ESESQSAEVG DFVNMERSLK
     KHLEATKKSV AAAKAELSSR REEIRTMKTT LSAASRGLEE RDNTIKSLKE KLNKAEAEQA
     KTSELLKEKT VAMNKIQVQL EMLQMDLEDN ESAMTSVEEL KGTIASLEAM LEESKAQVSV
     LETRLDEVQS EYSLLETKYV TAKDELLERS CEITRLEEDA VRRQQLEENV SALEAKLSQI
     TEENSKAETE LRQIIQEKES RLDQLNEEKN SLQASLTQSV DEQKRAESEI TRVKAEKAVL
     EERMSNLSKE IQQLHAEVRE LSEQKQEAEA TIDQMAAETQ QTESALRRVS EKKAQLDVAL
     SSASEEKVEL QEKISALTSE NGELVCKVKQ VEEEKLQLES KFSRFSEENV KLQSDMNRLT
     AEKQQLQARA ERLQEEMASL REESQHVQHS LLSAEEEQQM YVPYLSMNQQ FEAEQTALHQ
     KLSVLQTELA VLQQQYDVLQ QQVDQQQCII QQLTESQKHQ NPTGNIPHLE PRDAKDGEAA
     GQTEPNPELG ASVGTSAESD PLNEQEEASE KSPDQAASEA ELIAQEDASD QEMINEEEAH
     KHDAQEIQLH QQVSEENCSS NGDLENENCD ASSSQHEKRG MKFSGDESRP VNDVSVDTET
     ISKQQNELKT LQSEFDLLTS ELQLRAELTS ELEVQVQRLE EKVQAVEKQL STALEEKKSL
     SDQVTQLLEE RESLSLQLET SRCQLTDFME MLEGLEMAKG GWDEKFLQQE SELKRVRSEK
     ANLEQHILGM ESELESMQAE TSRLKEELET QRKTCSGREQ QIETLLTETT QLRAELVSCS
     EDRDELSQSL GQWRDKVHGL EKTNLETRNL ISILEEDIRV GRKEYQGLQS SMERVKAERE
     QVVVLEEAIS KHNREKEGLL NHLHEMEDDH TSTNQNTESM AGKIQALEGE VCRLSQSLES
     SLLEKGEIAS RLNSTQDEVR QMRTGIEKLQ VRIESDERKK KNMGELLKAA QRKSDSLQDR
     IDALEREKDE FEQNLEEAVL QVSELTSSLA CLTKERDSAV SKMNLWMNTC KQLEQEKQNI
     LNSSEGRSSE EFQAEATQLR AQAEVRKKEV QELKTALEKK TTEAEERRQE LRQKEEEVKE
     RAAALEGVRA EKERELEKFR KELDEVNTLL EEKSTEADES MEKYCSLMVK VHKLEESNDA
     LKTRLEQLTA SQPVNEAKLP PETRRRSARK SSSKHQEEKM SENTENLVPT TTPSSPQGWS
     PGKRSHKEIS DRDSAQEALH NLTKKLKANT ATPRGRGGQD DEEFRPEGLP DLVQKGFADI
     PLGEASPYII RRTTGRRCSP RLAARQSQPD VKVLGSVHLQ SPCGSSSDGS DRTRQPVRGE
     QKPPLSVHQE AEQREKPVLM EQTKQGENCH VQ
//
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