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Database: UniProt
Entry: K2RPG9_MACPH
LinkDB: K2RPG9_MACPH
Original site: K2RPG9_MACPH 
ID   K2RPG9_MACPH            Unreviewed;      1677 AA.
AC   K2RPG9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=MPH_08150 {ECO:0000313|EMBL:EKG14677.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG14677.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG14677.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG14677.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles. {ECO:0000256|PIRNR:PIRNR002290}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR002290}. Membrane, coated pit
CC       {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR002290}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC       {ECO:0000256|PIRNR:PIRNR002290}.
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:EKG14677.1}.
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DR   EMBL; AHHD01000338; EKG14677.1; -; Genomic_DNA.
DR   STRING; 1126212.K2RPG9; -.
DR   VEuPathDB; FungiDB:MPH_08150; -.
DR   eggNOG; KOG0985; Eukaryota.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   InParanoid; K2RPG9; -.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR   GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR   GO; GO:0071439; C:clathrin complex; IEA:InterPro.
DR   GO; GO:0032051; F:clathrin light chain binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 1.25.40.730; -; 1.
DR   Gene3D; 2.130.10.110; Clathrin heavy-chain terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR016025; Clathrin_H-chain_N.
DR   InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR   InterPro; IPR016341; Clathrin_heavy_chain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10292:SF1; CLATHRIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR10292; CLATHRIN HEAVY CHAIN RELATED; 1.
DR   Pfam; PF00637; Clathrin; 7.
DR   Pfam; PF13838; Clathrin_H_link; 1.
DR   Pfam; PF01394; Clathrin_propel; 3.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM repeat; 6.
DR   SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR   PROSITE; PS50236; CHCR; 7.
PE   3: Inferred from homology;
KW   Coated pit {ECO:0000256|PIRNR:PIRNR002290};
KW   Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR002290};
KW   Membrane {ECO:0000256|PIRNR:PIRNR002290};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT   REPEAT          541..687
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          690..832
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          838..977
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          984..1129
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1133..1274
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1279..1425
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1428..1571
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REGION          1619..1677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1619..1633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1677 AA;  189614 MW;  B34FFC25DE2E56EC CRC64;
     MAPLPIKFSE LLQLSQVDIL PTSIGFNSCT LESDSYICVR QQADQAASPE VIIIDLKNGN
     NIIRRPIKAD SAIMHWNKQI IALKAQQRTL QIFDLAQKAK LKSATMNEDV VFWKWYSESS
     LGLVTENSVY HWNVLDPNQA TPVKIFDRNP NLSGCQIINY RVNHDEKWSV IVGISQQQGR
     VVGAMQLYSR DRGISQNIEG HAAAFGTLRI EGAPADTKVF TFAVRTATGA KLHVVEIDHQ
     AGNPQFAKKA VDVYFPSEAT NDFPVAMQVS QKYNIIYLVT KYGFIHLYDL ETGTCIFMNR
     ISSDTIFVTA PDSDSAGIIG INRKGQVLSV TLDENTVIPY LLQNPANGEL AYRLASRAGL
     PGADNLYQQQ FENLLASGQY AEAAKTAANS PRGFLRTPQT IERFKQAPPQ QGQLSVILQY
     FGMLLDKGKL NQFETLELVR PVLQQGRKHL LEKWLGEGKL ECSEQLGDIV RLHDLNLALT
     IYQQAGSSQK VVAALAELGR FDEILPYAKE SGYTPDFTVL LQHIVRVNPE KGAEFATALA
     KEESGPLIDI DRVVDIFQSQ GMVQQCTAFL LDVLAPNLPE QGHLQTKLLE MNLLNAPQVA
     DAILGNEMFS HYDKARIAQL CENAGLLTRA LEHNDDPTAI KRIIIHTDKL PEEWLINYFG
     HLTVDLSLDC LDEMLKVNIR QNLQAVIRIA QKYSDLLGPT RIIDLLEKYR TAEGLFYYLG
     GIVNLSEDKD VVFKYIEAAT AMGQLNEVER ICRENNFFDP EKVKNFLKEA RLTEQLPLII
     VCDRFNFIHD LVLYLYKQQQ FKSIEVYVQR VNPSRTPAVI GGLLDVDCDE NIIKGLLQSV
     NPASIPIDEL VSEVETRNRL KLLLPFLEAT LASGNQQQAV YNALAKIYID SNNNPEKFLR
     ENDQYDTLTV GKYCEARDPN LAFIAYQKGQ NDLELINITN ENSMFKAQAR YLLERSDPEI
     WDYVLSSNNL FRRSVVDQVI ATAVPESQEP DKVSVAVKAF IGNDLPGELI ELLEKIILEP
     SAFSDNPTLQ NLLMLTAAKS DKGRLMGYIQ QLENYTADDI AAQCIELGMY DEAFEIHKKH
     NNHTEAVSVL VDHIVSIDRA QEYADRVDLP EVWSKVAKAQ LDGLRVTDSI ESYIRAQDPS
     NYNEVIEIAT HAGKDEDLIK FLKMARKTLR EPPIDTGLAF CYARTNQLAE LEDFLRATNV
     ADVEASGDKA YEEGYHEAAK IFFTSISNWA KLATTLVHLE DYQAAVECAR KANSTKVWKQ
     VNEACVAKKE FRLAQICGLN LIVHAEELSD LVKQYERNGY FDELIALLEA GLGLERAHMG
     MFTELGIALS KYHPERVMEH LRLFWSRINI PKMIRACEEA HLWPELVFLY VHYDEPDNAA
     LAMMERAADA WEHHSFKDTI VKVANLEIYY RALNFYLQEQ PSLLTDLLQA LTPRVDVNRV
     VRMFEKSDNI PLIKPFLLNV QSQNKRAVNN AINDLLIEEE DYKTLRDSVE NYDNYDAVEL
     AQRLEKHDLV FFRQIAANIY RKNKRWDKSI ALSKQDKLFK DAIETAAMSG KPEVVEELLR
     YFVDIGSREC YVGMLYACYD LIRPDVILEV SWRNGLHDFT MPYMINFLSQ QAATIEQLKK
     DNEERKAKEQ SQQKNEESTP ILGASRLMLT QGPSAPSPAP YGQANGIAPQ ATGYRAF
//
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