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Clathrin heavy chain

 A0A0F8BJ41_CERFI        Unreviewed;      1859 AA.
A0A0F8BJ41;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
23-MAY-2018, entry version 19.
RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
Name=chc1 {ECO:0000313|EMBL:KKF92273.1};
ORFNames=CFO_g5373 {ECO:0000313|EMBL:KKF92273.1};
Ceratocystis fimbriata f. sp. platani.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Ceratocystidaceae;
Ceratocystis.
NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF92273.1, ECO:0000313|Proteomes:UP000034841};
[1] {ECO:0000313|EMBL:KKF92273.1, ECO:0000313|Proteomes:UP000034841}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CFO {ECO:0000313|EMBL:KKF92273.1,
ECO:0000313|Proteomes:UP000034841};
Belbahri L.;
"Genome sequence of Ceratocystis platani, a major pathogen of plane
trees.";
Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
coated pits and vesicles. {ECO:0000256|PIRNR:PIRNR002290}.
-!- CATALYTIC ACTIVITY: 2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' +
H(2)O(2). {ECO:0000256|RuleBase:RU371123}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|RuleBase:RU371123};
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
{ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
{ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
{ECO:0000256|PIRNR:PIRNR002290}. Membrane, coated pit
{ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
{ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
{ECO:0000256|PIRNR:PIRNR002290}.
-!- SIMILARITY: Belongs to the clathrin heavy chain family.
{ECO:0000256|PIRNR:PIRNR002290}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KKF92273.1}.
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EMBL; LBBL01000477; KKF92273.1; -; Genomic_DNA.
EnsemblFungi; KKF92273; KKF92273; CFO_g5373.
Proteomes; UP000034841; Unassembled WGS sequence.
GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
GO; GO:0071439; C:clathrin complex; IEA:InterPro.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0032051; F:clathrin light chain binding; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0016972; F:thiol oxidase activity; IEA:UniProtKB-UniRule.
GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
GO; GO:0006895; P:Golgi to endosome transport; IEA:EnsemblFungi.
GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
Gene3D; 1.20.120.310; -; 1.
Gene3D; 1.25.40.10; -; 3.
Gene3D; 2.130.10.110; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
InterPro; IPR016025; Clathrin_H-chain_N.
InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
InterPro; IPR016341; Clathrin_heavy_chain.
InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF00637; Clathrin; 7.
Pfam; PF01394; Clathrin_propel; 2.
Pfam; PF04777; Evr1_Alr; 1.
PIRSF; PIRSF002290; Clathrin_H_chain; 1.
SMART; SM00299; CLH; 7.
SUPFAM; SSF48371; SSF48371; 6.
SUPFAM; SSF50989; SSF50989; 1.
SUPFAM; SSF69000; SSF69000; 1.
PROSITE; PS50236; CHCR; 7.
PROSITE; PS51324; ERV_ALR; 1.
3: Inferred from homology;
Coated pit {ECO:0000256|PIRNR:PIRNR002290};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000034841};
Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR002290};
FAD {ECO:0000256|RuleBase:RU371123};
Flavoprotein {ECO:0000256|RuleBase:RU371123};
Membrane {ECO:0000256|PIRNR:PIRNR002290, ECO:0000256|SAM:Phobius};
Oxidoreductase {ECO:0000256|RuleBase:RU371123};
Reference proteome {ECO:0000313|Proteomes:UP000034841};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 1685 1709 Helical. {ECO:0000256|SAM:Phobius}.
REPEAT 541 690 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
REPEAT 693 835 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
REPEAT 841 980 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
REPEAT 987 1132 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
REPEAT 1136 1277 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
REPEAT 1282 1428 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
REPEAT 1431 1574 CHCR. {ECO:0000256|PROSITE-
ProRule:PRU01006}.
DOMAIN 1737 1837 ERV/ALR sulfhydryl oxidase.
{ECO:0000259|PROSITE:PS51324}.
COILED 1616 1636 {ECO:0000256|SAM:Coils}.
SEQUENCE 1859 AA; 208833 MW; C4191C8AB3724615 CRC64;
MSPLPIRFTE LVQLTSLGVD PAAVTFNACT LESDAFVCVR EKKNEAAQPE VVIVDLKNGN
NVIRRPIKAD SAIMHWSKQV IALKAQSRTL QIFDLANKSK IKSATMNEDV QYWKWITETS
LGLVTDTSVY HWDVFDASQA MPVKMFERNP NLSGCQIINY RINSDGKWMV VVGISQQGGR
VVGSLQLYSK DRGISQAIEG HAATFGTIQR DGCSSETKVF AFAVRTAAGA KIHIVEIDHV
EGDPVFPKKA VDMYFPEEAT NDFPVAIQVS QKYGIIYMVT KYGFIHLYDL ETGSCLFMNR
ISSETIFTTC PETEGGGIVG INRKGQVLFV TVDETNMVPY LLQNPANTEI AIKLASRGGL
AGADDLYGRQ FEQLFNSGNY MEAAKIAANS PRGFLRTPQT IEKFKRLPAV AGQMSYILQY
FGLLLDKGAL NTHETLELAQ PVLAQNRKAL LEKWLGEGKL DCSEQLGDLV RPHDLNLALT
IYLKANVPYK VVAAFAETGQ FDKIIPYSSK VGFTPDYIQL LQHIVRVNPE KGAEFATSLA
NNEGGSLVDL DRVVDIFQSQ GMIQQGTAFL LDALKDNSPE HGHLQTRLLE MNLVQAPQVA
DAILGNDMFT HFDKGRIATL CEQAGLFQRA LELYEDPEAV KRVVVGIAGT PNFNLDWLTT
FFGKLSVEQS LTCLDAMMKH NIRQNLQAVV QVATKYSDLL GPVHLIDLFE KYKTAEGLFY
YLGSIVNLSE EPDVHFKYIE AATKMGQFNE VERICRDSNY YNPEKVKNFL KEAKLAEQLP
LIIVCDRFGF VHDLVLYLYQ NRQFQAIEAY VQRVNAARTP EVIGGLLDVD CDEDIIKKLL
STVNAASIPI DQLVEEVEKR NRLKILLPFL EATLAAGSQQ QALYNALAKI YIDSNNDPER
FLKENSQYDS LVVGKYCEKR DPQLAYIAYS KGQNDLELVN ITNENSMYRA QARYLLERAD
RELWKFVLSE NNVHRRFVID QVISTAVPES TDPAKVSEAV AAFLECDLPL ELIELLEKIV
LEPSPFSDNQ NLQNLLMFTA AKADKARVMD YIHKIDGFSA PEIATACIDV GLHEEAFEIY
KKTGDKLSAV DVLVDNIVSI DRAQSFAEDV DLPEVWSKVA KAQLDGLRVS DGIESYIKAE
DPKNYSEVIE ISVHAGKDED LIKYLRMARK TLRETEIDTA LAFCYARLDQ LSDLEDFLRG
TNVANIEESG DKAYAEGLYE AAKIFFTSIS NWAKLATTLV YLDDYQAAVE SARKANNIKV
WKEVHGACVN KQEFRLAQIC GLNLIIDAEE LQSLVKQYER NGNFDELISL LEQGLGLERA
HMGMFTELGI ALSKYRPEKL MEHLNLFWSR LNMPKMIKAC EEANLWPELV FCYQHYDEFD
NAALAIIERA ENSWEHHHFK EIVVKVANLE IYYRAIKFYM EQHPSLLTDL LQILTPRVDV
NRVVKLFQKN DDLPLIKPFL LNVQSQNKRI VNDAINDLLI EEEDYKTLRD SVENYDNYDA
VDLAGRLEKH DLIFFRQIAA SIYRKNKRWE KSIALSKQDK LFKDAIETAA ISGKTEIVQD
LIRYFVDIGS RECYVGMLYA CYDLLRPDFV LELSWRNGLN DFTMPYMINM LAQQTKELAA
IKADNEARKA KEAENNTEEA TGPILGMNRL MITAGPSGAM PANGFAPQPT GCQLRSTMMA
RKTPILLAVA ALLSIMYFFS GPGSGLSAAD YAMPKFDLSQ IGDNILKGGS IAPKLGNATA
KAELGRASWK VLHTMMARFP EKPTEDESTA LLTYITLFSR LYPCGECAAH FRKLLAKYPP
QVTSRNAAVG WACFAHNVVN ERLKKPIFDC ANIGDAYDCG CADSDKAMRE GHDTRLELE


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