ID G9NU45_HYPAI Unreviewed; 1054 AA.
AC G9NU45;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=CNH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIATDRAFT_161191 {ECO:0000313|EMBL:EHK46216.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK46216.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK46216.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK46216.1}.
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DR EMBL; ABDG02000023; EHK46216.1; -; Genomic_DNA.
DR RefSeq; XP_013944371.1; XM_014088896.1.
DR AlphaFoldDB; G9NU45; -.
DR STRING; 452589.G9NU45; -.
DR GeneID; 25776569; -.
DR eggNOG; KOG2063; Eukaryota.
DR HOGENOM; CLU_004190_1_1_1; -.
DR OMA; LFRLPNF; -.
DR OrthoDB; 38195at2759; -.
DR Proteomes; UP000005426; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR PANTHER; PTHR12894; CNH DOMAIN CONTAINING; 1.
DR PANTHER; PTHR12894:SF27; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR-ASSOCIATED PROTEIN 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF10366; Vps39_1; 1.
DR Pfam; PF10367; Vps39_2; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005426}.
FT DOMAIN 18..345
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 694..897
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 53..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 116646 MW; E7CE78D50B12EE35 CRC64;
MLSAFTARPI IELRQRDKSK IETILAHGDR ILVGLNNGAL RVYRLNELPA NGASTPPLTA
NATPPQNGDH PPADSASKPT DLLREIERFS TRAIEQLAII KEANTIVSLS NYHVSLHDLQ
SYDLIETLSR TKNASCFAIT SNIVRDSDTG IPEIISRLAV AVKRRLLLWS WHESELNNDV
SEVVLSESIR SITWASATKI VCGMNSGYVI VDAVTQEIED IVSPGAVGVS GQGSRFGAVS
SAGMGYMGLG SYIPKPLAAK LADGEMLLAK DINTLFVNDE GKALEKRQIP WQTAPESIGY
SYPYIVALQP PSKGSLEVRN PDTLSLMQTI QLPGAAQLHF PPPTSSLAHA GKGFHISSDR
CVWKMGATDY DSQIGELIEA GRFDEAISVL QMLEDALLRN KKETLREVKM LKAEGLFKQK
KFRQSMDLMN EDDVHAPPER VLRMYPPLIA GELSRWANCQ GAQENAETQV RKTNGTRPNS
PEVTTSEHAE SPTVGGFVKY FKGAQKKPTD VASIISTKKD GETEDSDNAR DAPASEDRPL
EGRDLTRAVL ELNSYLAGTR ARLQRVIDPV TGKLKPRVDQ PSSTADAEDR LLKITPDESD
KEREQKLREI FRLVDTTLFR AYMFSQPSLA GSLFRIPNFC DPDVVNEKLL EHNRYTELID
FFHGKKLHKS ALQLLHQFGA APKPNETAPT LHGPDRTIQY LQSLPPSEID LILEHAEWTL
KANPEFAMDI FIGDTENAET LPAEKVLPYL RDLDPKLERQ YLEHIIMELD DTTADFHNRL
VELYVSSLSN SERGHDWDDL EERFVKFLRE SRQVYSLTKA FALIPKDDAA FYEAQAVVLS
NMGQHRQSLE IYVFKMKDYV KAEDYCNRAH RSQASSTTPS DDPDESASSV YHTLLSLYLQ
PPPPHKPNLE PALDLLSKHG SRLPATSTLG LIPDDLPVGS LEAYFRGRIR AANSLVNESR
IMAGLRKAEG ISVAAELQLG DGKPGGQGGR NRHVVITDER HCVVCHKKLA GGMRMGGSVV
AVLTDNTVVH YGCLSKATGN KANGSRKPSW SRGF
//
