A2QUR1

PR
Gene name
sfh5 (An09g06480)
Protein name
Phosphatidylinositol transfer protein sfh5
Names
PITP sfh5
Species
Aspergillus niger (strain CBS 51388 / FGSC A1513)
KEGG Pathway
ang:ANI_1_844084
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-168 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A2QUR1

Entry ID Method Resolution Chain Position Source
AF-A2QUR1-F1 Predicted AlphaFoldDB

No variants for A2QUR1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2QUR1

No associated diseases with A2QUR1

2 regional properties for A2QUR1

Type Name Position InterPro Accession
domain CRAL-TRIO lipid binding domain 175 - 352 IPR001251
domain CRAL/TRIO, N-terminal domain 97 - 154 IPR011074

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Endoplasmic reticulum membrane ; Peripheral membrane protein
  • Microsome membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
phosphatidylinositol transfer activity Removes phosphatidylinositol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADQPEKTAA APAAPEAQPP TTATTTTEPA VSESQTQPEP QPEAEQKVEQ ATTGEEASPA
70 80 90 100 110 120
PAATEPPVTE PTPAPAQEAP EDKKEEAPKE ETKETKAEES KEEQKAEEPA AEPKAEAAKE
130 140 150 160 170 180
EEQKPAQPEY LAKNPALSQF FDRLSAILSS TGHNEMWGVT LKDSSDVPTV NILIKFLRAN
190 200 210 220 230 240
EGNVKLAEEQ LTKALQWRKE MNPLALTEGR YSAERYGGLG YVTKYPEANG KETIVTWNVY
250 260 270 280 290 300
GNVKSIDQTF GDVDGFIKWR VALMELAVKD LKLSEATTVI DYDGEDPYQM LQVHDYQNVS
310 320 330 340 350 360
FLRLNPTIKA ASKKTIEVFS MAYPELLREK FFVNVPAIMG WMFAAMKVFL SKNTTRKFHP
370 380 390 400 410 420
ISNGANLARE FPSLKDKFPK TYGGNGATLE EDAFTVNLEK AEPAPEAPKE EPKEESKQEQ
430 440 450 460 470
AEAPKEEAKA EQAEAPKEEV KEEAKEEAKT EQPAAEEPAK AEAAVTTQEA PAAAEAK