Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q54W20

Entry ID Method Resolution Chain Position Source
AF-Q54W20-F1 Predicted AlphaFoldDB

No variants for Q54W20

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54W20

No associated diseases with Q54W20

5 regional properties for Q54W20

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 507 - 737 IPR003439
domain AAA+ ATPase domain 532 - 720 IPR003593
domain ABC transporter type 1, transmembrane domain 74 - 283 IPR011527-1
domain ABC transporter type 1, transmembrane domain 317 - 417 IPR011527-2
conserved_site ABC transporter-like, conserved site 642 - 656 IPR017871

Functions

Description
EC Number
Subcellular Localization
  • Membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
ATP-binding cassette (ABC) transporter complex A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.

4 GO annotations of molecular function

Name Definition
ABC-type transporter activity Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATPase-coupled transmembrane transporter activity Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source.
long-chain fatty acid transporter activity Enables the transfer of long-chain fatty acids from one side of a membrane to the other. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.

4 GO annotations of biological process

Name Definition
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
long-chain fatty acid import into peroxisome The directed movement of long-chain fatty acids into a peroxisome. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
peroxisome organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.
very long-chain fatty acid catabolic process The chemical reactions and pathways resulting in the breakdown of a fatty acid which has a chain length greater than C22.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKKNNVNNIT ETLNSSSSSS SSSGSSSDEE VKSKLNFNQT DEMLKKIKEN KFDWALFKRF
70 80 90 100 110 120
IKIVIILYEK PVIPLLLFLL LFGSGVSQTY ISKFTGILLS NIYGSLTSGD KFLFVSSLIK
130 140 150 160 170 180
GCFAIGGSAL FDAIIKFIVS IMAWNWRKTL CLYIQNVYFK KSLFYKILAF DDRIDNPDQR
190 200 210 220 230 240
ITSDIDNFTT LLSSIVSQCI TGPMVVVYYT YLCYTTIDWY APLIVYGYFF LGYFINKLVM
250 260 270 280 290 300
SPMVSINYLQ DKLEGDFRYL HQRIRNFSES IALYNLSKEK QQKKSTTSVD NLDYYDDDHH
310 320 330 340 350 360
YHHHHDDGEE SDEYTDKTKI INRKNKNSKN KRSALLKRSN KNIKNEELLV EEEQAKQQFE
370 380 390 400 410 420
ALLKNKKRVI FWQFGLNTTS DMFTFFSPLI NYFIISIPVF FLSSKAALEP AQVTVQSYNC
430 440 450 460 470 480
IMLASGFSQY INVSQSISDL SGYISRISTM IEVCKKVMGD TSLDIEITKL NEKDKTKSLP
490 500 510 520 530 540
NSLIINNRDT SINTDFRHIS LNEGESITLD DVTYFTPKGT QLYEKISICI KKGNNLLIMG
550 560 570 580 590 600
PSGSGKSSLI RIINGLWPFF KGSINRPENE DMFFLPQQPY LIFGTLEEQI LYPFSKKQKR
610 620 630 640 650 660
IPKSIMRELF QRFDIDYLLD RERFIKKSAQ VNDLTHNWLN QLSPGEQQLI AIIRLIYHKP
670 680 690 700 710 720
KFALMDESTS SIPQSLEERV YSVAKELGIT IISVGHRISL LKYHSTLLRF DKDKNWYLED
730 740
IINQNNQSNN INTINIDNNT NKIAEDSVFD