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 Q54BT5

Entry ID Method Resolution Chain Position Source
AF-Q54BT5-F1 Predicted AlphaFoldDB

No variants for Q54BT5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54BT5

No associated diseases with Q54BT5

8 regional properties for Q54BT5

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 500 - 735 IPR003439-1
domain ABC transporter-like, ATP-binding domain 1292 - 1527 IPR003439-2
domain AAA+ ATPase domain 528 - 714 IPR003593-1
domain AAA+ ATPase domain 1322 - 1512 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 26 - 428 IPR013525-1
domain ABC-2 type transporter, transmembrane domain 861 - 1240 IPR013525-2
conserved_site ABC transporter-like, conserved site 636 - 650 IPR017871-1
conserved_site ABC transporter-like, conserved site 1429 - 1443 IPR017871-2

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
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.

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.
lipid transporter activity Enables the directed movement of lipids into, out of or within a cell, or between cells.

2 GO annotations of biological process

Name Definition
lipid transport The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
sorocarp morphogenesis The process in which the sorocarp is generated and organized. An example of this process is found in Dictyostelium discoideum.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGEFKFQLVT LLKKNSLLKG KSKIKFIGEI LAPMIVIGIL FGLLYLSAII QPDFSPRYAS
70 80 90 100 110 120
GFTEVVGRLK KLLVATNGPL VPYQQTIVNN LRKQIKLAHP DYTNEYIDQC FEIFQDFESM
130 140 150 160 170 180
QGYFLDPENY RGVMGGLWFD ENDYRYNAPK VLKYSISVDA DYTNDNNIQI SPRSDSQIYL
190 200 210 220 230 240
RHYFTQIQTA VDQAIFMAQN VEIPMVVTGQ RFPNPYIHLW QTWTDGRNMI LKETGGIFIT
250 260 270 280 290 300
AAIFVGLFTT ITNMVMEKES KILEAMKIMG LHSLPYYVSI AISSCYTIIP STIIVIVVLK
310 320 330 340 350 360
GSQLIWTTQW YILTIILILF SISLILLAFI LSKFFNRSKF AGLVCFLIVL IMAGIGIAVN
370 380 390 400 410 420
HINVSTTVKL IFCLLSPVAI SLANYSMSMK DLELVKIVNP DWSIIVSENQ VIGMLILDVV
430 440 450 460 470 480
LYAALVWYID NIISGEFGQS KPFYFFLTKS YWCKKNANEN DLVDLSKAIE SPLYLRKKDL
490 500 510 520 530 540
DYNNSQDFEL NEIHSSKATI QIRKLRKEFK TGDGKRVAVD DLSIDMYQDR IHCFLGPNGS
550 560 570 580 590 600
GKSTTIGMLT GLITCTRGSA LINGLDINQN IDLIRKNIGV VLQQDIIWDN LTVLEHLIFY
610 620 630 640 650 660
AQLKGYSNLK EAKTEAKKMG IEVGLELKLH NKAGTLSGGQ KRKLCLGIAF IGPNSNILFL
670 680 690 700 710 720
DEVSSGLDPL SRSEVQDFII SKKKGKTIIL STHYMDEADL LGDTISIIAH GKLKCNGSPL
730 740 750 760 770 780
FLKNRFGVGY LLTITKKSTE FNKDSVMEIT NKYIKQAHIL SDAGTELSIR LPMESLPMFS
790 800 810 820 830 840
QYFKHLEDCK NQLLIDSYGI SISTLEEVFL KIGQETLKST PNFNDPAVKE ALSTKSSGVK
850 860 870 880 890 900
VGQQLKGLLI KRICTTKKDF KSFMFSIVVP LIILALGLVM YKNMRTIETF NDVTTPLTFS
910 920 930 940 950 960
IDDYGDNIYV PWSISGQNQA IDLRIKNSIG KSNHSKLLPA DELEDYLTLN YEGNPGAFAF
970 980 990 1000 1010 1020
GKTIIEDIEM LSFKVYYNRD YLHALPIYIN FVDNLMLSNL GGVGIQTTSR PFQHIKSKFE
1030 1040 1050 1060 1070 1080
LATEKINFSA IIFFIILTLA AFALVVASHA GNIAQERAAR IKRLLYISGL KKYVYWLSNL
1090 1100 1110 1120 1130 1140
IWDYVLTFIM VIFLAVVVVI IDSKFRNQFP LFICALVLFV TAIIPLSYLF SYCWSSHGKA
1150 1160 1170 1180 1190 1200
TGFIFGIHFG IGLLMTVTCF ILRIWVIKDD NDILQTITDI IDLVFFFFSP FYCFSKVMVI
1210 1220 1230 1240 1250 1260
ISNFPGTTRL GESYIANYWG IKFGLPPVCF LALHTLVWTI WIMVLDYYPE LRGKYRKGRN
1270 1280 1290 1300 1310 1320
EKSSPPPPSD EDSDVSHERS KVLSFETSND PIIMRDFFKL YKGKGKAKDN LAVYNTSLSI
1330 1340 1350 1360 1370 1380
PKGQTFGLLG LNGAGKSTTL GCLSGEVIPS GGEIFVNGFN IQTQRLDALR SVGFCHQYNS
1390 1400 1410 1420 1430 1440
LIGLLSAREQ IRLYCRIKGI EESKIQETVE AFIKMMDLGS IGNSNVAGYS GGNKRKVALS
1450 1460 1470 1480 1490 1500
VAIVGNPSVC FLDEVSAGVD PVVARFMWNV ITELKKDKVI ILTTHSMLEC SAVCDRLTIM
1510 1520 1530 1540 1550 1560
KSGKMMCLGS IQHIKDKFGS GYSIDVKFKK EYLLSGINLF QKELPNAKLV DHHDLSASFE
1570 1580 1590 1600 1610 1620
LPNSLDSPIQ LSKIFSIIER NLKPILNDYS VGQTSIDHIF LKLTNLNQQK IKNQQKESIE
1630 1640 1650 1660 1670 1680
NHIIDINNNN NNNNNNSYLK NHKKTTSNNS ILTNNSTTKN FGSSNFLDLE SDNTYLNNLK
1690 1700
YLEDDDFNIE MPPYQNSLKK SF