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 Q54BU4

Entry ID Method Resolution Chain Position Source
AF-Q54BU4-F1 Predicted AlphaFoldDB

No variants for Q54BU4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54BU4

No associated diseases with Q54BU4

4 regional properties for Q54BU4

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 666 - 902 IPR003439
domain AAA+ ATPase domain 693 - 879 IPR003593
domain ABC transporter type 1, transmembrane domain 351 - 633 IPR011527
conserved_site ABC transporter-like, conserved site 805 - 819 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

1 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.

3 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.

4 GO annotations of biological process

Name Definition
chemotaxis The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
culmination involved in sorocarp development The process whose specific outcome is the progression of the culminant over time, from its formation to the mature structure. Culmination begins with a morphogenetic change of the finger-like or migratory slug giving rise to an organized structure containing a stalk and a sorus. This process is the final stage of sorocarp development.
hyperosmotic response Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKKNFNDEE NESLLETYNK QQQKQSISTT NRSDQKFGIN NANKQFSLNN KKSINGEEID
70 80 90 100 110 120
EEELIEDTIF FKFKLDSKQR NSIKLFIQIV SLVILAGYLI SINALYFSTN ARSIIFYPSI
130 140 150 160 170 180
NSNTTDSGSV SPTSTPSPTP TPTPSPTSLL LQTLTSTTTS YDSSEIEALN GGTFNMKYFF
190 200 210 220 230 240
YFSTFDILLI SYFISLFWLL LIFSDSFIYH TISYIITIIA LIYNVIKSYF TITQILSINN
250 260 270 280 290 300
NIITTSSSSN EIYNGSDSYL PNESPLFDSL KVREIIIVIV LVGIPLMVLF LVLHIITLQL
310 320 330 340 350 360
SFKKYKRLSD KEKQFYNQSN EEKRLNKKVE VKHSNLKRLI QLSRPELPII LAAMVALVFS
370 380 390 400 410 420
SLTSLAMPYF FGSIVQVVAT THSFNNLNSS TLALVVIFVI GSISTLVRSW LFYLAGQKFV
430 440 450 460 470 480
ARIRRNLFSS IVNQEIGYFD QCRTGELLSR LSSDSQVIQN SVTVNISMLF RYTIQIIGSV
490 500 510 520 530 540
ILLFITNWRL TLLMLGIVPV LAISTVVYGK KIKQLGKQFQ DELAKSSTTG EEVISNIRTV
550 560 570 580 590 600
RSFSKEQKFI DLYSKDINGS YLIGKSLAVA TGVFSGIVFL VAQLAIVLIV YVGARQVLDG
610 620 630 640 650 660
TLSTGDLTSF LLYTLSLAMS LAFISSLMTD FLKAIGSSDR IFEIFDRVPA INVSGGKQIQ
670 680 690 700 710 720
NPLGEIELKD VEFSYPTRPN NSVLKGLNLK LSKGTITALV GPSGGGKSTV IAMIERFYDP
730 740 750 760 770 780
NSGSITFDGI DIKELDPVWY RGIIGYVSQE PVLFAGSIKD NITFGNDSAT MDQIISAAEK
790 800 810 820 830 840
ANAHSFIEEF ENGYDTIVGE RGVRLSGGQK QRVAIARAMI QNPMILLLDE ATSALDAESE
850 860 870 880 890 900
YLVKQAIDEI MKDRTVIVIA HRLSTVINAN TVVVINQGKI EEMGTHKELL NNTDGIYHNL
VKRQLSSDD