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 Q8T6J5

Entry ID Method Resolution Chain Position Source
AF-Q8T6J5-F1 Predicted AlphaFoldDB

No variants for Q8T6J5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8T6J5

No associated diseases with Q8T6J5

7 regional properties for Q8T6J5

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 484 - 717 IPR003439-1
domain ABC transporter-like, ATP-binding domain 1293 - 1528 IPR003439-2
domain AAA+ ATPase domain 512 - 701 IPR003593-1
domain AAA+ ATPase domain 1323 - 1505 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 23 - 424 IPR013525-1
domain ABC-2 type transporter, transmembrane domain 854 - 1241 IPR013525-2
conserved_site ABC transporter-like, conserved site 619 - 633 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
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
MGEFKSQLRT LLKKNLLLKG KSKCAICCEI LFPIIVILVI FAILVLVMAF KANYDPYNAS
70 80 90 100 110 120
NFVNRFENTV LLYGNADGAL NVEQLGVMNI LKNEVATAKN LNSTQIDQLF IEINDQTAME
130 140 150 160 170 180
AFFQNKSDFV FSAVWFNNSA LSSGTNPFQY NIRVDSDDVM DTEELIKEDD TSDSEVYVKK
190 200 210 220 230 240
RFVATQVAMD QAIFSYFGLN KTLNVKGQRY PDPWTELWQK WIQGRDGIFK DAGSVFITAA
250 260 270 280 290 300
LMIFGFRLIT DLVIEKETKI RESMKMMGLN DLAYFISWMI TSLVTALPVN LIISIILKGS
310 320 330 340 350 360
SVIHHTNWGV VIFTLILYLL TLLLLAFILS MFFDKSKFCG LLSFVIIIAI NIGGIFVAKY
370 380 390 400 410 420
DFAPGAKLFL CLISPIAIAC SIFAMSARDL EEINTYNWDM MVTENQVIGM LVLDIFFYIF
430 440 450 460 470 480
LVWYLDNVVT TEFGTKQKWY FLFTKKYWFP KKCNENGDEQ DIESTYQNED VEMTPVGVGQ
490 500 510 520 530 540
KVTISIRNLR KEYNTGDGLR VAVNDLYLDM YENQIHALLG PNGSGKSTTI GMMTGLTPPT
550 560 570 580 590 600
NGNAFVHGYG ILNQMSSVRK HLGVCPQTDI IWQQLTVLDH LKIYASLKGV SPSEIQREAE
610 620 630 640 650 660
KMAVEVDLGE KIHSQAGSLS GGQKRKLCLG IAFIGRSDVI FLDEVSSGMD PLSRRVVWDF
670 680 690 700 710 720
LLKYKKGRTI ILTTHYLEEA DYLGDRIAII SHGKLRCDGS SLYLKNKFGC GYLLTCSKIL
730 740 750 760 770 780
SSMNNFNAQQ VTEFIHNYIP EATILSNAGT ELSYRLPTAS LPHFAQFFRE FDDRLQSFGL
790 800 810 820 830 840
LTYGISVTTL EEVFLSLGRE AALEKGGFNI DQNENQDLEQ LRKSIAISST GVKAGQQFKG
850 860 870 880 890 900
LLIKRIKTSI KDAKSFFLTL VIPLVFIIGS IIMYKAMDKP QIFYNNATVP LTMNLGIYSG
910 920 930 940 950 960
LENNFVPMQS SNELNWENSL NSSPYFNKFR FIPQTENFED YLIEGKTNGS FAYKSSAGAI
970 980 990 1000 1010 1020
NFTLPIDVSS TTIDYTAFYN KDYIHSLPVH INLVNDAVLR KHNNIGIQVT NMPFKHVLSN
1030 1040 1050 1060 1070 1080
FDLASEGMNI SSIVYFIIIM MAGYALMAGS FAGNVAQERT NRVKRLLYIS GCKKYVYWLS
1090 1100 1110 1120 1130 1140
NLVWDYFFSF ILILLTTCIL AGIRENYKSQ FGLMFLCLIL FCVSVVPLSY LLSYRFASFG
1150 1160 1170 1180 1190 1200
KATGAITAIH FAIGIIFVII SLNLRIQVLI DQDVDFQKAA DAVDIVFCIL SPLFAYSRIL
1210 1220 1230 1240 1250 1260
FLVSEFPGSV RVGTLKVDNY WSMDYGGSPM IILAAHCIVW VSWIMILDYT PELIGKIRNP
1270 1280 1290 1300 1310 1320
KNIEAPPPPD DEDSDVTAER TRLLSVGPND EPLQFRNLHK LFPAVGKAAP KAAVYNSTLS
1330 1340 1350 1360 1370 1380
IPKGQTFGLL GLNGAGKTTT IAMLCGDIVP SSGEVTINGH DLITDRGQAL RSNGLCPQFD
1390 1400 1410 1420 1430 1440
ALITLLSARE QLTLYCAIKG VPEDKVKEVV EAFIKMMDLG AIANSNTGGY SGGNKRKTSL
1450 1460 1470 1480 1490 1500
SIAMLGNPSI VSLDEPSTGC DAVVRKYIWN VVSELAKDKV IILTSHSMAE VEALCYRMTI
1510 1520 1530 1540 1550 1560
MRDGKMKCLG SIQHIKSKFG AGYTFDVKFK KEYLDSGIQT VLKAIPNSIV LDEHDVMASF
1570 1580 1590 1600 1610 1620
EIPNPPDNPV KISTLFESLS HLTILDDYNV SQTSLESVFL KLTGASYEDR LNLNNQKHTS
D