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 Q8T6H3

Entry ID Method Resolution Chain Position Source
AF-Q8T6H3-F1 Predicted AlphaFoldDB

No variants for Q8T6H3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8T6H3

No associated diseases with Q8T6H3

10 regional properties for Q8T6H3

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 474 - 700 IPR003439-1
domain ABC transporter-like, ATP-binding domain 1101 - 1336 IPR003439-2
domain AAA+ ATPase domain 502 - 677 IPR003593-1
domain AAA+ ATPase domain 1127 - 1321 IPR003593-2
domain ABC transporter type 1, transmembrane domain 115 - 389 IPR011527-1
domain ABC transporter type 1, transmembrane domain 777 - 1060 IPR011527-2
conserved_site ABC transporter-like, conserved site 601 - 615 IPR017871-1
conserved_site ABC transporter-like, conserved site 1239 - 1253 IPR017871-2
domain ABC transporter C family, six-transmembrane helical domain 2 777 - 1065 IPR044726
domain ABC transporter C family, six-transmembrane helical domain 1 114 - 405 IPR044746

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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

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.

2 GO annotations of biological process

Name Definition
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.
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
MFTKILKKFF SSYEKLKDNE DENEPSSNST NNFYKTCPED NSSKWSKISF NWVTKLIMKG
70 80 90 100 110 120
YLKESLEMND IYDLPELNKV QTTSKLLEDI DLSNNSNYTL IKHIYKKFLP KNKYALVSNL
130 140 150 160 170 180
FIIIFTFLSP ICLKFLINYI SIQDENEKSI LKGILLCCLL CLCVLGQSIS QELFYWFGIK
190 200 210 220 230 240
NGFDVRGALA AKIFEKTLKL SNASRKEYKS GKIMNIMSID VANISEYFWT HHINIVSHFI
250 260 270 280 290 300
QILSLVGLLC YVVGPSGLVG FGVMVIALPI NAMLCAKSSN YLEKSLEYSD SRTNLTSELI
310 320 330 340 350 360
TNIRPFKMYA WENFFINKID GQRKQELKNI FLRIFYSILD HMMIETNATL VLVSTFATYS
370 380 390 400 410 420
LNGNTMSLDV TFTAMTIFSK LEVPLIRLPY DIFKAIGLIP SVKRVQNFLK SSESLKYNKN
430 440 450 460 470 480
FKNENQKITT TKENNNQHGQ DNDIIVENCT FQWNEPENNN IFELNYGDNE EEENQDESIN
490 500 510 520 530 540
KKENDNEEFN YKLKDINLIV PKGKLTMICG VVGSGKTSLI FGLIGEIYKL NGSVSGVPNN
550 560 570 580 590 600
ISFTSQQPFL LSASLRENIL FGNEFDIERY KKVIESTALT KDIVNLAGLD LTEIGERGIN
610 620 630 640 650 660
LSGGQKQRIS LARALYANSD CFIFDEPLSA VDPEVASHLF DHCIQGELMR NKTRILVTHQ
670 680 690 700 710 720
LQFIPYADHI IVLNSNGQLI QGTYQELNEK GIDFKSILKT KEIKKNVENE TDSEELIKNE
730 740 750 760 770 780
IEIENEIIDV NNAISDKNDP NLIEKAKLLV KEDKNEGEVE FNVYKKYFSY GSSGVTLFIT
790 800 810 820 830 840
ISLFFVGQAI FKVSDFWLTI WTERSIEGKS DSFYIGYYLL IFGTFVVILM IRILLLCRIT
850 860 870 880 890 900
FNVGKNLHSA LLKSVTYASC RFFDTNPSGR ILNRFSKDTS DIDIHMFDIL TEVSMCFSEL
910 920 930 940 950 960
TIGLISIVFI IPIMVIPLII LSIAYYILQR LYRPSARELN RWESITVSPI FSLLQECYNG
970 980 990 1000 1010 1020
LLTIRTYKQE SRFIKEMFDN ININLGCFFY SFAVHRWVSM RLEVMGWIMV FFTSLIATLF
1030 1040 1050 1060 1070 1080
ISNNGLAALS VTTALSLNGY LSWGIRRIVD LEVKMNSFQR IQSYIEIPKE GNKLVSTNSN
1090 1100 1110 1120 1130 1140
EVDNHTIKDA DLVNWPNKGI IEFKNVEIKY RPNSEPNLKD LSFKVQSSEK IGIVGRTGAG
1150 1160 1170 1180 1190 1200
KTTIASSLFR MVECSKGLIL IDGIDISKVQ LQKLRSSIGI VPQDPFIFTG TIRSNIDPFN
1210 1220 1230 1240 1250 1260
EFTDFEIWES VEKVKLKDAI NSMPLKLETA LQENGDNGFS YGQKQLLCLC RTILKNFKII
1270 1280 1290 1300 1310 1320
LMDEATSSID YHTAQLIKQT IQENFKDCTT LTIAHRLETI IDCNKIAVID SGQLIEFDTP
1330 1340 1350
SNLMNIPNSK FNKLIKSQTD YNNNEKTIIN K