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 Q54TV1

Entry ID Method Resolution Chain Position Source
AF-Q54TV1-F1 Predicted AlphaFoldDB

No variants for Q54TV1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54TV1

No associated diseases with Q54TV1

11 regional properties for Q54TV1

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 138 - 385 IPR003439-1
domain ABC transporter-like, ATP-binding domain 924 - 1166 IPR003439-2
domain AAA+ ATPase domain 169 - 362 IPR003593-1
domain AAA+ ATPase domain 952 - 1143 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 467 - 677 IPR013525-1
domain ABC-2 type transporter, transmembrane domain 1242 - 1454 IPR013525-2
domain Plant PDR ABC transporter associated 714 - 762 IPR013581
conserved_site ABC transporter-like, conserved site 284 - 298 IPR017871
domain ATP-binding cassette transporter, PDR-like subfamily G, domain 2 910 - 1149 IPR034003
domain ABC transporter family G domain 343 - 398 IPR043926-1
domain ABC transporter family G domain 1123 - 1182 IPR043926-2

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

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.

2 GO annotations of biological process

Name Definition
aggregation involved in sorocarp development The process whose specific outcome is the progression of the aggregate over time, from its formation to the point when a slug is formed. Aggregate development begins in response to starvation and continues by the chemoattractant-mediated movement of cells toward each other. The aggregate is a multicellular structure that gives rise to the slug.
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
MAKQDPKDKN SDSPNLSIPI NNNNNENLDN DQELLNNNNN NNNNNNNNNN NNNNNNNNNN
70 80 90 100 110 120
NNNNLISSSR KHKDEESNYD SDDEKSVYQI AKEHEGEDDG DDEYFPIPLD ELMPNHENDE
130 140 150 160 170 180
LTKKIKQTRP EDKTGLYVYC RNATYTVKHR ENKKVKIKLI DDISFYLKPK EMTLILGTPG
190 200 210 220 230 240
CGKSTIFQML AGQLKDKHFK GELLFNGHPI NHKNHHRDIS YVTQDDIHVP TLTVKETFRF
250 260 270 280 290 300
ALDCLGRKEL TNEEKKETVD NCMNLLGLKE SENTVVGDNF VRGISGGQKK RVTIGVGVIK
310 320 330 340 350 360
GSNLLLMDEP TSGLDSSTSF EILSDVKKFV TYGYSPALIT LLQPSVQLTS LFDNLMILNK
370 380 390 400 410 420
GRICYFGPMN KALGYFKKLG FACPSHNNPA EFFQEVVDAP ERYSFIHPPK CKTSKDFVRA
430 440 450 460 470 480
YRESEFYKDL MEKMDANKDG IVDDNKPKVL VDSTAKELGM YPHGIGYQTK ICMKRGFTMI
490 500 510 520 530 540
RRNYYNFLTR VAKGIFFGLL LGTLYWRIGH NQSGGMERFG LLFFIMVTII FSSFAAVNSF
550 560 570 580 590 600
FGERKVFYSQ KALYYYKTGA YFISSIICDI PAGILEVAFF GPIVYWLANL RPVFIRFVYF
610 620 630 640 650 660
MLLLIMTDNL SLSFAKMCAA ISPTIEIANV IASVILSIWL LFSGFTAPKN DIGGWWIWLY
670 680 690 700 710 720
YISPYTWIFQ GLSINEFTYQ EYGCKTSELI PPRTPQNLLP YPEGFGGNQV CQFTSGEQIM
730 740 750 760 770 780
DAFGITNPNY FKWVVFGILS AYIVFFYVVC FFALKYFNFE DKKSKLAVKK LKKKKKVKTT
790 800 810 820 830 840
KQDEESAAIS SEALERIDDD NDDDADYETE IKKKKSHKKQ KEDTVIDVKS PSSLTTGSPY
850 860 870 880 890 900
YNINNNNNNL SGSGNNIKKR KVKTPSNLSP SVNSPITINS PMPTSPSNNN NNNNSNEKSK
910 920 930 940 950 960
NGKDIGSETG SYLQFKKLCY AVDVKVDDPD NPKKKKSQRL QLLTDIDGYV KPGQMLALMG
970 980 990 1000 1010 1020
PSGAGKSTLL DVLAQRKTGG HITGEILING KPPSEFTNRI RAYVEQMDVL PPTQTVREAI
1030 1040 1050 1060 1070 1080
AFSARCRLPP EVTKEERESY VDKIVEVLSL SSIKDLKIGV LGDGLSVSQR KRVNIGVELA
1090 1100 1110 1120 1130 1140
SNPEILFLDE PTSGLDSGDA FKVIDVVNKI AKVMNRTVIC TVHQPSAAIF EFFDQLLLLK
1150 1160 1170 1180 1190 1200
QGGETIYFGP LGNQSSVILD YCDKLGMHIK PHINPADFVM TLADQGKMVE GPNGEQVPLD
1210 1220 1230 1240 1250 1260
AKKAYFESDI CKKEYEIMEG QLIPDDFVIK TYDSRFASSW MTQFRALCMR SWLSRLRRPA
1270 1280 1290 1300 1310 1320
IFVSNCIRSI LLAVLLGTLF VRMDYEQKDA RSRVSLLFFS FLFAGMVAIG NIPTTVLERG
1330 1340 1350 1360 1370 1380
VFYREVTAGF YHSTAYMTSY VLTSYPFTLS TGILYIIPTF WIAGLDSGRH SSKFWYCLFI
1390 1400 1410 1420 1430 1440
FIITYVMYDA FGLCLAVCLP NEVMASTICG IGLSLSTLFG GFVIARPNYP SAYYWCHYLD
1450 1460 1470 1480 1490 1500
WLRYPLEASC TNEFTGLTFV CTNNKGAVPI PIIENGVQIA IKYYCPITNG DDFMLTYGFH
1510 1520 1530
KFMRYIDIAA IFGYIFIFVG LSFWGFKKIR WFNR