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 Q54TV2

Entry ID Method Resolution Chain Position Source
AF-Q54TV2-F1 Predicted AlphaFoldDB

No variants for Q54TV2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54TV2

No associated diseases with Q54TV2

11 regional properties for Q54TV2

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 129 - 376 IPR003439-1
domain ABC transporter-like, ATP-binding domain 888 - 1141 IPR003439-2
domain AAA+ ATPase domain 160 - 353 IPR003593-1
domain AAA+ ATPase domain 927 - 1118 IPR003593-2
domain ABC-2 type transporter, transmembrane domain 458 - 668 IPR013525-1
domain ABC-2 type transporter, transmembrane domain 1217 - 1429 IPR013525-2
domain Plant PDR ABC transporter associated 705 - 754 IPR013581
conserved_site ABC transporter-like, conserved site 275 - 289 IPR017871
domain ATP-binding cassette transporter, PDR-like subfamily G, domain 2 885 - 1124 IPR034003
domain ABC transporter family G domain 334 - 389 IPR043926-1
domain ABC transporter family G domain 1098 - 1157 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.

3 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.
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.
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
MVKQDPRDKS SYSPNLSIPI NNQEEPTLNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNK
70 80 90 100 110 120
NNNNNNIKHK DEENDFEDSI YQIAKEHEGE EDDEYFPIPL DELMPNHEND ELTKKIKQTR
130 140 150 160 170 180
PEDKTGLYVY CRNATYTVKH RENKKVKIKL LDDVSFFLRP KQMTLILGTP GCGKSTIFQM
190 200 210 220 230 240
LAGQLKDKHF EGELLFNGHP INHKNHHRDI SYVTQDDIHV PTLTVKETFR FALDCLGKKE
250 260 270 280 290 300
LTREEKQVSV DNCMKLLGLK HAENTLVGDN FIRGISGGQK KRVTIGVGVI KGSNLLLMDE
310 320 330 340 350 360
PTSGLDSSTS FEILSDVKKF VTYGYSPALI TLLQPSVQLT SLFDNLMIMS KGKICYFGPM
370 380 390 400 410 420
NRALGYFKKL GFACPSHNNP AEFFQEVVDA PERYSFIHPP KCKTSDDFVK AYRESDIYLE
430 440 450 460 470 480
LMEKMDANKD GIVDDNKPKV LVDSTAKELG MYPHGIGYQT KICLKRGFIM ISRNYYNFAT
490 500 510 520 530 540
RVFKGIFFGL LLGTLYWRIG HNQSGGMERF GLLFFIMTTI IFSSFAAVNS FFGERKVFYS
550 560 570 580 590 600
QKALHYYKTG AYFISSIICD IPAGLIEVAF FGPIVYWLAN LRPVFIRFVY FMILLFITDN
610 620 630 640 650 660
LSLSFAKMCA AISPTIEIAN VTASVILSIW LLFSGFTAPK NDIGGWWIWL YYISPYTWIF
670 680 690 700 710 720
QGLSINEFTY QAYGCKDSEL IPPRTPQNLL PYPEGFGGNQ VCQYTSGEQI MDAFGINNPD
730 740 750 760 770 780
YFKWIVYAIL GAYIVFFYSV CFFALKYLNF EDKKSKLAVK KLKKKKKVIV CKEDEEPNCK
790 800 810 820 830 840
VTTEALERVS DDNDDNADIS NYDDDTVIDM KSPLTSPNYN NNNNLSGSGN NIKRRKVKTP
850 860 870 880 890 900
STLSPMVNSP LTNLSPMVNT PSKNGNHSKQ KPISTSQKDI SSETGSYLQF KKLCYAVDVK
910 920 930 940 950 960
ADDPDNPKKK KSQRLQLLTD IDGYVKPGQM LALMGPSGAG KSTLLDVLAQ RKTGGHITGE
970 980 990 1000 1010 1020
ILINGKPPSE FTNRIRAYVE QMDVLPPTQT VREAIAFSAR CRLPPEVTKE EREIFVDKIV
1030 1040 1050 1060 1070 1080
EVLSLSSIKD LKIGVLGNGL SVSQRKRVNI GVELASNPEI LFLDEPTSGL DSGDAFKVID
1090 1100 1110 1120 1130 1140
VVNKIAKVMN RTVICTVHQP SAAIFEFFDQ LLLLKKGGET IYFGPLGNQS SVILDYCDKL
1150 1160 1170 1180 1190 1200
GMHIKPHINP ADFVMTLADE GKMVEGPNGE QEHLDAKKAY FESNICKKEY EIMEGQLIPD
1210 1220 1230 1240 1250 1260
DFVVKTYDSR FASSWMTQFR ALCMRSWLSR LRRPAIFVSN CLRSILLAVL LGTLFVRMDY
1270 1280 1290 1300 1310 1320
EQKDARSRVS LLFFSFLFAG MVAIGNIPTT VLERGVFYRE VTAGFYHSTA YMISYVLTSY
1330 1340 1350 1360 1370 1380
PFILSTGILY IIPTFWIAGL DSGRHSSKFW YCLFIFIITY IMYDAFALCL AVCLPNEVMA
1390 1400 1410 1420 1430 1440
STICGIGLSL ATLFGGFVIA RPNYPSAYYW CHYLDWLRYP LEASCTNEFT GLTFVCTNNK
1450 1460 1470 1480 1490 1500
GAVPIPIIEN GVQIAIKYYC PITNGDDFML TYGFHKFMRY IDIAAIFGYI FIFVGLSFWG
FKKVRWLNR