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 B5VGN1

Entry ID Method Resolution Chain Position Source
AF-B5VGN1-F1 Predicted AlphaFoldDB

No variants for B5VGN1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B5VGN1

No associated diseases with B5VGN1

5 regional properties for B5VGN1

Type Name Position InterPro Accession
domain Cation-transporting P-type ATPase, N-terminal 176 - 226 IPR004014
domain Cation-transporting P-type ATPase, C-terminal 966 - 1162 IPR006068
ptm P-type ATPase, phosphorylation site 498 - 504 IPR018303
domain P-type ATPase, haloacid dehalogenase domain 477 - 930 IPR044492
domain P5B-type ATPase, N-terminal 13 - 150 IPR047819

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.

1 GO annotations of molecular function

Name Definition
translation regulator activity Any molecular function involved in the initiation, activation, perpetuation, repression or termination of polypeptide synthesis at the ribosome.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLKCICRVYS QPLAQMVTSP LFKHMGSAGT YTILPITNLR HLSTKNCPLK IKSNRSEPLQ
70 80 90 100 110 120
FGDFERQVPC SRKSGSSKNV QKRLYELRQL KTVLSETFGV TEYASFFESL RNALHINNCS
130 140 150 160 170 180
ENEKKKLLYD IILHQHELYP EVARKIGFYL PGEVHRWFWY RIPKSESFNH YLFLLKSDVL
190 200 210 220 230 240
LFTSNYCTRF TNRLIKGTEM ERQLATFQIF LHDETNIKFI MEKVLKLHTF DSLIALVNGL
250 260 270 280 290 300
VKAKNFRFIK VFIQALLQKL EQHCYSGKDG AKQKNLRYVK FNNTLLYYLL KSGNVELFIK
310 320 330 340 350 360
TFQEELKFIV SSGLLNHIDG NEHILNFPIH HYLNLLRISN RQEELFNVIS CLQSSPLMKY
370 380 390 400 410 420
KLFKEFLMGE LIASFQAFRD PKLVCKYLLS SYSSKASANI LNALGIWGWL YHSKSTTLTA
430 440 450 460 470 480
PTLARELKNK NNILPNTMRI GSPVTVPILT ELYRSLLSSS SVSLESGQFK NCLLDLYYKY
490 500 510 520 530 540
KSFLSEEAHK YRYWRNDTGI LNVFLNYIRF QAREPRLAYN VLLDFYSQPF AKKVVLTTTL
550 560 570 580 590 600
CPFSIVAYKN HTLTQAELSE LLQVMHKNGV PLTFKFCSAM VMHYVKMRDE KGARSWYNKI
610 620 630 640 650 660
LFGGFEIRHM ALIQIIKDQG WPFPKNFDET LLTELVENNN IKEPTDSTLF TDEDMFEEDG
670 680
KPRFNDDDVN KCTNIIRETL KSLN