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 B2TJ00

Entry ID Method Resolution Chain Position Source
AF-B2TJ00-F1 Predicted AlphaFoldDB

No variants for B2TJ00

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2TJ00

No associated diseases with B2TJ00

15 regional properties for B2TJ00

Type Name Position InterPro Accession
domain Immunodeficiency lentiviral matrix, N-terminal 2 - 127 IPR000071
domain Reverse transcriptase domain 628 - 818 IPR000477
domain Integrase, C-terminal, retroviral 1367 - 1414 IPR001037
domain Integrase, catalytic core 1198 - 1348 IPR001584
domain Zinc finger, CCHC-type 390 - 406 IPR001878-1
domain Zinc finger, CCHC-type 411 - 427 IPR001878-2
active_site Aspartic peptidase, active site 507 - 518 IPR001969
domain Peptidase A2A, retrovirus, catalytic 505 - 574 IPR001995
domain Ribonuclease H domain 1018 - 1141 IPR002156
domain Integrase, N-terminal zinc-binding domain 1147 - 1188 IPR003308
domain Reverse transcriptase connection 902 - 1003 IPR010659
domain Reverse transcriptase thumb 825 - 887 IPR010661
domain Retropepsins 491 - 582 IPR018061
domain Retropepsin-like catalytic domain 496 - 576 IPR034170
domain Retroviral nucleocapsid Gag protein p24, C-terminal domain 277 - 349 IPR045345

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.

1 GO annotations of biological process

Name Definition
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEFESVIGLE VHAELLTNTK IYCGCTTEFG GKPNTHVCPV CLGLPGSLPQ LNKRVLELGI
70 80 90 100 110 120
KAGLALNCKI TKVGRMDRKN YFYPDCPKNY QITQDELPIC RDGYIDIELE SGEVKRIGIE
130 140 150 160 170 180
RIHIEEDAGK LLHTKRGTLV DFNRAGVPLI EVVSKPDIRT PEEATLYLTK LRSILSSAQI
190 200 210 220 230 240
SDCKMEEGSL RCDGNISIRE RGTEPFGIRS EIKNMNSFKA LEKALNYEFD RQVEAVTNGE
250 260 270 280 290 300
ALSVETRRWD ETNNKTIVMR SKEQANDYRY FPEGDLVTLN VSDEWIEEIR KTIPELPYQK
310 320 330 340 350 360
ADRFVKEYGL PKYDAHVLTL TDAMADYFDE CAKLSGDPKA ASNWIMGDIS RLMKEESTWV
370 380 390 400 410 420
EDLKFSPKEL AELIEVIKDG TISSAIGKKV LEDMFAEGKS PKTIIDEKGL KQNNDEDAIR
430 440 450 460 470
QLVNKVLDEN PQVIEQYKSG RTRILGFAVG QVMKETKGQA NPGIVNKLVT EEVEKR