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 Q8FMF7

Entry ID Method Resolution Chain Position Source
AF-Q8FMF7-F1 Predicted AlphaFoldDB

No variants for Q8FMF7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8FMF7

No associated diseases with Q8FMF7

2 regional properties for Q8FMF7

Type Name Position InterPro Accession
conserved_site Polyamine biosynthesis domain, conserved site 300 - 313 IPR030373
domain Polyamine biosynthesis domain 225 - 459 IPR030374

Functions

Description
EC Number 2.5.1.16 Transferring alkyl or aryl groups, other than methyl groups
Subcellular Localization
  • Cell 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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

1 GO annotations of molecular function

Name Definition
spermidine synthase activity Catalysis of the reaction: S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + spermidine.

1 GO annotations of biological process

Name Definition
spermidine biosynthetic process The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSGLEQPAEL SRVWRWLLLV SVAICAASGL VYELALVSLS ASLNGGGIVE TSLIVAGYVA
70 80 90 100 110 120
ALGVGAILVK PFLRWPAQTF LAVETLLGLI GGLSALVLYM TFAVVGQNLW MLVLATALIG
130 140 150 160 170 180
ILVGAELPLL MTMIQRGRLA DARTTGSLVA TLNAADYLGA LLGGLAWPFI LLPWLGMMRG
190 200 210 220 230 240
AAAAGMINLL AALFVGCVLL RHLLPRAQFI RAVVALLVAI AVLGTVLVRS DGIVATARQQ
250 260 270 280 290 300
LYRDPVIYAH QSDYQDIVVT QRGADRRLYL NGGLQYSTRD EHRYTESLVY PGLSDSARTA
310 320 330 340 350 360
LIIGGGDGLA ARELLRFPDM RITQVELDPE VIEVANTILL PDNGGAMQDP RVTVITDDAF
370 380 390 400 410 420
TWLRAGGDGG QRYDAIFVDL PDPNNDTMAR LYSQEFYTLA LARLNDGGRM VVQSSSAYTT
430 440 450 460 470 480
PDVFWRIAST MSAAGCGAVI PYHVHVPTFG DWGFQLCGPE GTELGLRGDT PSLRFLTDEV
490 500 510
LAAAGVFGAD NQPRELEPST LDHPRVVEDL RRGYRQAGE