tegument host shutoff protein [Felid alphaherpesvirus 1]
Protein Classification
PIN domain-containing protein( domain architecture ID 1000090)
PIN (PilT N terminus) domain-containing protein may function as a nuclease
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PIN_SF super family | cl28905 | PIN (PilT N terminus) domain: Superfamily; The PIN (PilT N terminus) domain belongs to a large ... |
161-215 | 2.35e-04 | ||
PIN (PilT N terminus) domain: Superfamily; The PIN (PilT N terminus) domain belongs to a large nuclease superfamily, and were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein, PilT, a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. The PIN domain superfamily includes: the FEN-like PIN domain family such as the PIN domains of Flap endonuclease-1 (FEN1), exonuclease-1 (EXO1), Mkt1, Gap Endonuclease 1 (GEN1), and Xeroderma pigmentosum complementation group G (XPG) nuclease, 5'-3' exonucleases of DNA polymerase I and bacteriophage T4- and T5-5' nucleases; the VapC-like PIN domain family which includes toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC, as well as eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1; the LabA-like PIN domain family which includes the PIN domains of Synechococcus elongatus LabA (low-amplitude and bright); the PRORP-Zc3h12a-like PIN domain family which includes the PIN domains of RNase P (PRORP), ribonuclease Zc3h12a; and Bacillus subtilis YacP/Rae1-like PIN domains. It also includes the Mut7-C PIN domain family, which is not represented here as it is a shortened version of the PIN fold and lacks a core strand and helix (H3 and S3). The Mut7-C PIN domain family includes the C-terminus of Caenorhabditis elegans exonuclease Mut-7. The actual alignment was detected with superfamily member cd00128: Pssm-ID: 475124 [Multi-domain] Cd Length: 162 Bit Score: 41.59 E-value: 2.35e-04
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| PIN_FEN1_EXO1-like | cd00128 | FEN-like PIN domains of Flap endonuclease-1 (FEN1)-like and exonuclease-1 (EXO1)-like ... |
161-215 | 2.35e-04 | ||
FEN-like PIN domains of Flap endonuclease-1 (FEN1)-like and exonuclease-1 (EXO1)-like nucleases, structure-specific, divalent-metal-ion dependent, 5' nucleases; PIN (PilT N terminus) domain of Flap endonuclease-1 (FEN1) and exonuclease-1 (EXO1)-like nucleases: FEN1, EXO1, Mkt1, Gap endonuclease 1 (GEN1) and Xeroderma pigmentosum complementation group G (XPG) nuclease. These nucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350200 [Multi-domain] Cd Length: 162 Bit Score: 41.59 E-value: 2.35e-04
|
||||||
| XPGI | smart00484 | Xeroderma pigmentosum G I-region; domain in nucleases |
169-215 | 2.52e-04 | ||
Xeroderma pigmentosum G I-region; domain in nucleases Pssm-ID: 214689 [Multi-domain] Cd Length: 73 Bit Score: 39.49 E-value: 2.52e-04
|
||||||
| XPG_I | pfam00867 | XPG I-region; |
172-242 | 3.21e-04 | ||
XPG I-region; Pssm-ID: 459970 [Multi-domain] Cd Length: 87 Bit Score: 39.42 E-value: 3.21e-04
|
||||||
| rad2 | TIGR00600 | DNA excision repair protein (rad2); All proteins in this family for which functions are known ... |
143-210 | 1.57e-03 | ||
DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273166 [Multi-domain] Cd Length: 1034 Bit Score: 41.04 E-value: 1.57e-03
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| PIN_FEN1_EXO1-like | cd00128 | FEN-like PIN domains of Flap endonuclease-1 (FEN1)-like and exonuclease-1 (EXO1)-like ... |
161-215 | 2.35e-04 | ||
FEN-like PIN domains of Flap endonuclease-1 (FEN1)-like and exonuclease-1 (EXO1)-like nucleases, structure-specific, divalent-metal-ion dependent, 5' nucleases; PIN (PilT N terminus) domain of Flap endonuclease-1 (FEN1) and exonuclease-1 (EXO1)-like nucleases: FEN1, EXO1, Mkt1, Gap endonuclease 1 (GEN1) and Xeroderma pigmentosum complementation group G (XPG) nuclease. These nucleases are members of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350200 [Multi-domain] Cd Length: 162 Bit Score: 41.59 E-value: 2.35e-04
|
||||||
| XPGI | smart00484 | Xeroderma pigmentosum G I-region; domain in nucleases |
169-215 | 2.52e-04 | ||
Xeroderma pigmentosum G I-region; domain in nucleases Pssm-ID: 214689 [Multi-domain] Cd Length: 73 Bit Score: 39.49 E-value: 2.52e-04
|
||||||
| XPG_I | pfam00867 | XPG I-region; |
172-242 | 3.21e-04 | ||
XPG I-region; Pssm-ID: 459970 [Multi-domain] Cd Length: 87 Bit Score: 39.42 E-value: 3.21e-04
|
||||||
| rad2 | TIGR00600 | DNA excision repair protein (rad2); All proteins in this family for which functions are known ... |
143-210 | 1.57e-03 | ||
DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair] Pssm-ID: 273166 [Multi-domain] Cd Length: 1034 Bit Score: 41.04 E-value: 1.57e-03
|
||||||
| PIN_XPG_RAD2 | cd09868 | FEN-like PIN domains of Xeroderma pigmentosum complementation group G (XPG) nuclease, a ... |
160-211 | 4.00e-03 | ||
FEN-like PIN domains of Xeroderma pigmentosum complementation group G (XPG) nuclease, a structure-specific, divalent-metal-ion dependent, 5' nuclease and homologs; The Xeroderma pigmentosum complementation group G (XPG) nuclease plays a central role in nucleotide excision repair (NER) in cleaving DNA bubble structures or loops. XPG is a member of the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), and at the C-terminus of the PIN domain a H3TH (helix-3-turn-helix) domain, an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included in this model) and the helical arch/clamp region are involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Pssm-ID: 350216 [Multi-domain] Cd Length: 209 Bit Score: 38.65 E-value: 4.00e-03
|
||||||
| Blast search parameters | ||||
|
