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Conserved domains on  [gi|395394049|ref|NP_001257448|]
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serine/threonine-protein kinase LATS1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MobB_NDR_LATS-like super family cl45907
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
 629-671 1.52e-23

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


The actual alignment was detected with superfamily member cd21778:

Pssm-ID: 459252  Cd Length: 76  Bit Score: 94.49  E-value: 1.52e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 395394049 629 SRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRV 671
Cdd:cd21778    1 SRVQSYSPQAFKFFMEQHVENVLKSHQQRLHRRKQLENEMAKV 43
UBA_LATS1 cd14397
UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large ...
 103-143 1.52e-23

UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large tumor suppressor homolog 1 or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. It plays a crucial role in the prevention of tumor formation by controlling mitosis progression. Human LATS1 is the mammalian homologs of Drosophila lats/warts gene that could suppress tumor growth and rescue all developmental defects in flies, including embryonic lethality. It forms a regulatory complex with zyxin, a regulator of actin filament assembly. The LATS1/zyxin complex plays a role in controlling mitosis progression on mitotic apparatus. LATS1 is phosphorylated in a cell-cycle-dependent manner and complexes with CDC2 in early mitosis. It can negatively modulates tumor cell growth by inducing G(2)/M cell cycle transition or apoptosis. It also functions as a mitotic exit network kinase interacting with MOB1A, a protein whose homolog in budding yeast associates with kinases involved in mitotic exit. Moreover, LATS1 acts as a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through inhibiting LIMK1. LATS1 can also inhibit transcription regulation and transformation functions of oncogene YAP by inhibiting its nuclear translocation through phosphorylation. In addition, LATS1 can regulate the transcriptional activity of forkhead L2 (FOXL2) via phosphorylation. It also acts as an acting-binding protein that can negatively regulate the actin polymerization. LATS1 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


:

Pssm-ID: 270580  Cd Length: 41  Bit Score: 93.56  E-value: 1.52e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSY 143
Cdd:cd14397    1 RQMLQDLQAAGFDEDMVIQALQQTNNRSIEAAIEFISKMSY 41
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
473-558 8.01e-04

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14950:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 585  Bit Score: 42.49  E-value: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049 473 ASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNY 552
Cdd:PRK14950 365 APQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKY 444


                 ....*.
gi 395394049 553 QGPPPP 558
Cdd:PRK14950 445 TPPAPP 450
 
Name Accession Description Interval E-value
MobB_LATS1 cd21778
Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; ...
 629-671 1.52e-23

Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; LATS1, also called WARTS protein kinase, is a serine/threonine-protein kinase that functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. LATS1 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS1 serine/threonine protein kinase and similar proteins.


Pssm-ID: 439273  Cd Length: 76  Bit Score: 94.49  E-value: 1.52e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 395394049 629 SRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRV 671
Cdd:cd21778    1 SRVQSYSPQAFKFFMEQHVENVLKSHQQRLHRRKQLENEMAKV 43
UBA_LATS1 cd14397
UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large ...
 103-143 1.52e-23

UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large tumor suppressor homolog 1 or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. It plays a crucial role in the prevention of tumor formation by controlling mitosis progression. Human LATS1 is the mammalian homologs of Drosophila lats/warts gene that could suppress tumor growth and rescue all developmental defects in flies, including embryonic lethality. It forms a regulatory complex with zyxin, a regulator of actin filament assembly. The LATS1/zyxin complex plays a role in controlling mitosis progression on mitotic apparatus. LATS1 is phosphorylated in a cell-cycle-dependent manner and complexes with CDC2 in early mitosis. It can negatively modulates tumor cell growth by inducing G(2)/M cell cycle transition or apoptosis. It also functions as a mitotic exit network kinase interacting with MOB1A, a protein whose homolog in budding yeast associates with kinases involved in mitotic exit. Moreover, LATS1 acts as a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through inhibiting LIMK1. LATS1 can also inhibit transcription regulation and transformation functions of oncogene YAP by inhibiting its nuclear translocation through phosphorylation. In addition, LATS1 can regulate the transcriptional activity of forkhead L2 (FOXL2) via phosphorylation. It also acts as an acting-binding protein that can negatively regulate the actin polymerization. LATS1 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270580  Cd Length: 41  Bit Score: 93.56  E-value: 1.52e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSY 143
Cdd:cd14397    1 RQMLQDLQAAGFDEDMVIQALQQTNNRSIEAAIEFISKMSY 41
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
 101-138 6.27e-08

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 48.98  E-value: 6.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 395394049  101 VNPQMLQDLQAAGFDEDMVIQALQKTNNrSIEAAIEFI 138
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGN-NVERAAEYL 37
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 473-558 8.01e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.49  E-value: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049 473 ASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNY 552
Cdd:PRK14950 365 APQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKY 444


                 ....*.
gi 395394049 553 QGPPPP 558
Cdd:PRK14950 445 TPPAPP 450
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 467-673 4.77e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049  467 NPLGNRASHSA--NSQPSATTVTAITPAPIQqpvksmrvlkPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMP 544
Cdd:PRK10263  308 DPLLNGAPITEpvAVAAAATTATQSWAAPVE----------PVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAP 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049  545 P-VAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVdsgdkekkqittSPITVRKNKKD 623
Cdd:PRK10263  378 EgYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYY------------APAPEQPVAGN 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 395394049  624 EERRESRIQSYSPQAFKFFMEQHVENVLkshQQRLHRKKQLENEMMRVKP 673
Cdd:PRK10263  446 AWQAEEQQSTFAPQSTYQTEQTYQQPAA---QEPLYQQPQPVEQQPVVEP 492
 
Name Accession Description Interval E-value
MobB_LATS1 cd21778
Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; ...
 629-671 1.52e-23

Mob-binding domain found in large tumor suppressor homolog 1 (LATS1) and similar proteins; LATS1, also called WARTS protein kinase, is a serine/threonine-protein kinase that functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. LATS1 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS1 serine/threonine protein kinase and similar proteins.


Pssm-ID: 439273  Cd Length: 76  Bit Score: 94.49  E-value: 1.52e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 395394049 629 SRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRV 671
Cdd:cd21778    1 SRVQSYSPQAFKFFMEQHVENVLKSHQQRLHRRKQLENEMAKV 43
UBA_LATS1 cd14397
UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large ...
 103-143 1.52e-23

UBA domain found in vertebrate serine/threonine-protein kinase LATS1; LATS1, also called large tumor suppressor homolog 1 or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. It plays a crucial role in the prevention of tumor formation by controlling mitosis progression. Human LATS1 is the mammalian homologs of Drosophila lats/warts gene that could suppress tumor growth and rescue all developmental defects in flies, including embryonic lethality. It forms a regulatory complex with zyxin, a regulator of actin filament assembly. The LATS1/zyxin complex plays a role in controlling mitosis progression on mitotic apparatus. LATS1 is phosphorylated in a cell-cycle-dependent manner and complexes with CDC2 in early mitosis. It can negatively modulates tumor cell growth by inducing G(2)/M cell cycle transition or apoptosis. It also functions as a mitotic exit network kinase interacting with MOB1A, a protein whose homolog in budding yeast associates with kinases involved in mitotic exit. Moreover, LATS1 acts as a novel cytoskeleton regulator that affects cytokinesis by regulating actin polymerization through inhibiting LIMK1. LATS1 can also inhibit transcription regulation and transformation functions of oncogene YAP by inhibiting its nuclear translocation through phosphorylation. In addition, LATS1 can regulate the transcriptional activity of forkhead L2 (FOXL2) via phosphorylation. It also acts as an acting-binding protein that can negatively regulate the actin polymerization. LATS1 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270580  Cd Length: 41  Bit Score: 93.56  E-value: 1.52e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSY 143
Cdd:cd14397    1 RQMLQDLQAAGFDEDMVIQALQQTNNRSIEAAIEFISKMSY 41
MobB_LATS2 cd21777
Mob-binding domain found in large tumor suppressor homolog 2 (LATS2); LATS2, also called ...
 622-670 1.12e-20

Mob-binding domain found in large tumor suppressor homolog 2 (LATS2); LATS2, also called kinase phosphorylated during mitosis protein, serine/threonine-protein kinase kpm, or Warts-like kinase, is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and for governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. LATS2 belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS2 serine/threonine protein kinase.


Pssm-ID: 439272  Cd Length: 83  Bit Score: 86.67  E-value: 1.12e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 395394049 622 KDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMR 670
Cdd:cd21777    1 RDEEKRESRIKSYSPFAFKFYMEQHVENVMKTYQQKLNRRLQLEQEMAK 49
UBA_LATS cd14322
UBA domain found in serine/threonine-protein kinase LATS and similar proteins; The LATS ...
 103-141 2.98e-15

UBA domain found in serine/threonine-protein kinase LATS and similar proteins; The LATS proteins family consists of two isoforms, LATS1 and LATS2, both of which are mammalian homologs of the Drosophila tumor suppressor gene lats/warts. LATS1, also called large tumor suppressor homolog 1, or WARTS protein kinase (warts), is a serine/threonine-protein kinase that highly conserved from fly to human. LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, inhibits the G1/S transition and is essential for embryonic development, proliferation control and genomic integrity. LATS proteins contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270507  Cd Length: 39  Bit Score: 69.81  E-value: 2.98e-15
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKM 141
Cdd:cd14322    1 NQMLQQLVAAGYSEEISMRALKKSGARTIEAAIEFIELM 39
MobB_LATS cd21774
Mob-binding domain found in the large tumor suppressor (LATS) subfamily; LATS was originally ...
 639-672 1.15e-13

Mob-binding domain found in the large tumor suppressor (LATS) subfamily; LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. This subfamily belongs to the NDR/LATS family of kinases that bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. LATS proteins contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of LATS subfamily serine/threonine protein kinases.


Pssm-ID: 439269  Cd Length: 62  Bit Score: 66.12  E-value: 1.15e-13
                         10        20        30
                 ....*....|....*....|....*....|....
gi 395394049 639 FKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVK 672
Cdd:cd21774    1 FKFYMEQHVENLLKSHKEREKRRRQLEKEMSKVG 34
UBA_LATS2 cd14398
UBA domain found in vertebrate serine/threonine-protein kinase LATS2; LATS2, also called ...
 104-143 5.32e-10

UBA domain found in vertebrate serine/threonine-protein kinase LATS2; LATS2, also called kinase phosphorylated during mitosis protein, or large tumor suppressor homolog 2, or serine/threonine-protein kinase KPM, or Warts-like kinase, is a novel mammalian homolog of the Drosophila tumor suppressor gene lats/warts. It inhibits the G1/S transition and is essential for embryonic development, proliferation control, and genomic integrity. LATS2 is a serine/threonine kinase that negatively regulates CyclinE/CDK2 and plays a role in tumor suppression. It also acts as the negative regulator of androgen receptor (AR) through inhibiting androgen-regulated gene expression and thus plays an important role in AR -regulated transcription and in the development of prostate cancer. Moreover, LATS2 induces apoptosis via down-regulation of anti-apoptotic proteins, BCL-2 and BCL-x(L), in human lung cancer cells. It is a centrosomal protein and forms a complex with Ajuba, a LIM protein, to regulate organization of the spindle apparatus through recruitment of gamma-tubulin to the centrosome during mitosis. Furthermore, LATS2 interacts with Mdm2 to inhibit p53 ubiquitination and promote p53 activation. It stabilizes the cellular protein level of Snail1, a central regulator of epithelial cell adhesion and movement in epithelial-to-mesenchymal transitions (EMTs) during embryo development, and enhances its EMT activity. LATS2 contains an N-terminal ubiquitin-associated (UBA) domain and a C-terminal protein kinase domain.


Pssm-ID: 270581  Cd Length: 41  Bit Score: 55.11  E-value: 5.32e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 395394049 104 QMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSY 143
Cdd:cd14398    2 QMLQELVNAGCDQEMAVRALKQTGSRSIEAALEYISKMSY 41
UBA pfam00627
UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes ...
 101-138 6.27e-08

UBA/TS-N domain; This small domain is composed of three alpha helices. This family includes the previously defined UBA and TS-N domains. The UBA-domain (ubiquitin associated domain) is a novel sequence motif found in several proteins having connections to ubiquitin and the ubiquitination pathway. The structure of the UBA domain consists of a compact three helix bundle. This domain is found at the N terminus of EF-TS hence the name TS-N. The structure of EF-TS is known and this domain is implicated in its interaction with EF-TU. The domain has been found in non EF-TS proteins such as alpha-NAC and MJ0280.


Pssm-ID: 395502 [Multi-domain]  Cd Length: 37  Bit Score: 48.98  E-value: 6.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 395394049  101 VNPQMLQDLQAAGFDEDMVIQALQKTNNrSIEAAIEFI 138
Cdd:pfam00627   1 EDEEAIQRLVEMGFDREQVREALRATGN-NVERAAEYL 37
MobB_NDR_LATS-like cd21742
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
 640-670 1.99e-05

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


Pssm-ID: 439267  Cd Length: 62  Bit Score: 42.57  E-value: 1.99e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 395394049 640 KFFMEQHVENVLKSHQQRLHRKKQLENEMMR 670
Cdd:cd21742    2 KQYIENHYTNLLQQLKERRERRKQLEEKLEN 32
UBA cd14270
UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ...
 106-136 1.45e-04

UBA domain found in proteins involved in ubiquitin-mediated proteolysis; The ubiquitin-associated (UBA) domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only the bind UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains.


Pssm-ID: 270456 [Multi-domain]  Cd Length: 30  Bit Score: 39.26  E-value: 1.45e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 395394049 106 LQDLQAAGFDEDMVIQALQKTNNrSIEAAIE 136
Cdd:cd14270    1 LAQLVEMGFSREQARRALRATNG-DVEAAVE 30
UBA2_KPC2 cd14304
UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar ...
 102-136 2.05e-04

UBA2 domain found in Kip1 ubiquitination-promoting complex protein 2 (KPC2) and similar proteins; KPC2, also called ubiquitin-associated domain-containing protein 1 (UBAC1), or glialblastoma cell differentiation-related protein 1, is one of two subunits of Kip1 ubiquitination-promoting complex (KPC), a novel E3 ubiquitin-protein ligase that also contains KPC1 subunit and regulates the ubiquitin-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor p27 at G1 phase. KPC2 contains a ubiquitin-like (UBL) domain and two ubiquitin-associated (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270489  Cd Length: 39  Bit Score: 39.16  E-value: 2.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 395394049 102 NPQMLQDLQAAGFDEDMVIQALQKTNNrSIEAAIE 136
Cdd:cd14304    2 NPRAVQSLMEMGFEEEDVLEALRVTRN-NQNAACE 35
UBA2_scUBP14_like cd14298
UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
 103-140 2.70e-04

UBA2 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270484 [Multi-domain]  Cd Length: 38  Bit Score: 38.59  E-value: 2.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNrSIEAAIEFISK 140
Cdd:cd14298    1 DEALAQLVSMGFDPEVARKALILTNG-NVERAIEWLFS 37
UBA_PUB_plant cd14290
UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family ...
 100-138 7.36e-04

UBA domain found in plant PNGase/UBA or UBX (PUB) domain-containing proteins; This family includes some uncharacterized hypothetical proteins found in plants. Although their biological function remain unclear, all family members contain an N-terminal ubiquitin-associated (UBA) domain and a C-terminal PUB domain. UBA domain, along with UBL (ubiquitin-like) domain, has been implicated in proteasomal degradation by associating with substrates destined for degradation as well as with subunits of the proteasome, thus regulating protein turnover. PUB domain functions as a p97 (also known as valosin-containing protein or VCP) adaptor by interacting with the D1 and/or D2 ATPase domains. The type II AAA+ ATPase p97 is involved in a variety of cellular processes such as the deglycosylation of ERAD substrates, membrane fusion, transcription factor activation and cell cycle regulation through differential binding to specific adaptor proteins.


Pssm-ID: 270476 [Multi-domain]  Cd Length: 49  Bit Score: 37.81  E-value: 7.36e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 395394049 100 EVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFI 138
Cdd:cd14290    1 EVNADLLKELEAMGFPRARAVRALHHTGNTSVEAAVNWI 39
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 473-558 8.01e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.49  E-value: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049 473 ASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNY 552
Cdd:PRK14950 365 APQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKY 444


                 ....*.
gi 395394049 553 QGPPPP 558
Cdd:PRK14950 445 TPPAPP 450
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 433-596 1.94e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049  433 WPQSSSAPAQSSPSSGHEIPTWQPNI---PVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPV--KSMRVLKPE 507
Cdd:PRK10263  333 WAAPVEPVTQTPPVASVDVPPAQPTVawqPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVqpQQPYYAPAA 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049  508 LQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPnYQgPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSL 587
Cdd:PRK10263  413 EQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQST-FA-PQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVV 490


                  ....*....
gi 395394049  588 PKEDESEKS 596
Cdd:PRK10263  491 EPEPVVEET 499
UBA2_UBP13 cd14387
UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called ...
 103-138 3.71e-03

UBA2 domain found in ubiquitin carboxyl-terminal hydrolase 13 (UBP13); UBP13, also called deubiquitinating enzyme 13, Isopeptidase T-3 (isoT3), ubiquitin thioesterase 13, or ubiquitin-specific-processing protease 13 is an ortholog of UBP5 implicated in catalyzing hydrolysis of various ubiquitin (Ub)-chains. It contains a zinc finger (ZnF) domain, a catalytic ubiquitin-specific processing protease (UBP) domain (catalytic C-box and H-box), and two ubiquitin-associated (UBA) domains. Due to the non-activating catalysis for K63-polyubiquitin chains, UBP13 may function differently from USP5 in cellular deubiquitination processes. Moreover, the zinc finger (ZnF) domain of USP13 cannot bind to Ub. Its tandem UBA domains can bind with different types of diUb but preferentially with K63-linked.USP13 can also regulate the protein level of CD3delta in cells via its UBA domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270570  Cd Length: 35  Bit Score: 35.43  E-value: 3.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNrSIEAAIEFI 138
Cdd:cd14387    1 EESIAILMSMGFPRNRAIEALKRTNN-NLDRALDWL 35
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 467-673 4.77e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049  467 NPLGNRASHSA--NSQPSATTVTAITPAPIQqpvksmrvlkPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMP 544
Cdd:PRK10263  308 DPLLNGAPITEpvAVAAAATTATQSWAAPVE----------PVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPVIAPAP 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395394049  545 P-VAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVdsgdkekkqittSPITVRKNKKD 623
Cdd:PRK10263  378 EgYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYY------------APAPEQPVAGN 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 395394049  624 EERRESRIQSYSPQAFKFFMEQHVENVLkshQQRLHRKKQLENEMMRVKP 673
Cdd:PRK10263  446 AWQAEEQQSTFAPQSTYQTEQTYQQPAA---QEPLYQQPQPVEQQPVVEP 492
UBA1_scUBP14_like cd14296
UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 ...
 103-138 7.03e-03

UBA1 domain found in Saccharomyces cerevisiae ubiquitin carboxyl-terminal hydrolase 14 (scUBP14) and similar proteins; scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, is the yeast ortholog of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA1 domain.


Pssm-ID: 270482 [Multi-domain]  Cd Length: 39  Bit Score: 34.91  E-value: 7.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFI 138
Cdd:cd14296    1 EEAVSQLMSMGFSENAAKRALYYTGNSSVEAAMNWL 36
UBA2_spUBP14_like cd14297
UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 ...
 103-138 9.22e-03

UBA2 domain found in Schizosaccharomyces pombe ubiquitin carboxyl-terminal hydrolase 14 (spUBP14) and similar proteins; spUBP14, also called deubiquitinating enzyme 14, UBA domain-containing protein 2, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14, functions as a deubiquitinating enzyme that is involved in protein degradation in fission yeast. Members in this family contain two tandem ubiquitin-association (UBA) domains. This model corresponds to the UBA2 domain.


Pssm-ID: 270483 [Multi-domain]  Cd Length: 39  Bit Score: 34.38  E-value: 9.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 395394049 103 PQMLQDLQAAGFDEDMVIQALQKTNNrSIEAAIEFI 138
Cdd:cd14297    1 EDLVKQLVDMGFTEAQARKALRKTNN-NVERAVDWL 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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