NCBI Conserved Domain Search

Conserved domains on [gi|755531599|ref|XP_011241233|]

View

tyrosine-protein phosphatase non-receptor type 23 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

Zoom to residue level

show extra options »

Show site features Horizontal zoom: ×

List of domain hits

Name

Accession

Description

Interval

E-value

V_HD-PTP_like

cd09234

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...

169-509

0e+00

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.

Pssm-ID: 185747 [Multi-domain] Cd Length: 337 Bit Score: 543.42 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLDPETVDNLDAYNHIPPQLMEKCAALSVRPDTVKNLVQS 248
Cdd:cd09234     1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPLNVMDMDGQFELPQDLVERCAALSVRPDTIKNLVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  249 MQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPgpsvakAELAEVRREWAKYMEVHEKASFTNSELHRAM 328
Cdd:cd09234    81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVGKRGSSI------AHVTELKRELKKYKEAHEKASQSNTELHKAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  329 NLHVGNLRLLSGPLDQVRAALPTPALT--PEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSE 406
Cdd:cd09234   155 NLHIANLKLLAGPLDELQKKLPSPSLLdrPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAIHEDDITSKLVTTTGGD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  407 MKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKD 486
Cdd:cd09234   235 MEDLFKEELKKHDQLVNLIEQNLAAQENILKALTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKGID 314

                         330       340
                  ....*....|....*....|...
gi 755531599  487 FYADLESKVATLLERAQSICRAQ 509
Cdd:cd09234   315 FYKKLEGNVSKLLQRIKSVCKVQ 337

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1106-1310

2.66e-129

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.

Pssm-ID: 350387 [Multi-domain] Cd Length: 205 Bit Score: 399.07 E-value: 2.66e-129

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVALSS 1185
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQRPLHTPIVVHCSSGVGRTGAF 1265
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755531599 1266 ALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14539   161 CLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

BRO1_Alix_like super family

cl14649

Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...

1-164

5.21e-93

Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and Rhophilin-2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Brox, Bro1 and Rim20 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, HD-PTP, and Brox) and Snf7 (in the case of yeast Bro1, and Rim20). The single domain protein human Brox, and the isolated Bro1-like domains of Alix, HD-PTP and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix, HD-PTP, Bro1, and Rim20 also have a V-shaped (V) domain, which in the case of Alix, has been shown to be a dimerization domain and to contain a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in this superfamily. Alix, HD-PTP and Bro1 also have a proline-rich region (PRR); the Alix PRR binds multiple partners. Rhophilin-1, and -2, in addition to this Bro1-like domain, have an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This protein has a C-terminal, catalytically inactive tyrosine phosphatase domain.

The actual alignment was detected with superfamily member cd09239:

Pssm-ID: 472700 Cd Length: 361 Bit Score: 305.51 E-value: 5.21e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    1 MLDNRKSFLVARISAQVVDYYKEACRALENPDTAS--LLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVA 78
Cdd:cd09239   194 LLDNRKSHITAKVSAQVVEYYKEALRALENWESNSkiILGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVA 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   79 YFQSALDKLNEAIKLAKGQPDT--VQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDP 156
Cdd:cd09239   274 YYQLANDKLEEAIKNAKGQPDTvnLQEALSFTMDVIGGKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPFSPTDP 353


                  ....*...
gi 755531599  157 AVTGPDIF 164
Cdd:cd09239   354 EVCGPDIF 361

PHA03247 super family

cl33720

large tegument protein UL36; Provisional

540-946

1.22e-10

large tegument protein UL36; Provisional

The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.89 E-value: 1.22e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  540 REEGEAVEAGDTPEELR--SLPPDMMVGPRLPDPflgttAPLHFSPGPFPSSTGPAThylsgPLPPGTYSGptqlmqpRA 617
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrrAARPTVGSLTSLADP-----PPPPPTPEPAPHALVSAT-----PLPPGPAAA-------RQ 2730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  618 AVPMAPATVLYPAPAYTSELGLVPRSSPQHGIVSSPYAGVGPPQPvvglPSAPPPQLSGPELAmTVRPATTTVDSVQAPi 697
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP----AAGPPRRLTRPAVA-SLSESRESLPSPWDP- 2804

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  698 SSHTAPRPNPTPALPQPCFPV-PQPVPQSVPQPQPLpvpytysigtKQPLPAPYTYSIGTKQHLTGPL---PQHQFPPGI 773
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAgPLPPPTSAQPTAPP----------PPPGPPPPSLPLGGSVAPGGDVrrrPPSRSPAAK 2874

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  774 PTGFPVPRTGPQAQAQPQPQPQPQPQPQPQPQPQPQpqsqsqpqpqpqpqpqrpafgPQPTQQPLPFQHPHLFPSQAPGI 853
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ---------------------PQAPPPPQPQPQPPPPPQPQPPP 2933

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  854 lppppptpyhfTPQPGVLGQPPPTLHTQLYPGPSQDPLPPHSGAlpfpspgpphphptLAYGPAPSPRPLGPQATPVSir 933
Cdd:PHA03247 2934 -----------PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA--------------LVPGRVAVPRFRVPQPAPSR-- 2986

                         410
                  ....*....|...
gi 755531599  934 gPPPASqPTPSPH 946
Cdd:PHA03247 2987 -EAPAS-STPPLT 2997

Name

Accession

Description

Interval

E-value

V_HD-PTP_like

cd09234

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...

169-509

0e+00

Pssm-ID: 185747 [Multi-domain] Cd Length: 337 Bit Score: 543.42 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLDPETVDNLDAYNHIPPQLMEKCAALSVRPDTVKNLVQS 248
Cdd:cd09234     1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPLNVMDMDGQFELPQDLVERCAALSVRPDTIKNLVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  249 MQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPgpsvakAELAEVRREWAKYMEVHEKASFTNSELHRAM 328
Cdd:cd09234    81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVGKRGSSI------AHVTELKRELKKYKEAHEKASQSNTELHKAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  329 NLHVGNLRLLSGPLDQVRAALPTPALT--PEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSE 406
Cdd:cd09234   155 NLHIANLKLLAGPLDELQKKLPSPSLLdrPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAIHEDDITSKLVTTTGGD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  407 MKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKD 486
Cdd:cd09234   235 MEDLFKEELKKHDQLVNLIEQNLAAQENILKALTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKGID 314

                         330       340
                  ....*....|....*....|...
gi 755531599  487 FYADLESKVATLLERAQSICRAQ 509
Cdd:cd09234   315 FYKKLEGNVSKLLQRIKSVCKVQ 337

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1106-1310

2.66e-129

Pssm-ID: 350387 [Multi-domain] Cd Length: 205 Bit Score: 399.07 E-value: 2.66e-129

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVALSS 1185
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQRPLHTPIVVHCSSGVGRTGAF 1265
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755531599 1266 ALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14539   161 CLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

BRO1_HD-PTP_like

cd09239

Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...

1-164

5.21e-93

Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP) and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. HD-PTP participates in cell migration and endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.

Pssm-ID: 185762 Cd Length: 361 Bit Score: 305.51 E-value: 5.21e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    1 MLDNRKSFLVARISAQVVDYYKEACRALENPDTAS--LLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVA 78
Cdd:cd09239   194 LLDNRKSHITAKVSAQVVEYYKEALRALENWESNSkiILGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVA 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   79 YFQSALDKLNEAIKLAKGQPDT--VQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDP 156
Cdd:cd09239   274 YYQLANDKLEEAIKNAKGQPDTvnLQEALSFTMDVIGGKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPFSPTDP 353


                  ....*...
gi 755531599  157 AVTGPDIF 164
Cdd:cd09239   354 EVCGPDIF 361

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1083-1313

8.31e-86

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 279.90 E-value: 8.31e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  1083 KNRHQDVMPYDSNRVVL--RSGKDDYINASCVEGlSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQ 1160
Cdd:pfam00102    4 KNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDG-YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGRE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  1161 KVARYFPTERGQPMVHGALSVALSSIRTTETH-VERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:pfam00102   83 KCAQYWPEEEGESLEYGDFTVTLKKEKEDEKDyTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRK 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599  1240 HYlhQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:pfam00102  163 SS--LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEA-EGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1083-1314

2.35e-82

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 271.07 E-value: 2.35e-82

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   1083 KNRHQDVMPYDSNRVVLRSGK---DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:smart00194   30 KNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGP-KAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGR 108

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   1160 QKVARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:smart00194  109 EKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRK 188

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531599   1240 HYLHQRplhTPIVVHCSSGVGRTGAFALLYAAVQEVEAGnGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:smart00194  189 SQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

ALIX_LYPXL_bnd

pfam13949

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...

224-510

7.52e-70

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.

Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 236.75 E-value: 7.52e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   224 IPPQLMEKCAALSVRpDTVKNLVQSMQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPGPSVAKAELaev 303
Cdd:pfam13949    2 LPPSLREKAEEVRQQ-GGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATL--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   304 RREWAKYMEVHEKASFTNSELHRAMNLHVGNLRLLSGPLDQVRAALPT---PALTPEDKAVLQNLKRILAKVQEMRDQRV 380
Cdd:pfam13949   78 RAEIRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSsrrAKNSPSVEEQVAKLRELLNKLNELKRERE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   381 SLEQQLRELIQKDDITASLVTT-----DHSEMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSE 455
Cdd:pfam13949  158 QLLKDLKEKARNDDISPKLLLEkarliAPNQEEQLFEEELEKYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSE 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755531599   456 LDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYADLESKVATLLERAQSICRAQE 510
Cdd:pfam13949  238 KQRQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARR 292

BRO1

pfam03097

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...

1-187

4.39e-68

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It is known to have a role in endosomal targeting. ESCRT-III subunit Snf7 binds to a conserved hydrophobic patch in the BRO1 domain that is required for protein complex formation and for the protein-sorting function of BRO1.

Pssm-ID: 460803 Cd Length: 366 Bit Score: 234.40 E-value: 4.39e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599     1 MLDNRKSFLVARISAQVVDYYKEACRALENPDTasllgrIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYF 80
Cdd:pfam03097  188 INDNKKDSLIAKLAAQVSELYEEALEALKLSGL------IDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARL 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    81 QSALDKLNEAIKLAKGQpdTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDPAVTG 160
Cdd:pfam03097  262 QLALSLLKEALKSDRYK--KVLEDLKGLLDVVEEKLKRAEKDNDFIYHERVPSESSLPPIKPASMVKPIPPLELYPFQIG 339

                          170       180
                   ....*....|....*....|....*..
gi 755531599   161 PDIFAKLVPMAAHEASSLYSEEKAKLL 187
Cdd:pfam03097  340 PDLFKKLVPLSVHEAASAYSERKAKLV 366

BRO1

smart01041

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...

1-189

8.58e-67

Pssm-ID: 214990 Cd Length: 381 Bit Score: 231.09 E-value: 8.58e-67

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599      1 MLDNRK--SFLVARISAQVVDYYKEACRALENPDTASllGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVA 78
Cdd:smart01041  190 ILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVK--GYIPKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIA 267

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599     79 YFQSALDKLNEAIKLA----KGQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPT 154
Cdd:smart01041  268 RLQEALERLKEAKKHLrckkLGKADKLQEDLSGLKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSEV 347

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 755531599    155 DpavTGPDIFAKLVPMAAHEASSLYSEEKAKLLRE 189
Cdd:smart01041  348 L---KGPDLFAKLVPMAVHEAASLYSEEKAKLVRA 379

PHA02738

hypothetical protein; Provisional

1084-1317

3.22e-36

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 140.45 E-value: 3.22e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLRSGKD--DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQK 1161
Cdd:PHA02738   53 NRYLDAVCFDHSRVILPAERNrgDYINANYVDGFE-YKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1162 VARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQfRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEV---- 1237
Cdd:PHA02738  132 CFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVrqcq 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1238 ---HAHYL---HQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEA 1311
Cdd:PHA02738  211 kelAQESLqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATV-SIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                  ....*.
gi 755531599 1312 LVRHVE 1317
Cdd:PHA02738  290 VKRYVN 295

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1080-1302

6.31e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 132.52 E-value: 6.31e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1080 YSLKNRHQDVMPYDSNRVvlrSGKDDYINASCVEGLSPYCppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:COG5599    42 GSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKV--ARYFPTErGQpmvHGALSVALSSIRTT--ETHVE-RVLSLQFRDQSLK-RSLVHLHFPTWPELGLPDSPgNLLRF 1233
Cdd:COG5599   117 PKVkmPVYFRQD-GE---YGKYEVSSELTESIqlRDGIEaRTYVLTIKGTGQKkIEIPVLHVKNWPDHGAISAE-ALKNL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599 1234 IQEVHAHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPE-LPQLVRRMRQQR-KHMLQEK 1302
Cdd:COG5599   192 ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsVEEIVIDMRTSRnGGMVQTS 262

PHA03247

large tegument protein UL36; Provisional

540-946

1.22e-10

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.89 E-value: 1.22e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  540 REEGEAVEAGDTPEELR--SLPPDMMVGPRLPDPflgttAPLHFSPGPFPSSTGPAThylsgPLPPGTYSGptqlmqpRA 617
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrrAARPTVGSLTSLADP-----PPPPPTPEPAPHALVSAT-----PLPPGPAAA-------RQ 2730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  618 AVPMAPATVLYPAPAYTSELGLVPRSSPQHGIVSSPYAGVGPPQPvvglPSAPPPQLSGPELAmTVRPATTTVDSVQAPi 697
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP----AAGPPRRLTRPAVA-SLSESRESLPSPWDP- 2804

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  698 SSHTAPRPNPTPALPQPCFPV-PQPVPQSVPQPQPLpvpytysigtKQPLPAPYTYSIGTKQHLTGPL---PQHQFPPGI 773
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAgPLPPPTSAQPTAPP----------PPPGPPPPSLPLGGSVAPGGDVrrrPPSRSPAAK 2874

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  774 PTGFPVPRTGPQAQAQPQPQPQPQPQPQPQPQPQPQpqsqsqpqpqpqpqpqrpafgPQPTQQPLPFQHPHLFPSQAPGI 853
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ---------------------PQAPPPPQPQPQPPPPPQPQPPP 2933

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  854 lppppptpyhfTPQPGVLGQPPPTLHTQLYPGPSQDPLPPHSGAlpfpspgpphphptLAYGPAPSPRPLGPQATPVSir 933
Cdd:PHA03247 2934 -----------PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA--------------LVPGRVAVPRFRVPQPAPSR-- 2986

                         410
                  ....*....|...
gi 755531599  934 gPPPASqPTPSPH 946
Cdd:PHA03247 2987 -EAPAS-STPPLT 2997

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

347-665

1.45e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.45e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  347 AALPTPAL-TPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSEMKKLfEEQL--------KK 417
Cdd:COG3883     6 LAAPTPAFaDPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-QAEIaeaeaeieER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  418 YDQLK-------------VYLEQNLAAQD--------NVLRALTEANV----QYAAVRRVLSELDQKWNSTLQTLVASYE 472
Cdd:COG3883    85 REELGeraralyrsggsvSYLDVLLGSESfsdfldrlSALSKIADADAdlleELKADKAELEAKKAELEAKLAELEALKA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  473 AYE----DLMKKSQEGKDFYADLESKVATLLERAQSICRAQEAARQQLLDRELKKKAPPPRPTAPKPLLSRREEGEAVEA 548
Cdd:COG3883   165 ELEaakaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  549 GDTPEELRSLPPDMMVGPRLPDPFLGTTAPLHFSPGPFPSSTGPATHYLSGPLPPGTYSGPTQLMQPRAAVPMAPATVLY 628
Cdd:COG3883   245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVG 324

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 755531599  629 PAPAYTSELGLVPRSSPQHGIVSSPYAGVGPPQPVVG 665
Cdd:COG3883   325 GASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSG 361

PRK03918

DNA double-strand break repair ATPase Rad50;

252-523

3.04e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.04e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  252 LSGVFTDVEASLKDIRDLLEEDELQEQKLQEtlgqagagpgpsvAKAELAEVRREWAKYMEvhekasftnselhramnlh 331
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENIEELIKE-------------KEKELEEVLREINEISS------------------- 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  332 vgNLRLLSGPLDQVRAALPT--------PALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDditaslvttd 403
Cdd:PRK03918  215 --ELPELREELEKLEKEVKEleelkeeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV---------- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  404 hSEMKKLfEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKwnstlqtlvasYEAYEDLMKKSQE 483
Cdd:PRK03918  283 -KELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKE 349

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 755531599  484 GKDFYADLESKVaTLLERAQSICRAQEAARQQLLDRELKK 523
Cdd:PRK03918  350 LEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEK 388

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

551-763

6.05e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.60 E-value: 6.05e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   551 TPEELRSLPPDMMVGPRLPDPFLGTTAPLHFSPGPFPSSTGPaTHYLSGPLPPGTYsgptqlmqPRAAVPMAPATVLYPA 630
Cdd:pfam05109  517 TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSP-TPAVTTPTPNATI--------PTLGKTSPTSAVTTPT 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   631 PAYTSElgLVPRSSPQH--------GIVSSPYAGVGPPQPVVGLPSAPPPQLSGPELAMTVRPATTTVDSVQAPISSHTA 702
Cdd:pfam05109  588 PNATSP--TVGETSPQAnttnhtlgGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTS 665

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599   703 PRPNPTPALPQPCFPVPQPVPQSVPqpqplpvpyTYSIGTKQPLPAPytysiGTKQHLTGP 763
Cdd:pfam05109  666 HMPLLTSAHPTGGENITQVTPASTS---------THHVSTSSPAPRP-----GTTSQASGP 712

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

227-523

5.49e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 5.49e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   227 QLMEKCAalsvrPDTVKNLVQSMQVLSGVFTDVEASLKDIRD----LLEEDELQEQ--KLQETLGQAGA------GPGPS 294
Cdd:TIGR00618  204 QLLTLCT-----PCMPDTYHERKQVLEKELKHLREALQQTQQshayLTQKREAQEEqlKKQQLLKQLRArieelrAQEAV 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   295 VAKA-ELAEVRREWAKYM-------EVHEKASFTNSELHRAMNLhvgnlrllsgpldqvRAALptpaltpedkavLQNLK 366
Cdd:TIGR00618  279 LEETqERINRARKAAPLAahikavtQIEQQAQRIHTELQSKMRS---------------RAKL------------LMKRA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   367 RILAKVQEMRDQRVSLEQQLRELIQKDDIT-ASLVTTDHSEMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQ 445
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHeVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   446 YAAV---RRVL---------SELDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYA-----DLESKVATLLERAQSI--C 506
Cdd:TIGR00618  412 IDTRtsaFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlkereQQLQTKEQIHLQETRKkaV 491

                          330
                   ....*....|....*..
gi 755531599   507 RAQEAARQQLLDRELKK 523
Cdd:TIGR00618  492 VLARLLELQEEPCPLCG 508

Name

Accession

Description

Interval

E-value

V_HD-PTP_like

cd09234

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...

169-509

0e+00

Pssm-ID: 185747 [Multi-domain] Cd Length: 337 Bit Score: 543.42 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLDPETVDNLDAYNHIPPQLMEKCAALSVRPDTVKNLVQS 248
Cdd:cd09234     1 PMEAHEASSLYSEEKAKLLREVVSEIEDKDEELDQFLSSLQLDPLNVMDMDGQFELPQDLVERCAALSVRPDTIKNLVEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  249 MQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPgpsvakAELAEVRREWAKYMEVHEKASFTNSELHRAM 328
Cdd:cd09234    81 MGELSDVYQDVEAMLNEIESLLEEEELQEKEFQEAVGKRGSSI------AHVTELKRELKKYKEAHEKASQSNTELHKAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  329 NLHVGNLRLLSGPLDQVRAALPTPALT--PEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSE 406
Cdd:cd09234   155 NLHIANLKLLAGPLDELQKKLPSPSLLdrPEDEAIEKELKRILNKVNEMRKQRRSLEQQLRDAIHEDDITSKLVTTTGGD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  407 MKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKD 486
Cdd:cd09234   235 MEDLFKEELKKHDQLVNLIEQNLAAQENILKALTEANAKYAPVRKALSETKQKRESTISSLIASYEAYEDLLKKSQKGID 314

                         330       340
                  ....*....|....*....|...
gi 755531599  487 FYADLESKVATLLERAQSICRAQ 509
Cdd:cd09234   315 FYKKLEGNVSKLLQRIKSVCKVQ 337

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1106-1310

2.66e-129

Pssm-ID: 350387 [Multi-domain] Cd Length: 205 Bit Score: 399.07 E-value: 2.66e-129

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVALSS 1185
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQRPLHTPIVVHCSSGVGRTGAF 1265
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755531599 1266 ALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14539   161 CLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

V_Alix_like

cd08915

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...

169-506

6.79e-96

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.

Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 312.74 E-value: 6.79e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREML-AKIEDKNEVLDQFMDSMQLdPETVDNLDAYNHIPPQLmeKCAALSVRPDTVKNLVQ 247
Cdd:cd08915     1 PYDVIESASAYNERQDDYVREHIvEPIEALNKLLNSFLAERNL-PASIDDLQKPENLPDSI--QHSQEIIEEGGLDNIEQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  248 SMQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPGPSvaKAELAEVRREWAKYMEVHEKASFTNSELHRA 327
Cdd:cd08915    78 SFKELSKLRQNVEELLQECEELLEEEAAEDDQLRAKFGTLRWRRPSS--DEAAKELYEKVTKLRGYLEQASNSDNEVLQC 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  328 MNLHVGNLRLLSGPLDQVRAALP--TPALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHS 405
Cdd:cd08915   156 YESIDPNLVLLCGGYKELKAFIPspYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELEIKSRNNDILPKLITEYKK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  406 ----EMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRvLSELDQKWNSTLQTLVASYEAYEDLMKKS 481
Cdd:cd08915   236 ngttEFEDLFEEHLKKFDKDLTYVEKTKKKQIELIKEIDAANQEFSQVKN-SNDSLDPREEALQDLEASYKKYLELKENL 314

                         330       340
                  ....*....|....*....|....*
gi 755531599  482 QEGKDFYADLESKVATLLERAQSIC 506
Cdd:cd08915   315 NEGSKFYNDLIEKVNRLLEECEDFV 339

BRO1_HD-PTP_like

cd09239

Protein-interacting, N-terminal, Bro1-like domain of mammalian His-Domain type N23 protein ...

1-164

5.21e-93

Pssm-ID: 185762 Cd Length: 361 Bit Score: 305.51 E-value: 5.21e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    1 MLDNRKSFLVARISAQVVDYYKEACRALENPDTAS--LLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVA 78
Cdd:cd09239   194 LLDNRKSHITAKVSAQVVEYYKEALRALENWESNSkiILGKIQKEWRKLVQMKIAYYASIAHLHMGKQSEEQQKMGERVA 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   79 YFQSALDKLNEAIKLAKGQPDT--VQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDP 156
Cdd:cd09239   274 YYQLANDKLEEAIKNAKGQPDTvnLQEALSFTMDVIGGKRNSAKKENDFIYHEAVPKLDTLQAVKGANLVKGIPFSPTDP 353


                  ....*...
gi 755531599  157 AVTGPDIF 164
Cdd:cd09239   354 EVCGPDIF 361

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1083-1313

8.31e-86

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 279.90 E-value: 8.31e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  1083 KNRHQDVMPYDSNRVVL--RSGKDDYINASCVEGlSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQ 1160
Cdd:pfam00102    4 KNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDG-YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGRE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  1161 KVARYFPTERGQPMVHGALSVALSSIRTTETH-VERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:pfam00102   83 KCAQYWPEEEGESLEYGDFTVTLKKEKEDEKDyTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRK 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599  1240 HYlhQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:pfam00102  163 SS--LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEA-EGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1083-1314

2.35e-82

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 271.07 E-value: 2.35e-82

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   1083 KNRHQDVMPYDSNRVVLRSGK---DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:smart00194   30 KNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGP-KAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGR 108

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   1160 QKVARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:smart00194  109 EKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRK 188

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531599   1240 HYLHQRplhTPIVVHCSSGVGRTGAFALLYAAVQEVEAGnGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:smart00194  189 SQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

ALIX_LYPXL_bnd

pfam13949

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...

224-510

7.52e-70

Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 236.75 E-value: 7.52e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   224 IPPQLMEKCAALSVRpDTVKNLVQSMQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPGPSVAKAELaev 303
Cdd:pfam13949    2 LPPSLREKAEEVRQQ-GGIERLEKSLDDLPKLKQRNREILDEAEKLLDEEESEDEQLRAKYGTRWTRPPSSELTATL--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   304 RREWAKYMEVHEKASFTNSELHRAMNLHVGNLRLLSGPLDQVRAALPT---PALTPEDKAVLQNLKRILAKVQEMRDQRV 380
Cdd:pfam13949   78 RAEIRKYREILEQASESDSQVRSKFREHEEDLELLSGPDEDLEAFLPSsrrAKNSPSVEEQVAKLRELLNKLNELKRERE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   381 SLEQQLRELIQKDDITASLVTT-----DHSEMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSE 455
Cdd:pfam13949  158 QLLKDLKEKARNDDISPKLLLEkarliAPNQEEQLFEEELEKYDPLQNRLEQNLHKQEELLKEITEANNEFLQDKRVDSE 237

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755531599   456 LDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYADLESKVATLLERAQSICRAQE 510
Cdd:pfam13949  238 KQRQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARR 292

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

1106-1310

1.42e-68

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.

Pssm-ID: 350343 [Multi-domain] Cd Length: 200 Bit Score: 229.09 E-value: 1.42e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPyCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVALSS 1185
Cdd:cd00047     1 YINASYIDGYRG-PKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAhylHQRPLHTPIVVHCSSGVGRTGAF 1265
Cdd:cd00047    80 EEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK---EARKPNGPIVVHCSAGVGRTGTF 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755531599 1266 ALLYAAVQEVEAGNgIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd00047   157 IAIDILLERLEAEG-EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

BRO1

pfam03097

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...

1-187

4.39e-68

Pssm-ID: 460803 Cd Length: 366 Bit Score: 234.40 E-value: 4.39e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599     1 MLDNRKSFLVARISAQVVDYYKEACRALENPDTasllgrIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYF 80
Cdd:pfam03097  188 INDNKKDSLIAKLAAQVSELYEEALEALKLSGL------IDKEWISHVQAKAHHFKALAQYRQALDDEEAKKYGEEIARL 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    81 QSALDKLNEAIKLAKGQpdTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDPAVTG 160
Cdd:pfam03097  262 QLALSLLKEALKSDRYK--KVLEDLKGLLDVVEEKLKRAEKDNDFIYHERVPSESSLPPIKPASMVKPIPPLELYPFQIG 339

                          170       180
                   ....*....|....*....|....*..
gi 755531599   161 PDIFAKLVPMAAHEASSLYSEEKAKLL 187
Cdd:pfam03097  340 PDLFKKLVPLSVHEAASAYSERKAKLV 366

BRO1

smart01041

BRO1-like domain; This domain is found in a number proteins including Rhophilin and BRO1. It ...

1-189

8.58e-67

Pssm-ID: 214990 Cd Length: 381 Bit Score: 231.09 E-value: 8.58e-67

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599      1 MLDNRK--SFLVARISAQVVDYYKEACRALENPDTASllGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVA 78
Cdd:smart01041  190 ILDGMKnkDSLIAKLAAQAAEYYEEALKALQTSEPVK--GYIPKSWIKLVQVKAHHFKALAHYYQALDLEEANKYGEAIA 267

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599     79 YFQSALDKLNEAIKLA----KGQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPT 154
Cdd:smart01041  268 RLQEALERLKEAKKHLrckkLGKADKLQEDLSGLKDVVEEKLKEAEKDNDFIYHERVPDIVSLPPIKKAPLVKPPPFSEV 347

                           170       180       190
                    ....*....|....*....|....*....|....*
gi 755531599    155 DpavTGPDIFAKLVPMAAHEASSLYSEEKAKLLRE 189
Cdd:smart01041  348 L---KGPDLFAKLVPMAVHEAASLYSEEKAKLVRA 379

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

1074-1309

2.85e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.

Pssm-ID: 350391 [Multi-domain] Cd Length: 271 Bit Score: 182.18 E-value: 2.85e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1074 IAIARCYSLKNRHQDVMPYDSNRVVL--RSGKD--DYINASCVEGLS---PYcpplVATQAPLPGTAADFWLMVHEQKVS 1146
Cdd:cd14543    23 CSLAPANQEKNRYGDVLCLDQSRVKLpkRNGDErtDYINANFMDGYKqknAY----IATQGPLPKTYSDFWRMVWEQKVL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1147 VIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDS 1226
Cdd:cd14543    99 VIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1227 PGNLLRFIQEVHAhylHQR-------------PLHTPIVVHCSSGVGRTGAFALLYAAVQEVEaGNGIPELPQLVRRMRQ 1293
Cdd:cd14543   179 AAALLDFLGEVRQ---QQAlavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLE-DVGTLNVMQTVRRMRT 254

                         250
                  ....*....|....*.
gi 755531599 1294 QRKHMLQEKLHLKFCH 1309
Cdd:cd14543   255 QRAFSIQTPDQYYFCY 270

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

1084-1309

1.53e-47

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.

Pssm-ID: 350395 [Multi-domain] Cd Length: 224 Bit Score: 169.88 E-value: 1.53e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLRSGKDD----YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMeK 1159
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKVARYFPTErgQPMVHGALSVALSSIRTTETHVERVLSLQFRDQslKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:cd14547    80 EKCAQYWPEE--ENETYGDFEVTVQSVKETDGYTVRKLTLKYGGE--KRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1240 HYLHQRPlHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCH 1309
Cdd:cd14547   156 ARQTEPH-RGPIVVHCSAGIGRTGCFIATSIGCQQLRE-EGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

1083-1316

1.13e-46

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350401 [Multi-domain] Cd Length: 238 Bit Score: 167.96 E-value: 1.13e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 1156
Cdd:cd14553     6 KNRYANVIAYDHSRVILQPIEgvpgSDYINANYCDG---YRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1157 MEKQKVARYFPTeRGQPmVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQE 1236
Cdd:cd14553    83 RSRVKCDQYWPT-RGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1237 VHAHYlhqRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14553   161 VKACN---PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTV-DIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

1085-1310

6.34e-46

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 165.22 E-value: 6.34e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1085 RHQDVMPYDSNRVVLRSGKD----DYINASCVEGlsPYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEeegsDYINANYIPG--YNSPrEFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKVARYFPtERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:cd14548    79 VKCDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599 1240 hYLHQRplHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14548   156 -YIKQE--KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYV-DIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

1106-1312

9.34e-46

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.

Pssm-ID: 350386 [Multi-domain] Cd Length: 207 Bit Score: 164.08 E-value: 9.34e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVE---GLSPYcpPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQP-MVHGALSV 1181
Cdd:cd14538     1 YINASHIRipvGGDTY--HYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPlICGGRLEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1182 ALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQevHAHYLHQRplhTPIVVHCSSGVGR 1261
Cdd:cd14538    79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIR--YMRRIHNS---GPIVVHCSAGIGR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1262 TGAFALLYAAVQEVEagNGIP-ELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14538   154 TGVLITIDVALGLIE--RDLPfDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

1083-1312

1.94e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 162.30 E-value: 1.94e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVL----RSGKDDYINASCVEGLS---PYcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEA 1155
Cdd:cd14603    33 KNRYKDILPYDQTRVILsllqEEGHSDYINANFIKGVDgsrAY----IATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1156 EMEKQKVARYFPTERgQPMVHGALSVA-LSSIRTTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPGNLLRFI 1234
Cdd:cd14603   109 EMGKKKCERYWAQEQ-EPLQTGPFTITlVKEKRLNEEVILRTLKVTFQKES--RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1235 QEVHAHYLHQRplhTPIVVHCSSGVGRTGAF-ALLYaaVQEVEAGNGIPE---LPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14603   186 ELARRLQGSGP---EPLCVHCSAGCGRTGVIcTVDY--VRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYH 260


                  ..
gi 755531599 1311 AL 1312
Cdd:cd14603   261 TV 262

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

1083-1314

3.05e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.

Pssm-ID: 350448 [Multi-domain] Cd Length: 274 Bit Score: 162.33 E-value: 3.05e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRsGKDDYINASCVEGLSPYCPPL---VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:cd14600    43 KNRYKDVLPYDATRVVLQ-GNEDYINASYVNMEIPSANIVnkyIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGR 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKVARYFPtERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:cd14600   122 TKCHQYWP-DPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599 1240 hylhQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEagNGIPELP-QLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:cd14600   201 ----KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTE--RNQPVYPlDIVRKMRDQRAMMVQTSSQYKFVCEAILR 270

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

1083-1309

6.08e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.

Pssm-ID: 350393 [Multi-domain] Cd Length: 231 Bit Score: 159.86 E-value: 6.08e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLR--SGKDDYINASCVEGLSP---YcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEM 1157
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKlkQGDNDYINASLVEVEEAkrsY----ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1158 EKQKVARYFPTERGQPMV--HGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQ 1235
Cdd:cd14545    77 GQIKCAQYWPQGEGNAMIfeDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531599 1236 EVHAHYLHQrPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIP-ELPQLVRRMRQQRKHMLQEKLHLKFCH 1309
Cdd:cd14545   157 KVRESGSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSvDVKKVLLEMRKYRMGLIQTPDQLRFSY 230

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

1082-1317

8.25e-44

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.

Pssm-ID: 350392 [Multi-domain] Cd Length: 251 Bit Score: 159.94 E-value: 8.25e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1082 LKNRHQDVMPYDSNRVVLRSGK-----DDYINASCV-----EGLSPYC-PPLVATQAPLPGTAADFWLMVHEQKVSVIVM 1150
Cdd:cd14544     3 GKNRYKNILPFDHTRVILKDRDpnvpgSDYINANYIrneneGPTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVIVM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1151 LVSEAEMEKQKVARYFPTErGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQ-SLKRSLVHLHFPTWPELGLPDSPGN 1229
Cdd:cd14544    83 TTKEVERGKNKCVRYWPDE-GMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQgDPIREIWHYQYLSWPDHGVPSDPGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1230 LLRFIQEVHAHYLHqRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIP---ELPQLVRRMRQQRKHMLQEKLHLK 1306
Cdd:cd14544   162 VLNFLEDVNQRQES-LPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKR-KGLDcdiDIQKTIQMVRSQRSGMVQTEAQYK 239

                         250
                  ....*....|.
gi 755531599 1307 FCHEALVRHVE 1317
Cdd:cd14544   240 FIYVAVAQYIE 250

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1079-1311

1.95e-43

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).

Pssm-ID: 350402 [Multi-domain] Cd Length: 238 Bit Score: 158.46 E-value: 1.95e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1079 CYSLKNRHQDVMPYDSNRVVLR--SGKD--DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSE 1154
Cdd:cd14554     5 CNKFKNRLVNILPYESTRVCLQpiRGVEgsDYINASFIDGYR-QRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1155 AEMEKQKVARYFPTERGQPmvHGALSV-ALSSIRTTETHVERVLSLQFRDQSLkRSLVHLHFPTWPELGLPDSPGNLLRF 1233
Cdd:cd14554    84 REMGREKCHQYWPAERSAR--YQYFVVdPMAEYNMPQYILREFKVTDARDGQS-RTVRQFQFTDWPEQGVPKSGEGFIDF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599 1234 IQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEA 1311
Cdd:cd14554   161 IGQVHKTK-EQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRY-EGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

1083-1313

3.03e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.

Pssm-ID: 350445 [Multi-domain] Cd Length: 234 Bit Score: 154.99 E-value: 3.03e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLrsGKD-DYINASCVE---GLSPYCppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14597     6 KNRYKNILPYDTTRVPL--GDEgGYINASFIKmpvGDEEFV--YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTERGQP-MVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQev 1237
Cdd:cd14597    82 KIKCQRYWPEILGKTtMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS-- 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599 1238 hahYLHQRPLHTPIVVHCSSGVGRTGAFALLyAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14597   160 ---YMRHIHKSGPIITHCSAGIGRSGTLICI-DVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

1083-1312

3.25e-42

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 155.89 E-value: 3.25e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGKDDYINASCV---EGLSPYcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:cd14607    27 RNRYRDVSPYDHSRVKLQNTENDYINASLVvieEAQRSY----ILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKVARYFPTERGQPMVHG--ALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEV 1237
Cdd:cd14607   103 VKCAQYWPTDEEEVLSFKetGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599 1238 HAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIP-ELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14607   183 RESG-SLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSvDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

1083-1320

1.14e-41

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.

Pssm-ID: 350452 [Multi-domain] Cd Length: 297 Bit Score: 155.48 E-value: 1.14e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVL----RSGKDDYINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEM 1157
Cdd:cd14604    60 KNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGV--YGPkAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEM 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1158 EKQKVARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPGNLLRFIQEV 1237
Cdd:cd14604   138 GRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1238 HAHYLHQRplhTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNgIPE---LPQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:cd14604   216 RKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGK-IPEefnVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQ 291


                  ....*.
gi 755531599 1315 HVEQVL 1320
Cdd:cd14604   292 LFEKQL 297

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1084-1300

2.25e-41

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 152.28 E-value: 2.25e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRV---VLRSGKDDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14615     1 NRYNNVLPYDISRVklsVQSHSTDDYINANYMPG---YNSKkeFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTErgQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVH 1238
Cdd:cd14615    78 RTKCEEYWPSK--QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1239 aHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQ 1300
Cdd:cd14615   156 -EYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVV-DVYGIVYDLRMHRPLMVQ 215

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

1084-1310

4.48e-41

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 151.61 E-value: 4.48e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLRSGKD----DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNN-FRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKVARYFPTERgQPMVHGALSVALSSIRTTETHVERVLSLQFRDQ-SLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVH 1238
Cdd:cd14617    80 VKCDHYWPADQ-DSLYYGDLIVQMLSESVLPEWTIREFKICSEEQlDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1239 aHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14617   159 -DYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

1106-1310

1.78e-40

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.

Pssm-ID: 350509 [Multi-domain] Cd Length: 212 Bit Score: 148.94 E-value: 1.78e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEglSPYCPPL--VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqPMVHGALSVAL 1183
Cdd:cd18533     1 YINASYIT--LPGTSSKryIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEY-EGEYGDLTVEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTE--THVERVLSLQfRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHaHYLHQRPLHTPIVVHCSSGVGR 1261
Cdd:cd18533    78 VSEEENDdgGFIVREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKR-ELNDSASLDPPIIVHCSAGVGR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755531599 1262 TGAFALLYAAVQEVEAG-NGIPELP-------QLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd18533   156 TGTFIALDSLLDELKRGlSDSQDLEdsedpvyEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

1084-1314

1.83e-40

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 149.65 E-value: 1.83e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLR----SGKDDYINASCVEGL-SPycPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKpiheEPGSDYINANYMPGYwSS--QEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTERgQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVH 1238
Cdd:cd14619    79 RVKCEHYWPLDY-TPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599 1239 aHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:cd14619   158 -QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQS-EGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1105-1314

4.51e-40

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.

Pssm-ID: 350389 [Multi-domain] Cd Length: 212 Bit Score: 147.86 E-value: 4.51e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1105 DYINASCVEGLSP-------YcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPtERGQPMVHG 1177
Cdd:cd14541     1 DYINANYVNMEIPgsgivnrY----IAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQFG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1178 ALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVhahylhqRPLHT----PIVV 1253
Cdd:cd14541    76 NLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV-------RQNRVgmvePTVV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599 1254 HCSSGVGRTGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:cd14541   149 HCSAGIGRTGVLITMETAMCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRFVCEAILR 208

BRO1_Alix_like

cd09034

Protein-interacting Bro1-like domain of mammalian Alix and related domains; This superfamily ...

4-151

7.52e-40

Pssm-ID: 185761 [Multi-domain] Cd Length: 345 Bit Score: 151.73 E-value: 7.52e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    4 NRKSFLVARISAQVVDYYKEACRALENPDtASLLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQSA 83
Cdd:cd09034   199 KAKLSLLARLACEAAKYYEEALKCLSGVD-LETIKNIPKKWLLFLKWKKCIFKALAYYYHGLKLDEANKIGEAIARLQAA 277

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599   84 LDKLNEAIKLAKGQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPV 151
Cdd:cd09034   278 LELLKESERLCKSFLLDVWGNLKKLKEKIEKELEKAERENDFIYFEEVPPEDPLPEIKGALLVKPPPL 345

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

1106-1310

2.28e-39

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350397 [Multi-domain] Cd Length: 204 Bit Score: 145.57 E-value: 2.28e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPyCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqpMVHGALSVALSS 1185
Cdd:cd14549     1 YINANYVDGYNK-ARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGT--ETYGNIQVTLLS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQ------FRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHylhqRPLHT-PIVVHCSSG 1258
Cdd:cd14549    78 TEVLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA----NPPGAgPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1259 VGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14549   154 VGRTGTYIVIDSMLQQIQDKGTV-NVFGFLKHIRTQRNYLVQTEEQYIFIHD 204

BRO1_ScRim20-like

cd09241

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and ...

2-174

6.56e-39

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 and related proteins; This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Rim20 (also known as PalA) and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Bro1, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Rim20 and Rim23 participate in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Rim20. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain is a dimerization domain that also contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the V-domain superfamily. Rim20 localizes to endosomes under alkaline pH conditions. By binding Snf7, it may bring the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and thus aid in the proteolytic activation of the latter. Rim20 and other intermediates in the Rim101 pathway play roles in the pathogenesis of fungal corneal infection during Candida albicans keratitis.

Pssm-ID: 185764 Cd Length: 355 Bit Score: 149.34 E-value: 6.56e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    2 LDNRKSFLVARISAQVVDYYKEACRALENPDTasllgrIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQ 81
Cdd:cd09241   188 SDGTKDSLIAKLAAQVSDYYQEALKYANKSDL------IRSDWINHLKVKKHHFKAAAHYRMALVALEKSKYGEEVARLR 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   82 SALDKLNEAIKLAKGQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKP-LPVNPTDPAVTG 160
Cdd:cd09241   262 VALAACKEALKEARYGNKAVLEDLQGLKDIVKESLKRAERDNDLIYLQPVPPASELPPIKPASMVKAiVPPELEEGSKLG 341

                         170
                  ....*....|....
gi 755531599  161 PDIFAKLVPMAAHE 174
Cdd:cd09241   342 KPLFKDLLPYGVHE 355

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

1083-1314

1.37e-38

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.

Pssm-ID: 350447 [Multi-domain] Cd Length: 287 Bit Score: 146.30 E-value: 1.37e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGKDD---YINAS----CVEGLSPYcppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEA 1155
Cdd:cd14599    41 RNRIREVVPYEENRVELVPTKENntgYINAShikvTVGGEEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1156 EMEKQKVARYFPT--ERGQPMVHGALSVAlSSIR-------TTETHVERVLSLQfrdqslKRSLVHLHFPTWPELGLPDS 1226
Cdd:cd14599   118 EGGRSKSHRYWPKlgSKHSSATYGKFKVT-TKFRtdsgcyaTTGLKVKHLLSGQ------ERTVWHLQYTDWPDHGCPEE 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1227 PGNLLRFIQEVHAHYLHQRPL-------HTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHML 1299
Cdd:cd14599   191 VQGFLSYLEEIQSVRRHTNSMldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKV-EVPVMLRHLREQRMFMI 269

                         250
                  ....*....|....*
gi 755531599 1300 QEKLHLKFCHEALVR 1314
Cdd:cd14599   270 QTIAQYKFVYQVLIQ 284

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

1058-1313

1.39e-38

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.

Pssm-ID: 350456 [Multi-domain] Cd Length: 277 Bit Score: 145.94 E-value: 1.39e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1058 WRELQEAQEHDARGRSIAIARCYSLK--NRHQDVMPYDSNRVVLRSGKDDYINASCV---EGLSPYcpplVATQAPLPGT 1132
Cdd:cd14608     1 WAAIYQDIRHEASDFPCRVAKLPKNKnrNRYRDVSPFDHSRIKLHQEDNDYINASLIkmeEAQRSY----ILTQGPLPNT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1133 AADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMV--HGALSVALSSIRTTETHVERVLSLQFRDQSLKRSL 1210
Cdd:cd14608    77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIfeDTNLKLTLISEDIKSYYTVRQLELENLTTQETREI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1211 VHLHFPTWPELGLPDSPGNLLRFIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAA--VQEVEAGNGIPELPQLV 1288
Cdd:cd14608   157 LHFHYTTWPDFGVPESPASFLNFLFKVRESG-SLSPEHGPVVVHCSAGIGRSGTFCLADTCllLMDKRKDPSSVDIKKVL 235

                         250       260
                  ....*....|....*....|....*
gi 755531599 1289 RRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14608   236 LEMRKFRMGLIQTADQLRFSYLAVI 260

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

1106-1310

1.45e-38

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.

Pssm-ID: 350496 [Multi-domain] Cd Length: 206 Bit Score: 143.37 E-value: 1.45e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVE-GLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE-MEKQKVARYFPTERGQPMVHGALSVAL 1183
Cdd:cd17658     1 YINASLVEtPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVE-RVLSLQFRDQSLK-RSLVHLHFPTWPELGLPDSPgnllRFIQEVHAHYLHQRPLHTPIVVHCSSGVGR 1261
Cdd:cd17658    81 KKLKHSQHSITlRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDT----RSVRELLKRLYGIPPSAGPIVVHCSAGIGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755531599 1262 TGAFALLYAAVQEVEAGN-GIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd17658   157 TGAYCTIHNTIRRILEGDmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

1055-1319

2.02e-38

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.

Pssm-ID: 350457 [Multi-domain] Cd Length: 281 Bit Score: 145.57 E-value: 2.02e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1055 DAIWRELQEAQEHDARGRSIAIARCYS--LKNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGLSPYCPPLVATQAP 1128
Cdd:cd14609    15 DRLAKEWQALCAYQAEPNTCSTAQGEAnvKKNRNPDFVPYDHARIKLKAesnpSRSDYINASPIIEHDPRMPAYIATQGP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1129 LPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTErGQPMVHgALSVALSSIRT-TETHVERVLSLQFRDQSLK 1207
Cdd:cd14609    95 LSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDE-GSSLYH-IYEVNLVSEHIwCEDFLVRSFYLKNVQTQET 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1208 RSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYlhqRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQL 1287
Cdd:cd14609   173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY---RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAAT 249

                         250       260       270
                  ....*....|....*....|....*....|..
gi 755531599 1288 VRRMRQQRKHMLQEKLHLKFCHEALVRHVEQV 1319
Cdd:cd14609   250 LEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1106-1314

4.53e-38

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.

Pssm-ID: 350388 [Multi-domain] Cd Length: 219 Bit Score: 142.60 E-value: 4.53e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINAS----CVEGLSPYcppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQ--PMVHGAL 1179
Cdd:cd14540     1 YINAShitaTVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1180 SVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA---HYLHQRPLHT---PIVV 1253
Cdd:cd14540    78 KVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrHTNQDVAGHNrnpPTLV 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531599 1254 HCSSGVGRTGAFAL----LYAAVQEVEagngiPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:cd14540   158 HCSAGVGRTGVVILadlmLYCLDHNEE-----LDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

1083-1313

6.10e-38

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350474 [Multi-domain] Cd Length: 276 Bit Score: 144.02 E-value: 6.10e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14626    44 KNRYANVIAYDHSRVILTSvdgvPGSDYINANYIDGYRKQ-NAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTeRGQPmVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVH 1238
Cdd:cd14626   123 RVKCDQYWPI-RGTE-TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531599 1239 AhylHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14626   201 A---CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV-DIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

1083-1317

9.64e-38

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.

Pssm-ID: 350453 [Multi-domain] Cd Length: 253 Bit Score: 142.85 E-value: 9.64e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGK-----DDYINASCV----EGLSPYCPP---LVATQAPLPGTAADFWLMVHEQKVSVIVM 1150
Cdd:cd14605     5 KNRYKNILPFDHTRVVLHDGDpnepvSDYINANIImpefETKCNNSKPkksYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1151 LVSEAEMEKQKVARYFPTERGQPMvHGALSValSSIRTTETH--VERVLSLQFRDQ-SLKRSLVHLHFPTWPELGLPDSP 1227
Cdd:cd14605    85 TTKEVERGKSKCVKYWPDEYALKE-YGVMRV--RNVKESAAHdyILRELKLSKVGQgNTERTVWQYHFRTWPDHGVPSDP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1228 GNLLRFIQEVHahyLHQRPLHT--PIVVHCSSGVGRTGAFA---LLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEK 1302
Cdd:cd14605   162 GGVLDFLEEVH---HKQESIMDagPVVVHCSAGIGRTGTFIvidILIDIIREKGVDCDI-DVPKTIQMVRSQRSGMVQTE 237

                         250
                  ....*....|....*
gi 755531599 1303 LHLKFCHEALVRHVE 1317
Cdd:cd14605   238 AQYRFIYMAVQHYIE 252

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

1106-1309

1.37e-37

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.

Pssm-ID: 350390 [Multi-domain] Cd Length: 202 Bit Score: 140.25 E-value: 1.37e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlsPYCPPL-VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVAL- 1183
Cdd:cd14542     1 YINANFIKG--VSGSKAyIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVERVLSLQFrdQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQRPlhtPIVVHCSSGVGRTG 1263
Cdd:cd14542    79 KEKRVGPDFLIRTLKVTF--QKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV---PICVHCSAGCGRTG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 755531599 1264 AFALLYAAVQEVEAGnGIPE---LPQLVRRMRQQRKHMLQEKLHLKFCH 1309
Cdd:cd14542   154 TICAIDYVWNLLKTG-KIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

1106-1321

1.37e-37

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.

Pssm-ID: 350444 [Multi-domain] Cd Length: 207 Bit Score: 140.65 E-value: 1.37e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEglSPYCPP---LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVA 1182
Cdd:cd14596     1 YINASYIT--MPVGEEelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1183 LSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQevhahYLHQRPLHTPIVVHCSSGVGRT 1262
Cdd:cd14596    79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFIC-----YMRKVHNTGPIVVHCSAGIGRA 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755531599 1263 GAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALVrhveQVLQ 1321
Cdd:cd14596   154 GVLICVDVLLSLIEKDLSF-NIKDIVREMRQQRYGMIQTKDQYLFCYKVVL----EVLQ 207

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1083-1316

4.21e-37

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 141.71 E-value: 4.21e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLR--SGKD----DYINASCVEGLSPyCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 1156
Cdd:cd17667    30 KNRYINILAYDHSRVKLRplPGKDskhsDYINANYVDGYNK-AKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1157 MEKQKVARYFPTERGQPmvHGALSVALSSIRTTETHVERVLSLqfRDQSLK-------------RSLVHLHFPTWPELGL 1223
Cdd:cd17667   109 KGRRKCDQYWPTENSEE--YGNIIVTLKSTKIHACYTVRRFSI--RNTKVKkgqkgnpkgrqneRTVIQYHYTQWPDMGV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1224 PDSPGNLLRFIQEVHAhylHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHMLQEKL 1303
Cdd:cd17667   185 PEYALPVLTFVRRSSA---ARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL-GFLKHIRTQRNYLVQTEE 260

                         250
                  ....*....|...
gi 755531599 1304 HLKFCHEALVRHV 1316
Cdd:cd17667   261 QYIFIHDALLEAI 273

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

1105-1312

4.56e-37

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 138.98 E-value: 4.56e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1105 DYINASCVEGL--SPYcppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTErgQPMVHGALSVA 1182
Cdd:cd14622     1 DYINASFIDGYrqKDY---FIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE--GSVTHGEITIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1183 LSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHylHQRPLHTPIVVHCSSGVGRT 1262
Cdd:cd14622    76 IKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQ--QQQTGNHPIVVHCSAGAGRT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755531599 1263 GAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14622   154 GTFIALSNILERVKA-EGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

1089-1312

4.92e-37

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 139.79 E-value: 4.92e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1089 VMPYDSNRVVL--RSGKD--DYINASCVEGLSPYCPPlVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVAR 1164
Cdd:cd14623     5 IIPYEFNRVIIpvKRGEEntDYVNASFIDGYRQKDSY-IASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1165 YFPTErgQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHylHQ 1244
Cdd:cd14623    84 YWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ--QQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599 1245 RPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14623   160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKA-EGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

1106-1310

8.94e-37

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 138.29 E-value: 8.94e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERgqpMVHGALSVALS 1184
Cdd:cd14558     1 YINASFIDGY--WGPkSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK---KTYGDIEVELK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1185 SIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHaHYLHQRPL----HTPIVVHCSSGVG 1260
Cdd:cd14558    76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIK-QKLPYKNSkhgrSVPIVVHCSDGSS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755531599 1261 RTGAFA----LLYAAVQEveagnGIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14558   155 RTGIFCalwnLLESAETE-----KVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

1083-1313

1.05e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.

Pssm-ID: 350450 [Multi-domain] Cd Length: 234 Bit Score: 139.20 E-value: 1.05e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLR---SGKD-DYINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEM 1157
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitSDEDsDYINANFIKGV--YGPrAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1158 EKQKVARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQFrdQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEV 1237
Cdd:cd14602    79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755531599 1238 HAHYLHQRPlhtPIVVHCSSGVGRTGAFALLYAAVQEVEAGNgIPE---LPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14602   157 RCYQEDDSV---PICIHCSAGCGRTGVICAIDYTWMLLKDGI-IPEnfsVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

1083-1319

1.55e-36

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.

Pssm-ID: 350458 [Multi-domain] Cd Length: 283 Bit Score: 140.19 E-value: 1.55e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14610    47 KNRSLAVLPYDHSRIILKAenshSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTErGQPMVHgalsvaLSSIRTTETHV--ERVLSLQFRDQSLK----RSLVHLHFPTWPELGLPDSPGNLLR 1232
Cdd:cd14610   127 VKQCYHYWPDE-GSNLYH------IYEVNLVSEHIwcEDFLVRSFYLKNLQtnetRTVTQFHFLSWNDQGVPASTRSLLD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1233 FIQEVHAHYlhqRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14610   200 FRRKVNKCY---RGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 276


                  ....*..
gi 755531599 1313 VRHVEQV 1319
Cdd:cd14610   277 AEEVNAI 283

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

1106-1313

2.15e-36

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).

Pssm-ID: 350400 [Multi-domain] Cd Length: 202 Bit Score: 137.02 E-value: 2.15e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTErgQPMVHGALSVALSS 1185
Cdd:cd14552     1 YINASFIDGYRQK-DAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED--GSVSSGDITVELKD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHylHQRPLHTPIVVHCSSGVGRTGAF 1265
Cdd:cd14552    78 QTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQ--QQQSGNHPITVHCSAGAGRTGTF 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755531599 1266 ALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14552   156 CALSTVLERVKA-EGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

1080-1312

2.45e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.

Pssm-ID: 350460 [Multi-domain] Cd Length: 247 Bit Score: 138.43 E-value: 2.45e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1080 YSLKNRHQDVMPYDSNRVVLRSGK-----DDYINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSE 1154
Cdd:cd14612    15 HASKDRYKTILPNPQSRVCLRRAGsqeeeGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1155 AEmEKQKVARYFPTERGQpmvHGALSVALSSIRTTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPGNLLRFI 1234
Cdd:cd14612    95 KE-KKEKCVHYWPEKEGT---YGRFEIRVQDMKECDGYTIRDLTIQLEEES--RSVKHYWFSSWPDHQTPESAGPLLRLV 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599 1235 QEVHAHyLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14612   169 AEVEES-RQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKD-TGKVDILGIVCQLRLDRGGMIQTSEQYQFLHHTL 244

PHA02738

hypothetical protein; Provisional

1084-1317

3.22e-36

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 140.45 E-value: 3.22e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLRSGKD--DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQK 1161
Cdd:PHA02738   53 NRYLDAVCFDHSRVILPAERNrgDYINANYVDGFE-YKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREK 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1162 VARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQfRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEV---- 1237
Cdd:PHA02738  132 CFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVrqcq 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1238 ---HAHYL---HQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEA 1311
Cdd:PHA02738  211 kelAQESLqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATV-SIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                  ....*.
gi 755531599 1312 LVRHVE 1317
Cdd:PHA02738  290 VKRYVN 295

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

1084-1313

4.34e-36

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.

Pssm-ID: 350466 [Multi-domain] Cd Length: 230 Bit Score: 137.00 E-value: 4.34e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLRS-GKD---DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQlGGEphsDYINANFIPGYT-SPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKVARYFPTErGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHA 1239
Cdd:cd14618    80 VLCDHYWPSE-STPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599 1240 HyLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14618   159 H-VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKE-EKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

1084-1310

4.78e-36

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.

Pssm-ID: 350464 [Multi-domain] Cd Length: 224 Bit Score: 136.96 E-value: 4.78e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1084 NRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAgvpgSDYINASYISGY--LCPnEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPtERGQPMvhgalsVALSSIRTTETHVERVLSLQFRDQSLKRS-----LVHLHFPTWPELGLPDSPGNLLRF 1233
Cdd:cd14616    79 RIRCHQYWP-EDNKPV------TVFGDIVITKLMEDVQIDWTIRDLKIERHgdymmVRQCNFTSWPEHGVPESSAPLIHF 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531599 1234 IQEVHAHYLHQrplHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14616   152 VKLVRASRAHD---NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFV-DIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

1106-1316

8.01e-36

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.

Pssm-ID: 350394 [Multi-domain] Cd Length: 208 Bit Score: 135.65 E-value: 8.01e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQpmVHGALSVALSS 1185
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE--VYHIYEVHLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRT-TETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYlhqRPLHTPIVVHCSSGVGRTGA 1264
Cdd:cd14546    79 EHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY---RGRSCPIVVHCSDGAGRTGT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1265 FALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14546   156 YILIDMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

1067-1310

1.19e-35

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 136.56 E-value: 1.19e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1067 HDARgrSIAIARCyslKNRHQDVMPYDSNRVVLRSGKD----DYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMV 1140
Cdd:cd14614     4 HFAA--DLPVNRC---KNRYTNILPYDFSRVKLVSMHEeegsDYINANYIPG---YNSPqeYIATQGPLPETRNDFWKMV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1141 HEQKVSVIVMLVSEAEMEKQKVARYFPTERgQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSlkRSLVHLHFPTWPE 1220
Cdd:cd14614    76 LQQKSQIIVMLTQCNEKRRVKCDHYWPFTE-EPVAYGDITVEMLSEEEQPDWAIREFRVSYADEV--QDVMHFNYTAWPD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1221 LGLP--DSPGNLLRFIQEVHAHYLHQRplhTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHM 1298
Cdd:cd14614   153 HGVPtaNAAESILQFVQMVRQQAVKSK---GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIL-GLVSEMRSYRMSM 228

                         250
                  ....*....|..
gi 755531599 1299 LQEKLHLKFCHE 1310
Cdd:cd14614   229 VQTEEQYIFIHQ 240

PHA02742

protein tyrosine phosphatase; Provisional

1065-1309

5.07e-35

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 136.29 E-value: 5.07e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1065 QEHDARGRSIAIARCYSL-------KNRHQDVMPYDSNRVVL--RSGKDDYINASCVEGLSPYcPPLVATQAPLPGTAAD 1135
Cdd:PHA02742   30 EEHEHIMQEIVAFSCNESlelknmkKCRYPDAPCFDRNRVILkiEDGGDDFINASYVDGHNAK-GRFICTQAPLEETALD 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1136 FWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVALSSIRTTETHveRVLSLQFRDQSLKRSL--VHL 1213
Cdd:PHA02742  109 FWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNY--AVTNLCLTDTNTGASLdiKHF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1214 HFPTWPELGLPDSPGNLLRFIQEV-HAHYLHQRPL-------HTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPeLP 1285
Cdd:PHA02742  187 AYEDWPHGGLPRDPNKFLDFVLAVrEADLKADVDIkgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP-LL 265

                         250       260
                  ....*....|....*....|....
gi 755531599 1286 QLVRRMRQQRKHMLQEKLHLKFCH 1309
Cdd:PHA02742  266 SIVRDLRKQRHNCLSLPQQYIFCY 289

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

1088-1313

6.31e-35

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).

Pssm-ID: 350468 [Multi-domain] Cd Length: 229 Bit Score: 133.91 E-value: 6.31e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1088 DVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVA 1163
Cdd:cd14620     3 NILPYDHSRVILSQLDgipcSDYINASYIDGYKEK-NKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1164 RYFPtERGqPMVHGALSVALSSIRTTETHVERVLSLQFR-DQSLK--RSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAh 1240
Cdd:cd14620    82 QYWP-DQG-CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlPDGCKapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS- 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599 1241 ylhQRPLHT-PIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14620   159 ---VNPVHAgPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKV-DVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

1083-1316

1.04e-34

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350473 [Multi-domain] Cd Length: 282 Bit Score: 134.84 E-value: 1.04e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14625    50 KNRYANVIAYDHSRVILQPIEgimgSDYINANYIDGYRKQ-NAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTeRGQPmVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVH 1238
Cdd:cd14625   129 RIKCDQYWPS-RGTE-TYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599 1239 AhylHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14625   207 T---CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTV-DIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1058-1316

1.82e-34

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 134.48 E-value: 1.82e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1058 WRELQEAQEHDARGRSIAIArCYSLKNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTA 1133
Cdd:cd14627    32 FKRLANSKAHTSRFISANLP-CNKFKNRLVNIMPYETTRVCLQPIRgvegSDYINASFIDGYRQQ-KAYIATQGPLAETT 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1134 ADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHgaLSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHL 1213
Cdd:cd14627   110 EDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQY--FVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1214 HFPTWPELGLPDSPGNLLRFIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQ 1293
Cdd:cd14627   188 QFTDWPEQGVPKSGEGFIDFIGQVHKTK-EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRY-EGVVDIFQTVKMLRT 265

                         250       260
                  ....*....|....*....|...
gi 755531599 1294 QRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14627   266 QRPAMVQTEDEYQFCYQAALEYL 288

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1080-1302

6.31e-34

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 132.52 E-value: 6.31e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1080 YSLKNRHQDVMPYDSNRVvlrSGKDDYINASCVEGLSPYCppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 1159
Cdd:COG5599    42 GSPLNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR--YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1160 QKV--ARYFPTErGQpmvHGALSVALSSIRTT--ETHVE-RVLSLQFRDQSLK-RSLVHLHFPTWPELGLPDSPgNLLRF 1233
Cdd:COG5599   117 PKVkmPVYFRQD-GE---YGKYEVSSELTESIqlRDGIEaRTYVLTIKGTGQKkIEIPVLHVKNWPDHGAISAE-ALKNL 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599 1234 IQEVHAHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPE-LPQLVRRMRQQR-KHMLQEK 1302
Cdd:COG5599   192 ADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITLsVEEIVIDMRTSRnGGMVQTS 262

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

1083-1317

1.48e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.

Pssm-ID: 350454 [Multi-domain] Cd Length: 266 Bit Score: 131.16 E-value: 1.48e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGKD-----DYINASCVEG--LSPYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVS 1153
Cdd:cd14606    21 KNRYKNILPFDHSRVILQGRDSnipgsDYINANYVKNqlLGPDENAktYIASQGCLEATVNDFWQMAWQENSRVIVMTTR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1154 EAEMEKQKVARYFPTERGQPMVhGALSVALSSIRTTETHVERVLSLQFRDQS-LKRSLVHLHFPTWPELGLPDSPGNLLR 1232
Cdd:cd14606   101 EVEKGRNKCVPYWPEVGMQRAY-GPYSVTNCGEHDTTEYKLRTLQVSPLDNGeLIREIWHYQYLSWPDHGVPSEPGGVLS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1233 FIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIP---ELPQLVRRMRQQRKHMLQEKLHLKFCH 1309
Cdd:cd14606   180 FLDQINQRQ-ESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIST-KGLDcdiDIQKTIQMVRAQRSGMVQTEAQYKFIY 257


                  ....*...
gi 755531599 1310 EALVRHVE 1317
Cdd:cd14606   258 VAIAQFIE 265

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

1105-1318

2.45e-33

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.

Pssm-ID: 350449 [Multi-domain] Cd Length: 212 Bit Score: 128.52 E-value: 2.45e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1105 DYINASCVEGLSPYCPPL---VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPmVHGALSV 1181
Cdd:cd14601     1 DYINANYINMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1182 ALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQrplHTPIVVHCSSGVGR 1261
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGK---DEPVVVHCSAGIGR 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755531599 1262 TGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHMLQEKLHLKFCHEALVRHVEQ 1318
Cdd:cd14601   157 TGVLITMETAMCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

1106-1313

2.65e-33

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350506 [Multi-domain] Cd Length: 209 Bit Score: 128.56 E-value: 2.65e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPmvHGALSVAL 1183
Cdd:cd17668     1 YINANYVDG---YNKPkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE--YGNFLVTQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVERVLSLqfRDQSLK----------RSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQrplHTPIVV 1253
Cdd:cd17668    76 KSVQVLAYYTVRNFTL--RNTKIKkgsqkgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHA---VGPVVV 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1254 HCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd17668   151 HCSAGVGRTGTYIVLDSMLQQIQH-EGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1058-1316

2.77e-33

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 131.01 E-value: 2.77e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1058 WRELQEAQEHDARGRSIAIArCYSLKNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTA 1133
Cdd:cd14628    31 FKRLASSKAHTSRFISANLP-CNKFKNRLVNIMPYESTRVCLQPIRgvegSDYINASFIDGYRQQ-KAYIATQGPLAETT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1134 ADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHgaLSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHL 1213
Cdd:cd14628   109 EDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY--FVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1214 HFPTWPELGLPDSPGNLLRFIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQ 1293
Cdd:cd14628   187 QFTDWPEQGVPKSGEGFIDFIGQVHKTK-EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRY-EGVVDIFQTVKMLRT 264

                         250       260
                  ....*....|....*....|...
gi 755531599 1294 QRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14628   265 QRPAMVQTEDQYQFCYRAALEYL 287

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

1083-1316

3.78e-33

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 130.62 E-value: 3.78e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14624    50 KNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYRKQ-NAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTeRGQPmVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVH 1238
Cdd:cd14624   129 RVKCDQYWPS-RGTE-TYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599 1239 AhylHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14624   207 T---CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTV-DIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

1083-1313

6.47e-33

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350478 [Multi-domain] Cd Length: 237 Bit Score: 128.22 E-value: 6.47e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLR----SGKDDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 1156
Cdd:cd14630     6 KNRYGNIISYDHSRVRLQlldgDPHSDYINANYIDG---YHRPrhYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1157 MEKQKVARYFPTErgqPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQE 1236
Cdd:cd14630    83 VGRVKCVRYWPDD---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531599 1237 VhaHYLHQrPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14630   160 V--KFLNP-PDAGPIVVHCSAGAGRTGCFIAIDIMLDMAEN-EGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

1082-1312

2.11e-32

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 127.29 E-value: 2.11e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1082 LKNRHQDVMPYDSNRVVLRSGKDD-----YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 1156
Cdd:cd14613    27 RKNRYKTILPNPHSRVCLTSPDQDdplssYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1157 MeKQKVARYFPTERGqpmVHGALSVALSSIRTTETHVERVLSLqfRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQE 1236
Cdd:cd14613   107 M-NEKCTEYWPEEQV---TYEGIEITVKQVIHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599 1237 VHAHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGnGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:cd14613   181 VEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNE-GVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255

BRO1_Alix

cd09240

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This ...

2-153

2.89e-32

Protein-interacting, N-terminal, Bro1-like domain of mammalian Alix and related domains; This family contains the N-terminal, Bro1-like domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), also called apoptosis-linked gene-2 interacting protein 1 (AIP1). It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4, in the case of Alix. The Alix Bro1-like domain can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid and Rab5-specfic GAP (RabGAP5, also known as Rab-GAPLP). In addition to this Bro1-like domain, Alix has a middle V-shaped (V) domain. The Alix V-domain is a dimerization domain, and carries a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2.

Pssm-ID: 185763 Cd Length: 346 Bit Score: 129.72 E-value: 2.89e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    2 LDNRKSFLVARISAQVVDYYKEACRALENPDTASLLgriQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQ 81
Cdd:cd09240   203 RDKMKDAIIAKLAAQAADYYGDAFKQCQREDVRSLL---PKDWIPVLAGKQAYFHALAEYHQSLVAKAQKKFGEEIARLQ 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755531599   82 SALDKLNEAIKLAkGQPDTVQDAlrfaMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNP 153
Cdd:cd09240   280 HALELIKTAQSRA-GEYVDVKDF----AAKISRALTAAKKDNDFIYHDRVPDVKSLPPIGKAALAKPTPVNV 346

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

1106-1310

3.25e-32

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.

Pssm-ID: 350405 [Multi-domain] Cd Length: 201 Bit Score: 124.94 E-value: 3.25e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspYCPPL--VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSVAL 1183
Cdd:cd14557     1 YINASYIDG---FKEPRkyIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVERVLSL-QFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAhylHQRPLHTPIVVHCSSGVGRT 1262
Cdd:cd14557    78 NEEKICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA---FNNFFSGPIVVHCSAGVGRT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755531599 1263 GAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14557   155 GTYIGIDAMLEGLEA-EGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

1083-1309

1.50e-31

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 123.87 E-value: 1.50e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGKDD-----YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEm 1157
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNSNdslstYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1158 EKQKVARYFPTERGqpmVHGALSVALSSIRTTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPGNLLRFIQEV 1237
Cdd:cd14611    81 KNEKCVLYWPEKRG---IYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1238 HAHYLhQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCH 1309
Cdd:cd14611   156 EEDRL-ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKE-EGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1053-1316

1.91e-31

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 125.61 E-value: 1.91e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1053 ALDAIWRELQEAQEHDARGRSIAIArCYSLKNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAP 1128
Cdd:cd14629    27 AMELEFKLLANSKAHTSRFISANLP-CNKFKNRLVNIMPYELTRVCLQPIRgvegSDYINASFIDGYRQQ-KAYIATQGP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1129 LPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHgaLSVALSSIRTTETHVERVLSLQFRDQSLKR 1208
Cdd:cd14629   105 LAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY--FVVDPMAEYNMPQYILREFKVTDARDGQSR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1209 SLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLV 1288
Cdd:cd14629   183 TIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTK-EQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRY-EGVVDMFQTV 260

                         250       260
                  ....*....|....*....|....*...
gi 755531599 1289 RRMRQQRKHMLQEKLHLKFCHEALVRHV 1316
Cdd:cd14629   261 KTLRTQRPAMVQTEDQYQLCYRAALEYL 288

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

1106-1310

1.99e-31

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350399 [Multi-domain] Cd Length: 202 Bit Score: 122.71 E-value: 1.99e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPtERGQpMVHGALSVALSS 1185
Cdd:cd14551     1 YINASYIDGYQEK-NKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGC-WTYGNLRVRVED 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQ--FRDQSLK--RSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAhylhQRPLHT-PIVVHCSSGVG 1260
Cdd:cd14551    78 TVVLVDYTTRKFCIQkvNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS----ANPPRAgPIVVHCSAGVG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755531599 1261 RTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14551   154 RTGTFIVIDAMLDMMHAEGKV-DVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

1083-1315

3.63e-31

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).

Pssm-ID: 350469 [Multi-domain] Cd Length: 296 Bit Score: 125.14 E-value: 3.63e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 1158
Cdd:cd14621    55 KNRYVNILPYDHSRVHLTPVEgvpdSDYINASFINGYQEK-NKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERK 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYFPTErgQPMVHGALSVALSSIRTTETHVERVLSLQ----FRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFI 1234
Cdd:cd14621   134 ECKCAQYWPDQ--GCWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1235 QEVHAhylhQRPLHT-PIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14621   212 KKVKN----CNPQYAgAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKV-DVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                  ..
gi 755531599 1314 RH 1315
Cdd:cd14621   287 EH 288

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

1106-1313

1.45e-30

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 120.41 E-value: 1.45e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqpmVHGALSVAL 1183
Cdd:cd14555     1 YINANYIDG---YHRPnhYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGDIKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAhylHQRPLHTPIVVHCSSGVGRTG 1263
Cdd:cd14555    75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA---SNPPSAGPIVVHCSAGAGRTG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755531599 1264 AFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14555   152 CYIVIDIMLDMAER-EGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

1209-1312

2.52e-30

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 115.92 E-value: 2.52e-30

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   1209 SLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLV 1288
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNL-NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....
gi 755531599   1289 RRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRAL 103

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1209-1312

2.52e-30

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 115.92 E-value: 2.52e-30

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   1209 SLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYlHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLV 1288
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNL-NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTV 79

                            90       100
                    ....*....|....*....|....
gi 755531599   1289 RRMRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRAL 103

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

1106-1313

2.97e-30

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350480 [Multi-domain] Cd Length: 205 Bit Score: 119.39 E-value: 2.97e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqpmVHGALSVALSS 1185
Cdd:cd14632     1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD---TYGDIKITLLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 IRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAhylHQRPLHTPIVVHCSSGVGRTGAF 1265
Cdd:cd14632    77 TETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA---STPPDAGPVVVHCSAGAGRTGCY 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 755531599 1266 ALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14632   154 IVLDVMLDMAEC-EGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

BRO1_ScBro1_like

cd09242

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related ...

2-152

4.31e-30

Protein-interacting, N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins; This family contains the N-terminal, Bro1-like domain of Saccharomyces cerevisiae Bro1 and related proteins. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Saccharomyces cerevisiae Rim20 (also known as PalA), Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1 participates in endosomal trafficking. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: Snf7 in the case of Bro1. Snf7 binds to a conserved hydrophobic patch on the middle of the concave side of the Bro1 domain. RIM20, and some other members of the BRO1_Alix_like superfamily including Alix, also have a V-shaped (V) domain. In the case of Alix, the V-domain contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the superfamily. The Alix V-domain is also a dimerization domain. The C-terminal portion (V-domain and proline rich-region) of Bro1 interacts with Doa4, a protease that deubiquitinates integral membrane proteins sorted into the lumenal vesicles of late-endosomal multivesicular bodies. It interacts with a YPxL motif in the Doa4 catalytic domain to stimulate its deubiquitination activity.

Pssm-ID: 185765 Cd Length: 348 Bit Score: 123.16 E-value: 4.31e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    2 LDNRKSFLVARISAQVVDYYKEACRALENPDTaSLLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQ 81
Cdd:cd09242   190 DAQKKASLISKLASATANLYESCVEFLKEIQE-KGISYGDPKWISLVQCKAHYYKSLAAYYHALALEAAGKYGEAIAYLT 268

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599   82 SALDKLNEAIKLAKGQPDTVQDA-------LRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVN 152
Cdd:cd09242   269 QAESILKEANPQKLSLKASAGDAayalnddFKGQKDTVEEKLKELEKDNDFIYHDIVPSEVTLPSIKPLDAAKPIPIE 346

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

1106-1310

6.11e-30

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350404 [Multi-domain] Cd Length: 201 Bit Score: 118.28 E-value: 6.11e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLvSEAEMEKQKVARYFPTERGQpmVHGALSVAL 1183
Cdd:cd14556     1 YINAALLDS---YKQPaaFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSG--TYGPIQVEF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVERVLSLQ--FRDQSLKRSLVHLHFPTWPELGL-PDSPGNLLRFIQEVHAhyLHQRPLHTPIVVHCSSGVG 1260
Cdd:cd14556    75 VSTTIDEDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRDtPPSKRALLKLLSEVEK--WQEQSGEGPIVVHCLNGVG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755531599 1261 RTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14556   153 RSGVFCAISSVCERIKVENVV-DVFQAVKTLRNHRPNMVETEEQYKFCYD 201

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

1082-1313

2.18e-29

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350481 [Multi-domain] Cd Length: 273 Bit Score: 119.38 E-value: 2.18e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1082 LKNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEA 1155
Cdd:cd14633    42 MKNRYGNIIAYDHSRVRLQPiegeTSSDYINGNYIDG---YHRPnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1156 EMEKQKVARYFPTErgqPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQ 1235
Cdd:cd14633   119 EVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599 1236 EVHAhylHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14633   196 QVKS---KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER-EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

1096-1313

1.52e-27

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.

Pssm-ID: 350479 [Multi-domain] Cd Length: 218 Bit Score: 112.04 E-value: 1.52e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1096 RVVLRSGKDD----YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTE 1169
Cdd:cd14631     1 RVILQPVEDDpssdYINANYIDG---YQRPshYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1170 rgqPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHahyLHQRPLHT 1249
Cdd:cd14631    78 ---TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---LSNPPSAG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599 1250 PIVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd14631   152 PIVVHCSAGAGRTGCYIVIDIMLDMAER-EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

PHA02746

protein tyrosine phosphatase; Provisional

1081-1312

4.24e-26

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 110.89 E-value: 4.24e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1081 SLKNRHQDVMPYDSNRVVLRS---------GKDD--------------YINASCVEGLSPyCPPLVATQAPLPGTAADFW 1137
Cdd:PHA02746   52 LKKNRFHDIPCWDHSRVVINAheslkmfdvGDSDgkkievtsednaenYIHANFVDGFKE-ANKFICAQGPKEDTSEDFF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1138 LMVHEQKVSVIVMLvSEAEMEKQKVARYFPTERGQPMVHGALSVALSSIRTTETHVERVLSLQFRDQSLKRSLVHLHFPT 1217
Cdd:PHA02746  131 KLISEHESQVIVSL-TDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPD 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1218 WPELGLPDSPGNLLRFIQEVHAHYL-------HQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRR 1290
Cdd:PHA02746  210 WPDNGIPTGMAEFLELINKVNEEQAelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV-CLGEIVLK 288

                         250       260
                  ....*....|....*....|..
gi 755531599 1291 MRQQRKHMLQEKLHLKFCHEAL 1312
Cdd:PHA02746  289 IRKQRHSSVFLPEQYAFCYKAL 310

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

1106-1314

5.35e-26

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.

Pssm-ID: 350446 [Multi-domain] Cd Length: 220 Bit Score: 107.75 E-value: 5.35e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVE-GLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPT--ERGQPMVHGALSVA 1182
Cdd:cd14598     1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1183 L------SSIRTTETHVERVLSLQfrdqslKRSLVHLHFPTWPELGLPDSPGNLLRFIQEVHAHYLHQ------RPLHTP 1250
Cdd:cd14598    81 TrfrtdsGCYATTGLKIKHLLTGQ------ERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTnstidpKSPNPP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599 1251 IVVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHEALVR 1314
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEH-NEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217

PHA02747

protein tyrosine phosphatase; Provisional

1083-1295

1.18e-25

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 109.32 E-value: 1.18e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1083 KNRHQDVMPYDSNRVVLRSG---KDDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLV-SEAEME 1158
Cdd:PHA02747   54 KNRYWDIPCWDHNRVILDSGggsTSDYIHANWIDGFEDD-KKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpTKGTNG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1159 KQKVARYF-PTERGQPMVHG------ALSVALSSIRTTethvervlsLQFRDQSLK--RSLVHLHFPTWPELGLPDSPGN 1229
Cdd:PHA02747  133 EEKCYQYWcLNEDGNIDMEDfrietlKTSVRAKYILTL---------IEITDKILKdsRKISHFQCSEWFEDETPSDHPD 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755531599 1230 LLRFI-------QEVHAHYLHQRPLHTPIVVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQR 1295
Cdd:PHA02747  204 FIKFIkiidinrKKSGKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI-CLAKTAEKIREQR 275

BRO1_Alix_like_1

cd09246

Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the ...

2-153

8.50e-25

Protein-interacting, N-terminal, Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily; This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to this Bro1-like domain, Alix, Bro1, Rim20, HD_PTP, and proteins belonging to this uncharacterized family, also have a V-shaped (V) domain. The Alix V-domain is a dimerization domain, and contains a binding site for the retroviral late assembly (L) domain YPXnL motif, which is partially conserved in the BRO1_Alix_like superfamily. Many members of this superfamily also have a proline-rich region (PRR), a protein interaction domain.

Pssm-ID: 185769 Cd Length: 353 Bit Score: 107.87 E-value: 8.50e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    2 LDNRKSFLVARISAQVVDYYKEACRALenpDTASLLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQ 81
Cdd:cd09246   195 ADGKSPAVCSKLAKQARSYYEEALEAL---DSPPLKGHFDKSWVAHVQLKAAYFRAEALYRAAKDLHEKEDIGEEIARLR 271

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755531599   82 SALDKLNEAIKLAKGQP-DTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNP 153
Cdd:cd09246   272 AASDALAEARKQAKGVNgDELIEAVSELEQVINELLERAEKENDCVYLDRVPAPSDLPPLGAASMVKPAAPPA 344

V_ScBro1_like

cd09237

Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family ...

169-504

1.46e-23

Protein-interacting V-domain of Saccharomyces cerevisiae Bro1 and related domains; This family contains the V-shaped (V) domain of Saccharomyces cerevisiae Bro1, and related domains. It belongs to the V_Alix_like superfamily which also includes the V-domain of Saccharomyces cerevisiae Rim20 (also known as PalA), mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Bro1 interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in endosomal trafficking. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Bro1 also has an N-terminal Bro1-like domain, which binds Snf7, a component of the ESCRT-III complex, and a C-terminal proline-rich region (PRR). The C-terminal portion (V-domain and PRR) of S. cerevisiae Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes. It interacts with a YPxL motif in the Doa4s catalytic domain to stimulate its deubiquitination activity.

Pssm-ID: 185750 [Multi-domain] Cd Length: 356 Bit Score: 104.30 E-value: 1.46e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLdPETVDNLDAYNHIPPQLMEkcAALSVRPDTVKNLVQS 248
Cdd:cd09237     1 PLAVHEKESLYSEEKAKLLRAEVERVEVANEEYASFLEYLNL-PKLLVDLKERFEGENELME--IVSGLKSSSVDSQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  249 MqvlsgvFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPGPSVAKAELAEVRREWAKYMEVHEKASFTNSELHRAM 328
Cdd:cd09237    78 L------RPQSASWVNEIDSSYNDLDEEMKEIEKMRKKILAKWTQSPSSSLTASLREDLVKLKKSLVEASASDEKLFSLV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  329 NLHVGNLRLLSGPLDQVRAAL-------PTPAL-----TPEDKAVLQNLKRI---LAKVQEMRDQRVSLEQQLRELIQKD 393
Cdd:cd09237   152 DPVKEDIALLLNGGSLWEELFgfsssgsPEPSLldlddSQNEQTVLKQIKQLeelLEDLNLIKEERQRVLKDLKQKIHND 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  394 DITASLVttDHSEMKK-----LFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEA--NV-QYAAVRRVLSELD------QK 459
Cdd:cd09237   232 DISDILI--LNSKSKSeiekqLFPEELEKFKPLQNRLEATIFKQSSLINELKIEldKLfKLPGVKEKQSKEKskqklrKE 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 755531599  460 WNSTLQTLVASYEAYEDLMKKsqeGKDFYADLESKVATLLERAQS 504
Cdd:cd09237   310 FFEKLKKAYNSFKKFSAGLPK---GLEFYDDLLKMAKDLAKNVQA 351

V_Alix

cd09235

Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction ...

169-506

6.81e-22

Middle V-domain of mammalian Alix and related domains are dimerization and protein interaction modules; This family contains the middle V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X) and related domains. It belongs to the V_Alix_like superfamily which includes the V-domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), is part of the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in membrane remodeling processes, including the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), the abscission reactions of mammalian cell division, and in apoptosis. The Alix V-domain is a dimerization domain, and contains a binding site, partially conserved in the V_Alix_like superfamily, for the retroviral late assembly (L) domain YPXnL motif. In addition to the V-domain, Alix also has an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex, in particular CHMP4. The Bro1-like domain of Alix can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Alix also has a C-terminal proline-rich region (PRR) that binds multiple partners including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1), and the apoptotic protein ALG-2.

Pssm-ID: 185748 Cd Length: 339 Bit Score: 98.89 E-value: 6.81e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLdPETVDNLDAyNHIPPQLMEKCAAlsVRPDTVKNLVQS 248
Cdd:cd09235     1 PVSVHQALAAYNQRKAELVNREIGKLREATQLLNGVLASLNL-PAAIEDVSG-DTVPQSLLEKSRT--VIEKGGIQTIDQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  249 MqvlsgvFTDVEASLKDIRDLLEE------------DELQEQ---KLQETlgqagagpgPSvakAELAEV-RREWAKYME 312
Cdd:cd09235    77 L------IKELPELLQRNREILDEalrmldeeeasdNQLRAQfkeRWTRT---------PS---NKLTKPlRAEGSKYRT 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  313 VHEKASFTNSELHRAMNLHVGNLRLLSGPLDQVRAALPT--PALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLREli 390
Cdd:cd09235   139 ILDNAVQADKIVREKYESHREGIELLSKPEEELANAIPSasPAKTLQGSEAVQELRQLMEQVETIKAEREVIESELKS-- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  391 qkdditaslVTTDhseMKKLF-----------EEQL------KKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVL 453
Cdd:cd09235   217 ---------ATFD---MKSKFlsalaqdgainEEAIsveeldRVYGPLQKQVQESLSRQESLLANIQVAHQEFSKEKQSN 284

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755531599  454 SELDQKwNSTLQTLVASYEAYEDLMKKSQEGKDFYADLeskvATLLERAQSIC 506
Cdd:cd09235   285 SGANER-EEVLKDLAAAYDAFMELTANLKEGTKFYNDL----TEILVKFQNKC 332

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

1106-1281

1.84e-18

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 85.45 E-value: 1.84e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspY--CPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVarYFPTErGQPMVHGALSVAL 1183
Cdd:cd14550     1 YINASYLQG---YrrSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTK-EKPLECETFKVTL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSirTTETHVERVLSLQFRD---QSLKRSLV----HLHFPTWPElglPDSPG-NLLRFIQEVHAHYLHQrplHTPIVVHC 1255
Cdd:cd14550    75 SG--EDHSCLSNEIRLIVRDfilESTQDDYVlevrQFQCPSWPN---PCSPIhTVFELINTVQEWAQQR---DGPIVVHD 146

                         170       180
                  ....*....|....*....|....*.
gi 755531599 1256 SSGVGRTGAFALLYAAVQEVEAGNGI 1281
Cdd:cd14550   147 RYGGVQAATFCALTTLHQQLEHESSV 172

V_AnPalA_UmRIM20_like

cd09236

Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and ...

169-513

1.01e-17

Protein-interacting V-domains of Aspergillus nidulans PalA/RIM20, Ustilago maydis RIM20, and related proteins; This family belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Aspergillus nidulas PalA/RIM20 and Ustilago maydis RIM20, like Saccharomyces cerevisiae Rim20, participate in the response to the external pH via the Pal/Rim101 pathway; however, Saccharomyces cerevisiae Rim20 does not belong to this family. This pathway is a signaling cascade resulting in the activation of the transcription factor PacC/Rim101. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. Aspergillus nidulas PalA binds a nonviral YPXnL motif (tandem YPXL/I motifs within PacC). The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_like superfamily also have an N-terminal Bro1-like domain, which has been shown to bind CHMP4/Snf7, a component of the ESCRT-III complex.

Pssm-ID: 185749 [Multi-domain] Cd Length: 353 Bit Score: 86.64 E-value: 1.01e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREMLA-KIEDKNEVLDQFMDSMQLdPETVDNLDAYNHIPPQLMEKcaALSVR----PDTVK 243
Cdd:cd09236     1 PFGVHLAISIYDDRKDRLVNESIIdELEELTNRAHSTLRSLNL-PGSLQALEKPLGLPPSLLRH--AEEIRqedgLERIR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  244 NLVQSMQVLSGvfTDvEASLKDIRDLLEEDELQEQKLQETLGQAG-AGPGPSVAKAELaevrreWAKYMEVH---EKASF 319
Cdd:cd09236    78 ASLDDVARLAA--SD-RAILEEAMDILDDEASEDESLRRKFGTDRwTRPDSHEANPKL------YTQAAEYEgylKQAGA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  320 TNSELHRAMNLHVGNLRLLSGPLDQVRAALPT---PALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDIT 396
Cdd:cd09236   149 SDELVRRKLDEWEDLIQILTGDERDLENFVPSsrrPSIPPELERHVRALRVSLEELDRLESRRRRKVERARTKARADDIR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  397 ASL---------------VTTDHSEmkKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYaAVRRVLSELDQKWN 461
Cdd:cd09236   229 PEIlreaarlereypateVAPAHFE--DLFDKRLAKYDKDLDAVSEEAQEQEEILQQIEVANKAF-LQSRKGDPATKERE 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755531599  462 STLQTLVASYEAYEDLMKKSQEGKDFYADLeskvATLLERAQSICRAQEAAR 513
Cdd:cd09236   306 RALQSLDLAYFKYKEIVSNLDEGRKFYNDL----AKILSQFRDACKAWVYER 353

V_Alix_like_1

cd09238

Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This ...

169-503

2.91e-17

Protein-interacting V-domain of an uncharacterized family of the V_Alix_like superfamily; This domain family is comprised of uncharacterized plant proteins. It belongs to the V_Alix_like superfamily which includes the V-shaped (V) domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X), (His-Domain) type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), and related domains. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. The mammalian Alix V-domain (belonging to a different family) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to this V-domain, members of the V_Alix_Rim20_Bro1_like superfamily also have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members of the V_Alix_like superfamily also have a proline-rich region (PRR).

Pssm-ID: 185751 Cd Length: 339 Bit Score: 84.83 E-value: 2.91e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  169 PMAAHEASSLYSEEKAKLLREmlakiedKNEVLDQFMDSMQLD------PETVDNLDAYnhippqlmekcAALSVrPDTV 242
Cdd:cd09238     1 PESSAKALSKYTEMVDELIRT-------EADRLAAASDEARVAlremelPETLIALDGG-----------ASLPG-DLGL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  243 KNLVQSMQVLSGVfTDVEASLKDIRDLLEEDELQEQKLQETL--------------GQAGAGPGPSVAKAELAEVRREWA 308
Cdd:cd09238    62 DEEVEAVQISGGL-AALEGELPRLRELRRVCTELLAAAQESLeaeatedsaartqyGTAWTRPPSATLTKNLWERLNRFR 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  309 KYMEvheKASFTNSELHRAMNLHVGNLRLLSGPldQVRAALPT---PALT--PEDKAVLQNLKRILAKVQEMRDQRVSLE 383
Cdd:cd09238   141 VNLE---QAGDSDESLRRRIEDAMDGMLILDDE--PAAAAAPTlraPMLStdEDDASIVGTLRSNLEELEALGNERAGIE 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  384 QQLRELIQKDDITASLVTTDhSEMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVlseldQKWNST 463
Cdd:cd09238   216 DMMKALKRNDNILAKVMATT-GSYDALFKEELKKYDSVREAVSKNISSQDDLLSRLRALNEKFSQIFDV-----EGWRAA 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 755531599  464 LQT----LVASYEAYEDLMKKSQEGKDFYADLESKVATLLERAQ 503
Cdd:cd09238   290 TEShatqIRAAVAKYRELREGMEEGLRFYSGFQEAVRRLKQECE 333

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

1106-1310

2.70e-16

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350482 [Multi-domain] Cd Length: 206 Bit Score: 79.29 E-value: 2.70e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEglSPYCPP-LVATQAPLPGTAADFWLMVHEQKVSVIVMLvseAEMEK-QKVARYFPTErgQPMVHGALSVAL 1183
Cdd:cd14634     1 YINAALMD--SHKQPAaFIVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDAaQLCMQYWPEK--TSCCYGPIQVEF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1184 SSIRTTETHVERVLSL--QFRDQSLKRSLVHLHFPTWPEL-GLPDSPGNLLRFIQEVHAHYLHQRPLHTPIVVHCSSGVG 1260
Cdd:cd14634    74 VSADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755531599 1261 RTGAFALLYAAVQEVEAGNgIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14634   154 RSGTFCAICSVCEMIQQQN-IIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

1106-1313

1.35e-11

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).

Pssm-ID: 350508 [Multi-domain] Cd Length: 205 Bit Score: 65.47 E-value: 1.35e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVArYFPTeRGQPMVHGALSVAL-S 1184
Cdd:cd17670     1 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPS-REESMNCEAFTVTLiS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1185 SIRTTETHVERVLSLQFRDQSLKRSLV----HLHFPTWPElglPDSP-GNLLRFIQEVHAHYLHQrplHTPIVVHCSSGV 1259
Cdd:cd17670    78 KDRLCLSNEEQIIIHDFILEATQDDYVlevrHFQCPKWPN---PDAPiSSTFELINVIKEEALTR---DGPTIVHDEFGA 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755531599 1260 GRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd17670   152 VSAGTLCALTTLSQQLENENAV-DVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

1106-1310

1.77e-11

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 65.09 E-value: 1.77e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVML--VSEAEMEKQkvarYFPtERGQPMvHGALSV 1181
Cdd:cd14635     1 YINAALMDS---YKQPsaFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLndVDPAQLCPQ----YWP-ENGVHR-HGPIQV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1182 ALSSIRTTETHVERVLSL--QFRDQSLKRSLVHLHFPTWPEL-GLPDSPGNLLRFIQEVHAHYLHQRPLHTPIVVHCSSG 1258
Cdd:cd14635    72 EFVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1259 VGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14635   152 GGRSGTFCAISIVCEMLRHQRAV-DVFHAVKTLRNNKPNMVDLLDQYKFCYE 202

R-PTP-Z-2

cd17669

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

1106-1313

2.65e-11

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).

Pssm-ID: 350507 [Multi-domain] Cd Length: 204 Bit Score: 64.63 E-value: 2.65e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVArYFPTeRGQPMVHGALSVALSS 1185
Cdd:cd17669     1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPN-KDEPINCETFKVTLIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1186 irttETHV-----ERVLSLQFRDQSLKRSLV----HLHFPTWPElglPDSPGN----LLRFIQEVHAHYlhqrplHTPIV 1252
Cdd:cd17669    78 ----EEHKclsneEKLIIQDFILEATQDDYVlevrHFQCPKWPN---PDSPISktfeLISIIKEEAANR------DGPMI 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599 1253 VHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLKFCHEALV 1313
Cdd:cd17669   145 VHDEHGGVTAGTFCALTTLMHQLEKENSV-DVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

1123-1306

1.11e-10

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.

Pssm-ID: 350407 [Multi-domain] Cd Length: 227 Bit Score: 63.19 E-value: 1.11e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1123 VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFpterGQPMVHGALSValSSIRTTETHVERVL----- 1197
Cdd:cd14559    32 IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYF----RQSGTYGSVTV--KSKKTGKDELVDGLkadmy 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1198 SLQFRDQSLKRSLVHLHFPTWPELGLPDSPG-------------NLLRFIQEVHAHYLHQRPLHTPiVVHCSSGVGRTGA 1264
Cdd:cd14559   106 NLKITDGNKTITIPVVHVTNWPDHTAISSEGlkeladlvnksaeEKRNFYKSKGSSAINDKNKLLP-VIHCRAGVGRTGQ 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 755531599 1265 FAllyAAVQEVEAGNGIpELPQLVRRMRQQRK-HMLQEKLHLK 1306
Cdd:cd14559   185 LA---AAMELNKSPNNL-SVEDIVSDMRTSRNgKMVQKDEQLD 223

PHA03247

large tegument protein UL36; Provisional

540-946

1.22e-10

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.89 E-value: 1.22e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  540 REEGEAVEAGDTPEELR--SLPPDMMVGPRLPDPflgttAPLHFSPGPFPSSTGPAThylsgPLPPGTYSGptqlmqpRA 617
Cdd:PHA03247 2668 RRLGRAAQASSPPQRPRrrAARPTVGSLTSLADP-----PPPPPTPEPAPHALVSAT-----PLPPGPAAA-------RQ 2730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  618 AVPMAPATVLYPAPAYTSELGLVPRSSPQHGIVSSPYAGVGPPQPvvglPSAPPPQLSGPELAmTVRPATTTVDSVQAPi 697
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP----AAGPPRRLTRPAVA-SLSESRESLPSPWDP- 2804

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  698 SSHTAPRPNPTPALPQPCFPV-PQPVPQSVPQPQPLpvpytysigtKQPLPAPYTYSIGTKQHLTGPL---PQHQFPPGI 773
Cdd:PHA03247 2805 ADPPAAVLAPAAALPPAASPAgPLPPPTSAQPTAPP----------PPPGPPPPSLPLGGSVAPGGDVrrrPPSRSPAAK 2874

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  774 PTGFPVPRTGPQAQAQPQPQPQPQPQPQPQPQPQPQpqsqsqpqpqpqpqpqrpafgPQPTQQPLPFQHPHLFPSQAPGI 853
Cdd:PHA03247 2875 PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQ---------------------PQAPPPPQPQPQPPPPPQPQPPP 2933

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  854 lppppptpyhfTPQPGVLGQPPPTLHTQLYPGPSQDPLPPHSGAlpfpspgpphphptLAYGPAPSPRPLGPQATPVSir 933
Cdd:PHA03247 2934 -----------PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA--------------LVPGRVAVPRFRVPQPAPSR-- 2986

                         410
                  ....*....|...
gi 755531599  934 gPPPASqPTPSPH 946
Cdd:PHA03247 2987 -EAPAS-STPPLT 2997

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

1106-1310

1.64e-09

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350485 [Multi-domain] Cd Length: 207 Bit Score: 59.54 E-value: 1.64e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLvseAEMEKQKVA----RYFPTERGQPmvHGALSV 1181
Cdd:cd14637     1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML---NQLNQSNSAwpclQYWPEPGLQQ--YGPMEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1182 ALSSIRTTETHVERVLSLQ--FRDQSLKRSLVHLHFPTW-PELGLPDSPGNLLRFIQEVHAHYLHQRPLHTpiVVHCSSG 1258
Cdd:cd14637    75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRT--VVHCLNG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755531599 1259 VGRTGAFALLyAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14637   153 GGRSGTYCAS-AMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYE 203

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

1106-1310

2.34e-09

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.

Pssm-ID: 350484 [Multi-domain] Cd Length: 206 Bit Score: 58.88 E-value: 2.34e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1106 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLvSEAEMeKQKVARYFPTE---RGQPMVHGALS 1180
Cdd:cd14636     1 YINAALMDS---YRQPaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEVDL-AQGCPQYWPEEgmlRYGPIQVECMS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1181 VALSSirttethveRVLSLQFRDQSLKRSLV-HLHFPTWPELG------LPDSPGNLLRFIQEVHAHYLHQRPLHTPIVV 1253
Cdd:cd14636    76 CSMDC---------DVISRIFRICNLTRPQEgYLMVQQFQYLGwashreVPGSKRSFLKLILQVEKWQEECDEGEGRTII 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755531599 1254 HCSSGVGRTGAFALLYAAVQEVEAGNgIPELPQLVRRMRQQRKHMLQEKLHLKFCHE 1310
Cdd:cd14636   147 HCLNGGGRSGMFCAISIVCEMIKRQN-VVDVFHAVKTLRNSKPNMVETPEQYRFCYD 202

BRO1_Alix_like_2

cd09247

Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like ...

9-153

4.76e-08

Protein-interacting Bro1-like domain of an Uncharacterized family of the BRO1_Alix_like superfamily; This domain family is comprised of uncharacterized proteins. It belongs to the BRO1_Alix_like superfamily which includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20 and Rim23 interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP and Bro1 function in endosomal trafficking, with HD-PTP having additional functions in cell migration. Rim20 and Rim23 play roles in the response to the external pH via the Rim101 pathway. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. These domains bind components of the ESCRT-III complex: CHMP4 (in the case of Alix, Brox and HD-PTP) and Snf7 (in the case of yeast Bro1 and Rim20). The Bro1-like domains of Alix, HD-PTP, Brox, and Rhophilin can bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.

Pssm-ID: 185770 Cd Length: 346 Bit Score: 56.63 E-value: 4.76e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599    9 LVARISAQVVDYYKEACRALENpDTASLLGRIQKDWKKLVQMKIYYfAAVAHLHMGKQAEEQQKFGERVAYFQSALDKLN 88
Cdd:cd09247   207 LLAKLHYGATQFLEEAKNVLRS-LATDLKDLDPRFLRFISSCIALH-EARSQLYLARRLKEAGHIGVAVGVLREALRNLK 284

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755531599   89 EAIKLAKGQPDTVQDALRFAMDVIGGKYnsaKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNP 153
Cdd:cd09247   285 KKLPGSDISSPVIFRDERAEVATLLQKY---EKENEVIYFEKVPDIDELPLPEGKVIVKPVPYKP 346

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

1193-1292

5.61e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 53.44 E-value: 5.61e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1193 VERVLSLQFRDQSL-----KRSLVHLHFPtWPELGLPDsPGNLLRFIQEVHAHylhqRPLHTPIVVHCSSGVGRTGAFAL 1267
Cdd:COG2453    26 IDAVVSLTEEEELLlglleEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDEA----LREGKKVLVHCRGGIGRTGTVAA 99

                          90       100
                  ....*....|....*....|....*
gi 755531599 1268 LYAAVQEVEAGNGIpelpQLVRRMR 1292
Cdd:COG2453   100 AYLVLLGLSAEEAL----ARVRAAR 120

PHA03247

large tegument protein UL36; Provisional

531-782

7.10e-07

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 7.10e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  531 TAPKPLLSRREEGEAVEAGDTPEELRSLPPDMMVGPRLP-------DPFLGTTAPLHFSP-----GPFPSSTGPATHYL- 597
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggparpaRPPTTAGPPAPAPPaapaaGPPRRLTRPAVASLs 2792

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  598 ----SGPLPPGTYSGPTQLMQPRAAVPMA---------PATVLYPAPAYTSelGLVPRSSPQHGIVS--SPYAGVGPPQP 662
Cdd:PHA03247 2793 esreSLPSPWDPADPPAAVLAPAAALPPAaspagplppPTSAQPTAPPPPP--GPPPPSLPLGGSVApgGDVRRRPPSRS 2870

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  663 VVGLPSAP--PP--QLSGPELAMTVRPATTTVDSVQAPISSHTAPRPNPTPALPQPCFPVPQPVPQsvpqpqplpvpyty 738
Cdd:PHA03247 2871 PAAKPAAParPPvrRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP-------------- 2936

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 755531599  739 siGTKQPLPAPYTYSIGTKQHlTGPLPQHQFPPGIPTGFPVPRT 782
Cdd:PHA03247 2937 --PRPQPPLAPTTDPAGAGEP-SGAVPQPWLGALVPGRVAVPRF 2977

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

347-665

1.45e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.45e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  347 AALPTPAL-TPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSEMKKLfEEQL--------KK 417
Cdd:COG3883     6 LAAPTPAFaDPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-QAEIaeaeaeieER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  418 YDQLK-------------VYLEQNLAAQD--------NVLRALTEANV----QYAAVRRVLSELDQKWNSTLQTLVASYE 472
Cdd:COG3883    85 REELGeraralyrsggsvSYLDVLLGSESfsdfldrlSALSKIADADAdlleELKADKAELEAKKAELEAKLAELEALKA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  473 AYE----DLMKKSQEGKDFYADLESKVATLLERAQSICRAQEAARQQLLDRELKKKAPPPRPTAPKPLLSRREEGEAVEA 548
Cdd:COG3883   165 ELEaakaELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  549 GDTPEELRSLPPDMMVGPRLPDPFLGTTAPLHFSPGPFPSSTGPATHYLSGPLPPGTYSGPTQLMQPRAAVPMAPATVLY 628
Cdd:COG3883   245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVG 324

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 755531599  629 PAPAYTSELGLVPRSSPQHGIVSSPYAGVGPPQPVVG 665
Cdd:COG3883   325 GASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSG 361

BRO1_Rhophilin

cd09244

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; ...

10-164

2.72e-06

Protein-interacting Bro1-like domain of RhoA-binding protein Rhophilin and related domains; This family contains the Bro1-like domain of RhoA-binding proteins, Rhophilin-1 and -2, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Brox, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Rhophilin-1 and -2 bind both GDP- and GTP-bound RhoA. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. In addition to this Bro1-like domain, Rhophilin-1 and -2, contain an N-terminal Rho-binding domain and a C-terminal PDZ (PS.D.-95, Disc-large, ZO-1) domain. Their PDZ domains have limited homology. Rhophilin-1 and -2 have different activities. The Drosophila knockout of Rhophilin-1 is embryonic lethal, suggesting an essential role in embryonic development. Roles of Rhophilin-2 may include limiting stress fiber formation or increasing the turnover of F-actin in the absence of high levels of RhoA signaling activity. The isolated Bro1-like domain of Rhophilin-1 binds human immunodeficiency virus type 1 (HIV-1) nucleocapsid. This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix _like superfamily.

Pssm-ID: 185767 Cd Length: 350 Bit Score: 51.19 E-value: 2.72e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   10 VARISAQVVDYYKEACRALENPDTASLlgrIQKDWKKLVQMKIYYFAAVAHLH--MGKQAEEQQKFGErvAYFQSALDKL 87
Cdd:cd09244   200 LAQEAAQVSDCYSEVHKLMNQEPVKDY---IPYSWISLVEVKSEHYKALAHYYaaMGLLLEERRLLGK--AHLKEALLLH 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   88 NEAIKLAK-----GQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPaldtlqPVKGAPLVKPLPVNPTDPAVTGPD 162
Cdd:cd09244   275 EEALRLHRmcrflRNVDSLQEVLKEAHDRSLNKYSSLEEEDDFSDALDAP------DIQAKTKQQLEIIPPDFTQVKVKD 348


                  ..
gi 755531599  163 IF 164
Cdd:cd09244   349 LF 350

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

1231-1310

5.51e-06

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 46.96 E-value: 5.51e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599 1231 LRFIQEVHAHYlhqrplhTPIVVHCSSGVGRTGAFALLYAavqeVEAGNGIPElpQLVRRMRQQRKHMLQEKL-HLKFCH 1309
Cdd:cd14494    46 LEVLDQAEKPG-------EPVLVHCKAGVGRTGTLVACYL----VLLGGMSAE--EAVRIVRLIRPGGIPQTIeQLDFLI 112


                  .
gi 755531599 1310 E 1310
Cdd:cd14494   113 K 113

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

259-522

5.85e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 5.85e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  259 VEASLKDIRDLLEEDELQEQKLQETLGQAGAgpgpsvAKAELAEVRREwakYMEVHEKASFTNSELHRAMNLhvgnlrll 338
Cdd:COG4372    33 LRKALFELDKLQEELEQLREELEQAREELEQ------LEEELEQARSE---LEQLEEELEELNEQLQAAQAE-------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  339 sgpLDQVRAALptpaltpedKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSEMKKLfEEQLKky 418
Cdd:COG4372    96 ---LAQAQEEL---------ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL-EEQLE-- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  419 dqlkvYLEQNLAAQDNVLRALTEANVQyAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYADLESKVATL 498
Cdd:COG4372   161 -----SLQEELAALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234

                         250       260
                  ....*....|....*....|....
gi 755531599  499 LERAQSICRAQEAARQQLLDRELK 522
Cdd:COG4372   235 LSALLDALELEEDKEELLEEVILK 258

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

330-523

1.22e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.22e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  330 LHVGNLRLLSGPL-----DQVRAALPtpaltpEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELiqkdditaslvttdH 404
Cdd:COG4372    13 LSLFGLRPKTGILiaalsEQLRKALF------ELDKLQEELEQLREELEQAREELEQLEEELEQA--------------R 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  405 SEMKKLfEEQLKKYDQLkvyLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEG 484
Cdd:COG4372    73 SELEQL-EEELEELNEQ---LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 755531599  485 KDFYADLESKVATLLERAQSICRAQEAARQQLLDRELKK 523
Cdd:COG4372   149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187

PRK03918

DNA double-strand break repair ATPase Rad50;

252-523

3.04e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 3.04e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  252 LSGVFTDVEASLKDIRDLLEEDELQEQKLQEtlgqagagpgpsvAKAELAEVRREWAKYMEvhekasftnselhramnlh 331
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKRTENIEELIKE-------------KEKELEEVLREINEISS------------------- 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  332 vgNLRLLSGPLDQVRAALPT--------PALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDditaslvttd 403
Cdd:PRK03918  215 --ELPELREELEKLEKEVKEleelkeeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV---------- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  404 hSEMKKLfEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKwnstlqtlvasYEAYEDLMKKSQE 483
Cdd:PRK03918  283 -KELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKE 349

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 755531599  484 GKDFYADLESKVaTLLERAQSICRAQEAARQQLLDRELKK 523
Cdd:PRK03918  350 LEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEK 388

mukB

PRK04863

chromosome partition protein MukB;

263-523

4.13e-05

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 4.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  263 LKDIRDLLEEDELQEQKLQETLGQAgagpgpsVAKA-ELAEVRREWAKYMEVHEKAsftNSELHRAMNLhvgnLRLLSGP 341
Cdd:PRK04863  423 LERAKQLCGLPDLTADNAEDWLEEF-------QAKEqEATEELLSLEQKLSVAQAA---HSQFEQAYQL----VRKIAGE 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  342 LDQVRA---ALPTPALTPEDKAVLQNLKRILAKVQEMRdQRVSLEQQLRELIQkdditaslvttdhsEMKKLFEEQLKKY 418
Cdd:PRK04863  489 VSRSEAwdvARELLRRLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLA--------------EFCKRLGKNLDDE 553

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  419 DQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWnSTLQTLVASYEAYEDLMKKSQE--GKDFY--ADLESK 494
Cdd:PRK04863  554 DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI-QRLAARAPAWLAAQDALARLREqsGEEFEdsQDVTEY 632

                         250       260       270
                  ....*....|....*....|....*....|.
gi 755531599  495 VATLL--ERAQSICRAQEAARQQLLDRELKK 523
Cdd:PRK04863  633 MQQLLerERELTVERDELAARKQALDEEIER 663

PHA03247

large tegument protein UL36; Provisional

541-971

4.30e-05

large tegument protein UL36; Provisional

Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 4.30e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  541 EEGEAVEAGDTPEEL----------RSLPPDMmVGPRLPDPFLGTTA------PLHFSP-GPFPSSTGPATHYLSGPLPP 603
Cdd:PHA03247 2541 EELASDDAGDPPPPLppaappaapdRSVPPPR-PAPRPSEPAVTSRArrpdapPQSARPrAPVDDRGDPRGPAPPSPLPP 2619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  604 GTYSGPTQLMQPRAAVPMAPATVLYPAPAYTSelglvPRSSPQHGIVSSPYAGVGPPQPVVglPSAPPPQLSGPELAMTV 683
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPER-----PRDDPAPGRVSRPRRARRLGRAAQ--ASSPPQRPRRRAARPTV 2692

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  684 RPATTTVDSVQAPISSHTAPRPnPTPALPQPcfPVPQPVPQSVPQPQPLPVPYTYSIGTKQPL-PAPytysIGTKQHLTG 762
Cdd:PHA03247 2693 GSLTSLADPPPPPPTPEPAPHA-LVSATPLP--PGPAAARQASPALPAAPAPPAVPAGPATPGgPAR----PARPPTTAG 2765

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  763 PlpQHQFPPGIPTGFPVPRTGPQAQAQPQPQPQPQPQpqpqpqpqpqpqsqsqpqpqpqpqpqrpAFGPQPTQQPLPFQH 842
Cdd:PHA03247 2766 P--PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS----------------------------PWDPADPPAAVLAPA 2815

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  843 PHLFPSQAPGILPPppptpyhftPQPGVLGQPPPTLhtqlyPGPSQDPLPPHSGALPFPSPGPPHPHPTLAYGPAPSPRP 922
Cdd:PHA03247 2816 AALPPAASPAGPLP---------PPTSAQPTAPPPP-----PGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARP 2881

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599  923 L-------GPQATPVSIRGPPPASQPTPSPhlvpspapspgPGPVPSRPPTAEPPP 971
Cdd:PHA03247 2882 PvrrlarpAVSRSTESFALPPDQPERPPQP-----------QAPPPPQPQPQPPPP 2926

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

551-763

6.05e-05

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.60 E-value: 6.05e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   551 TPEELRSLPPDMMVGPRLPDPFLGTTAPLHFSPGPFPSSTGPaTHYLSGPLPPGTYsgptqlmqPRAAVPMAPATVLYPA 630
Cdd:pfam05109  517 TPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSP-TPAVTTPTPNATI--------PTLGKTSPTSAVTTPT 587

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   631 PAYTSElgLVPRSSPQH--------GIVSSPYAGVGPPQPVVGLPSAPPPQLSGPELAMTVRPATTTVDSVQAPISSHTA 702
Cdd:pfam05109  588 PNATSP--TVGETSPQAnttnhtlgGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTS 665

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755531599   703 PRPNPTPALPQPCFPVPQPVPQSVPqpqplpvpyTYSIGTKQPLPAPytysiGTKQHLTGP 763
Cdd:pfam05109  666 HMPLLTSAHPTGGENITQVTPASTS---------THHVSTSSPAPRP-----GTTSQASGP 712

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

542-970

6.18e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 47.84 E-value: 6.18e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   542 EGEAVEAGDTPEELRSLPPDM-----MVGPRLPDP--------------FLGTTAPLHFSP-GPFPSSTGPATHYLSGPL 601
Cdd:pfam03154  117 EGESSDGRSVNDEGSSDPKDIdqdnrSTSPSIPSPqdnesdsdssaqqqILQTQPPVLQAQsGAASPPSPPPPGTTQAAT 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   602 PPGTYSGPTQLMQPRAAVPMAPATVLYPAPaytselglvPRSSPQHGIVSSPYAGVGPPQPVVGLPSAPPPQLSGPElam 681
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAA---------PHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQ--- 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   682 TVRPATTTVDSVQAPISSHTAPRPNPTPALPQPcFPVPQPVPQSvpqpqplpvpytysigtKQPLPAPYTYSIGTKQHLT 761
Cdd:pfam03154  265 PLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQP-FPLTPQSSQS-----------------QVPPGPSPAAPGQSQQRIH 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   762 GPLPQHQFPPGIPtgfpvPRTGPQAQAQPQPQPQPQPQPQPQPQPQPQPQSQSQPQPQPQPQPQRPA-FGPQPTQQPLPF 840
Cdd:pfam03154  327 TPPSQSQLQSQQP-----PREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnLPPPPALKPLSS 401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   841 QHPHLFPSQAPGILPPPPPTPyhftPQPGVLGQPPPTLHTQLYPGPSQDPlPPHSGALPFPSPGPPHPHPTLAYGPAPSP 920
Cdd:pfam03154  402 LSTHHPPSAHPPPLQLMPQSQ----QLPPPPAQPPVLTQSQSLPPPAASH-PPTSGLHQVPSQSPFPQHPFVPGGPPPIT 476

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755531599   921 RPLGPQAT--------------PVSIRGPPPASQPTPSPHLVPSPAPSPGPGPVPSRPPTAEPP 970
Cdd:pfam03154  477 PPSGPPTStssampgiqppssaSVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSP 540

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

263-521

2.35e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 2.35e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  263 LKDIRDLLEEDELQEQKLQETLGQagagpgpSVAKAELA-EVRREWAKYMEVHEKASftnSELHRAMNLhvgnLRLLSGP 341
Cdd:COG3096   422 LEKARALCGLPDLTPENAEDYLAA-------FRAKEQQAtEEVLELEQKLSVADAAR---RQFEKAYEL----VCKIAGE 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  342 LDQVRAALPTPALT---PEDKAVLQNLKRILAKVQEMRdQRVSLEQQLRELIQkdditaslvttdhsEMKKLFEEQLKKY 418
Cdd:COG3096   488 VERSQAWQTARELLrryRSQQALAQRLQQLRAQLAELE-QRLRQQQNAERLLE--------------EFCQRIGQQLDAA 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  419 DQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMK-KSQEGKDFY--ADLESKV 495
Cdd:COG3096   553 EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERlREQSGEALAdsQEVTAAM 632

                         250       260
                  ....*....|....*....|....*...
gi 755531599  496 ATLL--ERAQSICRAQEAARQQLLDREL 521
Cdd:COG3096   633 QQLLerEREATVERDELAARKQALESQI 660

COG1340

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

351-516

5.14e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 5.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  351 TPALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLRELIQKDDI----TASLVT----------TDHSEMKKLFEEQLK 416
Cdd:COG1340     3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDElnaqVKELREeaqelrekrdELNEKVKELKEERDE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  417 KYDQLKVYLEQnLAAQDNVLRALTEANVQYAAVRRVLSELDQKwnstLQTLVASYEAYEDLMKKSQEGKDFYADLE---- 492
Cdd:COG1340    83 LNEKLNELREE-LDELRKELAELNKAGGSIDKLRKEIERLEWR----QQTEVLSPEEEKELVEKIKELEKELEKAKkale 157

                         170       180
                  ....*....|....*....|....*.
gi 755531599  493 --SKVATLLERAQSICRAQEAARQQL 516
Cdd:COG1340   158 knEKLKELRAELKELRKEAEEIHKKI 183

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

560-770

5.33e-04

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 44.52 E-value: 5.33e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   560 PDMMVGPRLPDPFLGTTAPLHFSPGPFPSSTGPaTHYLSGPLPPGTYSG-------PTQLMQPRAAVP-MAPATVLYPAP 631
Cdd:pfam05109  400 PKTLIITRTATNATTTTHKVIFSKAPESTTTSP-TLNTTGFAAPNTTTGlpssthvPTNLTAPASTGPtVSTADVTSPTP 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   632 AYTSelglvprsspqhgivsspyAGVGPPQPvvglpsAPPPQLSGPElamtvrpatTTVDSVQAPISSHTAPRPNPTPAL 711
Cdd:pfam05109  479 AGTT-------------------SGASPVTP------SPSPRDNGTE---------SKAPDMTSPTSAVTTPTPNATSPT 524

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 755531599   712 PQPCFPVPQPVPQSVPQPQPLPVPYTYSIGTKQPLPApytysigtkqhLTGPLPQHQFP 770
Cdd:pfam05109  525 PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPA-----------VTTPTPNATIP 572

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

227-523

5.49e-04

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 5.49e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   227 QLMEKCAalsvrPDTVKNLVQSMQVLSGVFTDVEASLKDIRD----LLEEDELQEQ--KLQETLGQAGA------GPGPS 294
Cdd:TIGR00618  204 QLLTLCT-----PCMPDTYHERKQVLEKELKHLREALQQTQQshayLTQKREAQEEqlKKQQLLKQLRArieelrAQEAV 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   295 VAKA-ELAEVRREWAKYM-------EVHEKASFTNSELHRAMNLhvgnlrllsgpldqvRAALptpaltpedkavLQNLK 366
Cdd:TIGR00618  279 LEETqERINRARKAAPLAahikavtQIEQQAQRIHTELQSKMRS---------------RAKL------------LMKRA 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   367 RILAKVQEMRDQRVSLEQQLRELIQKDDIT-ASLVTTDHSEMKKLFEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQ 445
Cdd:TIGR00618  332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHeVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   446 YAAV---RRVL---------SELDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYA-----DLESKVATLLERAQSI--C 506
Cdd:TIGR00618  412 IDTRtsaFRDLqgqlahakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSlkereQQLQTKEQIHLQETRKkaV 491

                          330
                   ....*....|....*..
gi 755531599   507 RAQEAARQQLLDRELKK 523
Cdd:TIGR00618  492 VLARLLELQEEPCPLCG 508

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

255-516

7.44e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.44e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  255 VFTDVEASLKDIRDLLE-EDELQEQKLQETLgqagagpgpsvakaeLAEVRREWAKYMEVHEKASFTNSELHRAmNLHVG 333
Cdd:COG4913   223 TFEAADALVEHFDDLERaHEALEDAREQIEL---------------LEPIRELAERYAAARERLAELEYLRAAL-RLWFA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  334 NLRLlsgplDQVRAALPtpALTPEDKAVLQNLKRILAKVQEMRDQRVSLEQQLREL--IQKDDITASLVTTdhsemkklf 411
Cdd:COG4913   287 QRRL-----ELLEAELE--ELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLEREIERL--------- 350

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  412 EEQLKKydqlkvyLEQNLAAQDNVLRALTEANV----QYAAVRRVLSELDQKWNSTLQTLVasyEAYEDLMKKSQEGKDF 487
Cdd:COG4913   351 ERELEE-------RERRRARLEALLAALGLPLPasaeEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRE 420

                         250       260
                  ....*....|....*....|....*....
gi 755531599  488 YADLESKVATLLERAQSICRAQEAARQQL 516
Cdd:COG4913   421 LRELEAEIASLERRKSNIPARLLALRDAL 449

Smc

COG1196

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...

359-520

9.02e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 9.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  359 KAVLQNLKRILAKVQEMRDQRVSLEQQ---------LRE----------LIQKDDITASL--VTTDHSEMKKLFEEQLKK 417
Cdd:COG1196   182 EATEENLERLEDILGELERQLEPLERQaekaeryreLKEelkeleaellLLKLRELEAELeeLEAELEELEAELEELEAE 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  418 YDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYADLESKVAT 497
Cdd:COG1196   262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                         170       180
                  ....*....|....*....|...
gi 755531599  498 LLERAQSICRAQEAARQQLLDRE 520
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAE 364

ClyA_Cry6Aa-like

cd22656

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...

181-318

1.06e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.

Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 1.06e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  181 EEKAKLLREMLAKIEDKNEVLDQFMDSMQLDPETVDNLDAynhippqlmekcAALSVrpDTVKNLVQ----SMQVLSGVF 256
Cdd:cd22656   190 KLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTA------------ADTDL--DNLLALIGpaipALEKLQGAW 255

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755531599  257 TDVEASLKDIRDLLEEDELQEqklqetlgqagagPGPSVAKAELAEVRREWAkymEVHEKAS 318
Cdd:cd22656   256 QAIATDLDSLKDLLEDDISKI-------------PAAILAKLELEKAIEKWN---ELAEKAD 301

BRO1_Brox_like

cd09243

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains ...

44-133

1.33e-03

Protein-interacting Bro1-like domain of human Brox1 and related proteins; This family contains the Bro1-like domain of a single-domain protein, human Brox, and related domains. It belongs to the BRO1_Alix_like superfamily which also includes the Bro1-like domains of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), RhoA-binding proteins Rhophilin-1 and -2, Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, Ustilago maydis Rim23 (also known as PalC), and related domains. Alix, HD-PTP, Brox, Bro1, Rim20, and Rim23, interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Bro1-like domains are boomerang-shaped, and part of the domain is a tetratricopeptide repeat (TPR)-like structure. Bro1-like domains bind components of the ESCRT-III complex: CHMP4 in the case of Brox. Human Brox can bind to human immunodeficiency virus type 1 (HIV-1) nucleocapsid. In addition to a Bro1-like domain, Brox also has a C-terminal thioester-linkage site for isoprenoid lipids (CaaX motif). This family lacks the V-shaped (V) domain found in many members of the BRO1_Alix_like superfamily.

Pssm-ID: 185766 Cd Length: 353 Bit Score: 42.71 E-value: 1.33e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   44 WKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQSALDKLNEAIKLAK--------GQPDTVQDALRFAMdvIGGK 115
Cdd:cd09243   235 WRKYLQLKSVFYLAYAYCYHGETLLAKDKCGEAIRSLQESEKLYNKAEALCKeyaktkgpGTTAKPDQHLFFRK--LGPL 312

                          90       100
                  ....*....|....*....|..
gi 755531599  116 YNS----AKKDNDFIYHEAVPA 133
Cdd:cd09243   313 VKRtlekCERENGFIYHQKVPD 334

LapB

COG2956

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...

296-516

1.50e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.41 E-value: 1.50e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  296 AKAELAEVRREWAKYMEVHEKASFTNSELHRAMnLHVGNLRLLSGPLDQVRAALpTPALT--PEDKAVLQNLKRILAKVQ 373
Cdd:COG2956    47 ALGNLYRRRGEYDRAIRIHQKLLERDPDRAEAL-LELAQDYLKAGLLDRAEELL-EKLLEldPDDAEALRLLAEIYEQEG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  374 EMRDqrvsLEQQLRELIQKDDITASLvttdHSEMKKLFEEQlKKYDQLKVYLEQNLAAQDNVLRALTE-ANV-----QYA 447
Cdd:COG2956   125 DWEK----AIEVLERLLKLGPENAHA----YCELAELYLEQ-GDYDEAIEALEKALKLDPDCARALLLlAELyleqgDYE 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755531599  448 AVRRVLSELDQKWNSTLQTLVASYEAYEDLmKKSQEGKDFY---------ADLESKVATLLERAQSICRAQEAARQQL 516
Cdd:COG2956   196 EAIAALERALEQDPDYLPALPRLAELYEKL-GDPEEALELLrkaleldpsDDLLLALADLLERKEGLEAALALLERQL 272

Gag_spuma

pfam03276

Spumavirus gag protein;

598-723

1.77e-03

Spumavirus gag protein;

Pssm-ID: 460872 [Multi-domain] Cd Length: 614 Bit Score: 42.81 E-value: 1.77e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   598 SGPLPPG-TYSGPTQLmqPRAAVPMAPATvlyPAPAYTSELGLVPRSSPQHGIVSSPYAGvgPPQPVVGLPSAPPPQLSG 676
Cdd:pfam03276  183 QGGIPPGaSFSGLPSL--PAIGGIHLPAI---PGIHARAPPGNIARSLGDDIMPSLGDAG--MPQPRFAFHPGNPFAEAE 255

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 755531599   677 ---PELAMTVRPATTTVDSVQAPISSHTAPRPNPTPALPQPCFPVPQPVP 723
Cdd:pfam03276  256 ghpFAEAEGERPRDIPRAPRIDAPSAPAIPAIQPIAPPMIPPIGAPIPIP 305

PRK11281

mechanosensitive channel MscK;

354-517

3.20e-03

mechanosensitive channel MscK;

Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 3.20e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  354 LTPEDKAVLQNLK---RILAKVQEMRDQRVSLEQQLRELIQK-DDITASLVTTDHSEMKKLfEEQLKKY--DQLKVYLEQ 427
Cdd:PRK11281   54 LEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKlRQAQAELEALKDDNDEET-RETLSTLslRQLESRLAQ 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  428 NLAAQDNVLRALTEANVQYAAVR----RVLSELDQkwNST-LQTLvasyeayEDLMKKSQEGKdfyADLESKVATLLERA 502
Cdd:PRK11281  133 TLDQLQNAQNDLAEYNSQLVSLQtqpeRAQAALYA--NSQrLQQI-------RNLLKGGKVGG---KALRPSQRVLLQAE 200

                         170
                  ....*....|....*
gi 755531599  503 QSICRAQEAARQQLL 517
Cdd:PRK11281  201 QALLNAQNDLQRKSL 215

SMC_prok_B

TIGR02168

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

259-513

4.03e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 4.03e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   259 VEASLKDIRDLLEEDELQEQKLQETLGQAGAgpgpSVAKAE---------LAEVRREWAKYMEVHEKASFTNSELHRAMN 329
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALAN----EISRLEqqkqilrerLANLERQLEELEAQLEELESKLDELAEELA 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   330 LHVGNLRLLSGPLDQVRAALPtpaltpEDKAVLQNLKRILAKVQEMRDQRVSLEQQLREliQKDDITASLVTtdhsemkk 409
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELE------ELEAELEELESRLEELEEQLETLRSKVAQLEL--QIASLNNEIER-------- 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   410 lFEEQLKkydQLKVYLEQNLAAQDNVLRALTEANVQyaAVRRVLSELDQKWNSTLQTLVASYEAYEDLMKKSQEGKDFYA 489
Cdd:TIGR02168  405 -LEARLE---RLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260
                   ....*....|....*....|....
gi 755531599   490 DLESKVATLLERAQSICRAQEAAR 513
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLE 502

mukB

PRK04863

chromosome partition protein MukB;

300-515

6.51e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 6.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  300 LAEVRREWAKYMEVHEKASFTNSELHRamnlhvgnlrlLSGPLDQVRAALPTPALTPEDKAVLQ-----------NLKRI 368
Cdd:PRK04863  788 IEQLRAEREELAERYATLSFDVQKLQR-----------LHQAFSRFIGSHLAVAFEADPEAELRqlnrrrvelerALADH 856

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  369 LAKVQEMRDQRVSLEQQLRELIQKDDITASLVTTDHSEMKKLFEEQLKKYDQLKVYLEQN---LAAQDNVLRALTEANVQ 445
Cdd:PRK04863  857 ESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSDPEQ 936

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755531599  446 YAAVRRVLSELDQKWNSTLQTL--------VASYEAYEDlmkkSQEGKDFYADLESKVATLLERAQSIC-RAQEAARQQ 515
Cdd:PRK04863  937 FEQLKQDYQQAQQTQRDAKQQAfaltevvqRRAHFSYED----AAEMLAKNSDLNEKLRQRLEQAEQERtRAREQLRQA 1011

COG4913

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

267-476

6.58e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  267 RDLLEEDELQEQKLQETLGQAGAgpgpsvAKAELAEVRREWAKYMEVHEK-ASFTNSELhramnlhvgNLRLLSGPLDQV 345
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEE------RLEALEAELDALQERREALQRlAEYSWDEI---------DVASAEREIAEL 673

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  346 RAALPtpALTpEDKAVLQNLKRILAKVQ-----------EMRDQRVSLEQQL----RELIQKDDITASLVTTDHSEMKKL 410
Cdd:COG4913   674 EAELE--RLD-ASSDDLAALEEQLEELEaeleeleeeldELKGEIGRLEKELeqaeEELDELQDRLEAAEDLARLELRAL 750

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755531599  411 FEEQLKKYDQLKVYLEQNLAAQDNVLRALTEANVQYAAVRRVLSELDQKWNSTLQTLVASYEAYED 476
Cdd:COG4913   751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPE 816

PHA03307

transcriptional regulator ICP4; Provisional

548-721

6.63e-03

transcriptional regulator ICP4; Provisional

Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.31 E-value: 6.63e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  548 AGDTPEELRSLPPDMMVgprlPDPFLGTTAPLHFSPGP---FPSSTGPATHylSGPLPPGTYSGPTQLMQPRAAVPMAPA 624
Cdd:PHA03307   28 PGDAADDLLSGSQGQLV----SDSAELAAVTVVAGAAAcdrFEPPTGPPPG--PGTEAPANESRSTPTWSLSTLAPASPA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599  625 TVLYPAPAYTSELGLVPRSSPQHGIVSSPYAGVGPPQPVVGLPSAPPPQLSGPELAMTVRPATTTVDSVQAPISSHTAPR 704
Cdd:PHA03307  102 REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE 181

                         170
                  ....*....|....*..
gi 755531599  705 PNPTPALPQPCFPVPQP 721
Cdd:PHA03307  182 TARAPSSPPAEPPPSTP 198

Atrophin-1

pfam03154

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...

557-940

7.23e-03

Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.91 E-value: 7.23e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   557 SLPPDMMVGPRLPDPFLGTTAPLHfsPGPFPSSTGPATHYLSGPLPPGTYSGPTQlmQPRAAVPMAPAtvlyPAPAYTSE 636
Cdd:pfam03154  215 SQPPNQTQSTAAPHTLIQQTPTLH--PQRLPSPHPPLQPMTQPPPPSQVSPQPLP--QPSLHGQMPPM----PHSLQTGP 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   637 lglvprSSPQHGIVSSPYaGVGPPQPVVGLPSAPPPQLSGPELAMTVRPAT-TTVDSVQAPISSHTAPRPNPTPAL-PQP 714
Cdd:pfam03154  287 ------SHMQHPVPPQPF-PLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSqSQLQSQQPPREQPLPPAPLSMPHIkPPP 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   715 CFPVPQ-PVPQSVPQPQPLPVPYTYSIGTKQPlPAPYTYSIGTkqhltgpLPQHQFPPGIPTGFPVPRTGPQAQAQPQPQ 793
Cdd:pfam03154  360 TTPIPQlPNPQSHKHPPHLSGPSPFQMNSNLP-PPPALKPLSS-------LSTHHPPSAHPPPLQLMPQSQQLPPPPAQP 431

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755531599   794 PQPQPQPQPQPQPQPQPQSQsqpqpqpqpqpqrpAFGPQPTQQPLPfQHPhLFPSQAPGILPPPPPTPYHFTPQPGVlgQ 873
Cdd:pfam03154  432 PVLTQSQSLPPPAASHPPTS--------------GLHQVPSQSPFP-QHP-FVPGGPPPITPPSGPPTSTSSAMPGI--Q 493

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755531599   874 PPPTLhtqlyPGPSQDPLPPHSGALPFPSPGPPHPHPTLAYGPAPSPRPLGPQATPVSIRGPPPASQ 940
Cdd:pfam03154  494 PPSSA-----SVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSHASQ 555

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