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Conserved domains on  [gi|359474593|ref|XP_002279188|]
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type I inositol polyphosphate 5-phosphatase 2 isoform X2 [Vitis vinifera]

Protein Classification

type I inositol polyphosphate 5-phosphatase 2( domain architecture ID 10011027)

type I inositol polyphosphate 5-phosphatase 2 (IP5PII) has phosphatase activity toward Ins(1,4,5)P3 and Ins(1,3,4,5)P4; could also be able to hydrolyze PtdIns(4,5)P2 and PtdIns(3,4,5)P3

CATH:  3.60.10.10
EC:  3.1.3.56
Gene Ontology:  GO:0032957|GO:0046856|GO:0004445
PubMed:  10838565
SCOP:  4002213

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 1-626 0e+00

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


:

Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 1215.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   1 MRTRQGKRSEAFWPSIVMKKWLNIKPKAYDFSEDEVDTETESEDDACSLKDARVQMGEDHACRMQRNQSVCTNQTSE--- 77
Cdd:PLN03191   1 MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSVFGNQISDggv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593  78 --SKGYSSSHRRGKSETLRVHYINRKDIRLTIGTWNVAGRLPNEDLEIEEWLCMQEPADIYILGFQEVVPLNAGNVLGAE 155
Cdd:PLN03191  81 svSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADIYIIGFQEVVPLNAGNVLGAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 156 DSQPIPKWEAIIRRTLNKSFEPESEYKSYSAPTSPVLRASCVADALKEEVDSPTLEMMNNETAAPTNGCNLERHKLNGMI 235
Cdd:PLN03191 161 DSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPVLRTSIVADELAEEVDSLPLEMMNNEFIDAATGCPSLEPERNKNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 236 GtgkkfqlrrlyggdsdirldWPEYSLDKVPQVL-SNLKLRRVLSSSARVGFGWMETPINFSPQKVTLDGGGMKRSYRSS 314
Cdd:PLN03191 241 G--------------------WPEHSLDATPQVVsSNSKLRRVFSSSARLGFKWPENPSLFSPQRFALNARGLKRSHRSF 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 315 GNLGLIFMEQQERSKLCDYL------SDVSDRSSEEEDESLIEIPEHQFKDGENKDCMKSRQSYVRIVSKQMVGIYISVW 388
Cdd:PLN03191 301 GNLGLSWNEIKQRSEVPEVPevidslSDVSDRSSEAEDDTFKEVPSYQLPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVW 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 389 VRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDGDKQRRNSDVYEILRRTQFSSVIDA 468
Cdd:PLN03191 381 VRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDT 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 469 DQPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEGWKEGVIDFPPTYKYEINSDRY 548
Cdd:PLN03191 461 DQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRY 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 549 VGENPKEGEKKRSPAWCDRILWLGKGIKQLCYNRAEIRVSDHRPVSSNFMVEVEVFDHRKLQRALKPTDA---RVHPEIF 625
Cdd:PLN03191 541 VGENPKEGEKKRSPAWCDRILWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRALNVNSAaasAVHPEPS 620


                 .
gi 359474593 626 L 626
Cdd:PLN03191 621 F 621
 
Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 1-626 0e+00

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 1215.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   1 MRTRQGKRSEAFWPSIVMKKWLNIKPKAYDFSEDEVDTETESEDDACSLKDARVQMGEDHACRMQRNQSVCTNQTSE--- 77
Cdd:PLN03191   1 MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSVFGNQISDggv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593  78 --SKGYSSSHRRGKSETLRVHYINRKDIRLTIGTWNVAGRLPNEDLEIEEWLCMQEPADIYILGFQEVVPLNAGNVLGAE 155
Cdd:PLN03191  81 svSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADIYIIGFQEVVPLNAGNVLGAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 156 DSQPIPKWEAIIRRTLNKSFEPESEYKSYSAPTSPVLRASCVADALKEEVDSPTLEMMNNETAAPTNGCNLERHKLNGMI 235
Cdd:PLN03191 161 DSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPVLRTSIVADELAEEVDSLPLEMMNNEFIDAATGCPSLEPERNKNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 236 GtgkkfqlrrlyggdsdirldWPEYSLDKVPQVL-SNLKLRRVLSSSARVGFGWMETPINFSPQKVTLDGGGMKRSYRSS 314
Cdd:PLN03191 241 G--------------------WPEHSLDATPQVVsSNSKLRRVFSSSARLGFKWPENPSLFSPQRFALNARGLKRSHRSF 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 315 GNLGLIFMEQQERSKLCDYL------SDVSDRSSEEEDESLIEIPEHQFKDGENKDCMKSRQSYVRIVSKQMVGIYISVW 388
Cdd:PLN03191 301 GNLGLSWNEIKQRSEVPEVPevidslSDVSDRSSEAEDDTFKEVPSYQLPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVW 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 389 VRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDGDKQRRNSDVYEILRRTQFSSVIDA 468
Cdd:PLN03191 381 VRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDT 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 469 DQPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEGWKEGVIDFPPTYKYEINSDRY 548
Cdd:PLN03191 461 DQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRY 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 549 VGENPKEGEKKRSPAWCDRILWLGKGIKQLCYNRAEIRVSDHRPVSSNFMVEVEVFDHRKLQRALKPTDA---RVHPEIF 625
Cdd:PLN03191 541 VGENPKEGEKKRSPAWCDRILWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRALNVNSAaasAVHPEPS 620


                 .
gi 359474593 626 L 626
Cdd:PLN03191 621 F 621
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 363-599 3.19e-81

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins; This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain.


Pssm-ID: 197327  Cd Length: 292  Bit Score: 258.01  E-value: 3.19e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 363 KDCMKSRQSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLtSGHK 442
Cdd:cd09093   63 ERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHL-AAHM 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 443 dGDKQRRNSDVYEILRRTQFssVIDADQPETIPSHDQIFWFGDLNYRLNMLDAEIRK-LVARKKWDELINSDQLSKELRS 521
Cdd:cd09093  142 -EEVERRNQDYKDICARMKF--EDPDGPPLSISDHDVVFWLGDLNYRIQELPTEEVKeLIEKNDLEELLKYDQLNIQRRA 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359474593 522 GHVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQLCYNR-AEIRVSDHRPVSSNFMV 599
Cdd:cd09093  219 GKVFEGFTEGEINFIPTYKYDPGTDNW-----DSSEKCRAPAWCDRILWRGTNIVQLSYRShMELKTSDHKPVSALFDI 292
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 364-601 5.49e-65

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 215.68  E-value: 5.49e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   364 DCMKSRQSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGhkD 443
Cdd:smart00128  73 SSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAG--A 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   444 GDKQRRNSDVYEILRRTQFSsvidADQPETIPSHDQIFWFGDLNYRLNMLDAE-IRKLVARKKWDELINSDQLSKELRSG 522
Cdd:smart00128 151 SNVEQRNQDYKTILRALSFP----ERALLSQFDHDVVFWFGDLNFRLDSPSYEeVRRKISKKEFDDLLEKDQLNRQREAG 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   523 HVFEGWKEGVIDFPPTYKYE-INSDRYVGenpkeGEKKRSPAWCDRILW--LGKGIKQLC--YNRAEIRVSDHRPVSSNF 597
Cdd:smart00128 227 KVFKGFQEGPITFPPTYKYDsVGTETYDT-----SEKKRVPAWCDRILYrsNGPELIQLSeyHSGMEITTSDHKPVFATF 301


                   ....
gi 359474593   598 MVEV 601
Cdd:smart00128 302 RLKV 305
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
348-609 7.95e-47

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 171.50  E-value: 7.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 348 SLIEIPEHQFKDGENKDCMKSRQS---YVRIVSKQMVGIYISVWVRKRlrrhiNNLKVSPVG-----VGLMGYMGNKGSV 419
Cdd:COG5411   82 SADPYDRLRIWESKVLDCLNGAQSdekYSLLRSPQLGGILLRVFSLAT-----NLPVVKPVSgtvkkTGFGGSSSNKGAV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 420 SVSMSVFQTRICFVCSHLTSGHKDGDKqrRNSDVYEILRRTQFSSvidadqPETIPSHDQIFWFGDLNYRLNMLDAEIRK 499
Cdd:COG5411  157 AIRFNYERTSFCFVNSHLAAGVNNIEE--RIFDYRSIASNICFSR------GLRIYDHDTIFWLGDLNYRVTSTNEEVRP 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 500 LVARKKW--DELINSDQLSKELRSGHVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQ 577
Cdd:COG5411  229 EIASDDGrlDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEY-----DTSDKGRIPSWTDRILYKSEQLTP 303

                        250       260       270
                 ....*....|....*....|....*....|...
gi 359474593 578 LCYNRAE-IRVSDHRPVSSNFMVEVEVFDHRKL 609
Cdd:COG5411  304 HSYSSIPhLMISDHRPVYATFRAKIKVVDPSKK 336
 
Name Accession Description Interval E-value
PLN03191 PLN03191
Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional
 1-626 0e+00

Type I inositol-1,4,5-trisphosphate 5-phosphatase 2; Provisional


Pssm-ID: 215624 [Multi-domain]  Cd Length: 621  Bit Score: 1215.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   1 MRTRQGKRSEAFWPSIVMKKWLNIKPKAYDFSEDEVDTETESEDDACSLKDARVQMGEDHACRMQRNQSVCTNQTSE--- 77
Cdd:PLN03191   1 MRTRRGKRPEAFWPSIVMKKWLNIKPKVYDFSEDEYDTETESEDDACSVKDVRVNVDEDHANRRQGNQSVFGNQISDggv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593  78 --SKGYSSSHRRGKSETLRVHYINRKDIRLTIGTWNVAGRLPNEDLEIEEWLCMQEPADIYILGFQEVVPLNAGNVLGAE 155
Cdd:PLN03191  81 svSKGYSSKHRRGKSETLRAQYINTKDIRVTIGTWNVAGRLPSEDLEIEDWLSTEEPADIYIIGFQEVVPLNAGNVLGAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 156 DSQPIPKWEAIIRRTLNKSFEPESEYKSYSAPTSPVLRASCVADALKEEVDSPTLEMMNNETAAPTNGCNLERHKLNGMI 235
Cdd:PLN03191 161 DSRPIPKWEAIIRRTLNKSNKPESKHKSYSAPPSPVLRTSIVADELAEEVDSLPLEMMNNEFIDAATGCPSLEPERNKNI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 236 GtgkkfqlrrlyggdsdirldWPEYSLDKVPQVL-SNLKLRRVLSSSARVGFGWMETPINFSPQKVTLDGGGMKRSYRSS 314
Cdd:PLN03191 241 G--------------------WPEHSLDATPQVVsSNSKLRRVFSSSARLGFKWPENPSLFSPQRFALNARGLKRSHRSF 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 315 GNLGLIFMEQQERSKLCDYL------SDVSDRSSEEEDESLIEIPEHQFKDGENKDCMKSRQSYVRIVSKQMVGIYISVW 388
Cdd:PLN03191 301 GNLGLSWNEIKQRSEVPEVPevidslSDVSDRSSEAEDDTFKEVPSYQLPEDLIKDCRKVKQKYVRIVSKQMVGIYVSVW 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 389 VRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDGDKQRRNSDVYEILRRTQFSSVIDA 468
Cdd:PLN03191 381 VRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSISMSLFQSRLCFVCSHLTSGHKDGAEQRRNADVYEIIRRTRFSSVLDT 460

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 469 DQPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEGWKEGVIDFPPTYKYEINSDRY 548
Cdd:PLN03191 461 DQPQTIPSHDQIFWFGDLNYRLNMLDTEVRKLVAQKRWDELINSDQLIKELRSGHVFDGWKEGPIKFPPTYKYEINSDRY 540

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 549 VGENPKEGEKKRSPAWCDRILWLGKGIKQLCYNRAEIRVSDHRPVSSNFMVEVEVFDHRKLQRALKPTDA---RVHPEIF 625
Cdd:PLN03191 541 VGENPKEGEKKRSPAWCDRILWLGKGIKQLCYKRSEIRLSDHRPVSSMFLVEVEVFDHRKLQRALNVNSAaasAVHPEPS 620


                 .
gi 359474593 626 L 626
Cdd:PLN03191 621 F 621
INPP5c_INPP5B cd09093
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol ...
 363-599 3.19e-81

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Type II inositol polyphosphate 5-phosphatase I, Oculocerebrorenal syndrome of Lowe 1, and related proteins; This subfamily contains the INPP5c domain of type II inositol polyphosphate 5-phosphatase I (INPP5B), Oculocerebrorenal syndrome of Lowe 1 (OCRL-1), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5B and OCRL1 preferentially hydrolyze the 5-phosphate of phosphatidylinositol (4,5)- bisphosphate [PI(4,5)P2] and phosphatidylinositol (3,4,5)- trisphosphate [PI(3,4,5)P3]. INPP5B can also hydrolyze soluble inositol (1,4,5)-trisphosphate [I(1,4,5)P3] and inositol (1,3,4,5)-tetrakisphosphate [I(1,3,4,5)P4]. INPP5B participates in the endocytic pathway and in the early secretory pathway. In the latter, it may function in retrograde ERGIC (ER-to-Golgi intermediate compartment)-to-ER transport; it binds specific RAB proteins within the secretory pathway. In the endocytic pathway, it binds RAB5 and during endocytosis, may function in a RAB5-controlled cascade for converting PI(3,4,5)P3 to phosphatidylinositol 3-phosphate (PI3P). This cascade may link growth factor signaling and membrane dynamics. Mutation in OCRL1 is implicated in Lowe syndrome, an X-linked recessive multisystem disorder, which includes defects in eye, brain, and kidney function, and in Type 2 Dent's disease, a disorder with only the renal symptoms. OCRL-1 may have a role in membrane trafficking within the endocytic pathway and at the trans-Golgi network, and may participate in actin dynamics or signaling from endomembranes. OCRL1 and INPP5B have overlapping functions: deletion of both 5-phosphatases in mice is embryonic lethal, deletion of OCRL1 alone has no phenotype, and deletion of Inpp5b alone has only a mild phenotype (male sterility). Several of the proteins that interact with OCRL1 also bind INPP5B, for examples, inositol polyphosphate phosphatase interacting protein of 27kDa (IPIP27)A and B (also known as Ses1 and 2), and endocytic signaling adaptor APPL1. OCRL1, but not INPP5B, binds clathrin heavy chain, the plasma membrane AP2 adaptor subunit alpha-adaptin. In addition to this INPP5c domain, most proteins in this subfamily have a C-terminal RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain.


Pssm-ID: 197327  Cd Length: 292  Bit Score: 258.01  E-value: 3.19e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 363 KDCMKSRQSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLtSGHK 442
Cdd:cd09093   63 ERGLHPDAKYKKVKLIRLVGMMLLVFVKKEHRQHIKEVAAETVGTGIMGKMGNKGGVAVRFQFHNTTFCFVNSHL-AAHM 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 443 dGDKQRRNSDVYEILRRTQFssVIDADQPETIPSHDQIFWFGDLNYRLNMLDAEIRK-LVARKKWDELINSDQLSKELRS 521
Cdd:cd09093  142 -EEVERRNQDYKDICARMKF--EDPDGPPLSISDHDVVFWLGDLNYRIQELPTEEVKeLIEKNDLEELLKYDQLNIQRRA 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 359474593 522 GHVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQLCYNR-AEIRVSDHRPVSSNFMV 599
Cdd:cd09093  219 GKVFEGFTEGEINFIPTYKYDPGTDNW-----DSSEKCRAPAWCDRILWRGTNIVQLSYRShMELKTSDHKPVSALFDI 292
INPP5c cd09074
Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate ...
 363-599 2.48e-75

Catalytic domain of inositol polyphosphate 5-phosphatases; Inositol polyphosphate 5-phosphatases (5-phosphatases) are signal-modifying enzymes, which hydrolyze the 5-phosphate from the inositol ring of specific 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), such as PI(4,5)P2, PI(3,4,5)P3, PI(3,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4. These enzymes are Mg2+-dependent, and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, 5-phosphatases often contain additional domains and motifs, such as the SH2 domain, the Sac-1 domain, the proline-rich domain (PRD), CAAX, RhoGAP (RhoGTPase-activating protein), and SKICH [SKIP (skeletal muscle- and kidney-enriched inositol phosphatase) carboxyl homology] domains, that are important for protein-protein interactions and/or for the subcellular localization of these enzymes. 5-phosphatases incorporate into large signaling complexes, and regulate diverse cellular processes including postsynaptic vesicular trafficking, insulin signaling, cell growth and survival, and endocytosis. Loss or gain of function of 5-phosphatases is implicated in certain human diseases. This family also contains a functionally unrelated nitric oxide transport protein, Cimex lectularius (bedbug) nitrophorin, which catalyzes a heme-assisted S-nitrosation of a proximal thiolate; the heme however binds at a site distinct from the active site of the 5-phosphatases.


Pssm-ID: 197308 [Multi-domain]  Cd Length: 299  Bit Score: 243.01  E-value: 2.48e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 363 KDCMKSRQSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVS--PVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSG 440
Cdd:cd09074   66 QEALNEKENYVLLGSAQLVGIFLFVFVKKEHLPQIKDLEVEgvTVGTGGGGKLGNKGGVAIRFQINDTSFCFVNSHLAAG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 441 hkDGDKQRRNSDVYEILRRTQFSSVIDADQPetIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELR 520
Cdd:cd09074  146 --QEEVERRNQDYRDILSKLKFYRGDPAIDS--IFDHDVVFWFGDLNYRIDSTDDEVRKLISQGDLDDLLEKDQLKKQKE 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 521 SGHVFEGWKEGVIDFPPTYKYEINSDRYVgenpkEGEKKRSPAWCDRILW---LGKGIKQLCYNRAE-IRVSDHRPVSSN 596
Cdd:cd09074  222 KGKVFDGFQELPITFPPTYKFDPGTDEYD-----TSDKKRIPAWCDRILYkskAGSEIQPLSYTSVPlYKTSDHKPVRAT 296


                 ...
gi 359474593 597 FMV 599
Cdd:cd09074  297 FRV 299
INPP5c_ScInp51p-like cd09090
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae ...
 363-597 3.47e-68

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Saccharomyces cerevisiae Inp51p, Inp52p, and Inp53p, and related proteins; This subfamily contains the INPP5c domain of three Saccharomyces cerevisiae synaptojanin-like inositol polyphosphate 5-phosphatases (INP51, INP52, and INP53), Schizosaccharomyces pombe synaptojanin (SPsynaptojanin), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. In addition to this INPP5c domain, these proteins have an N-terminal catalytic Sac1-like domain (found in other proteins including the phophoinositide phosphatase Sac1p), and a C-terminal proline-rich domain (PRD). The Sac1 domain allows Inp52p and Inp53p to recognize and dephosphorylate a wider range of substrates including PI3P, PI4P, and PI(3,5)P2. The Sac1 domain of Inp51p is non-functional. Disruption of any two of INP51, INP52, and INP53, in S. cerevisiae leads to abnormal vacuolar and plasma membrane morphology. During hyperosmotic stress, Inp52p and Inp53p localize at actin patches, where they may facilitate the hydrolysis of PI(4,5)P2, and consequently promote actin rearrangement to regulate cell growth. SPsynaptojanin is also active against a range of soluble and lipid inositol phosphates, including I(1,4,5)P3, I(1,3,4,5)P4, I(1,4,5,6)P4, PI(4,5)P2, and PIP3. Transformation of S. cerevisiae with a plasmid expressing the SPsynaptojanin 5-phosphatase domain rescues inp51/inp52/inp53 triple-mutant strains.


Pssm-ID: 197324  Cd Length: 291  Bit Score: 223.76  E-value: 3.47e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 363 KDCMKSRQS--YVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSG 440
Cdd:cd09090   66 KTTLNGRGGekYVLLRSEQLVGTALLFFVKESQLPKVKNVEGSTKKTGLGGMSGNKGAVAIRFDYGDTSFCFVTSHLAAG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 441 HKDGDKqrRNSDVYEILRRTQFSsvidadQPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELR 520
Cdd:cd09090  146 LTNYEE--RNNDYKTIARGLRFS------RGRTIKDHDHVIWLGDFNYRISLTNEDVRRFILNGKLDKLLEYDQLNQQMN 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 359474593 521 SGHVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQLCYNRAEIRVSDHRPVSSNF 597
Cdd:cd09090  218 AGEVFPGFSEGPITFPPTYKYDKGTDNY-----DTSEKQRIPAWTDRILYRGENLRQLSYNSAPLRFSDHRPVYATF 289
INPP5c_Synj cd09089
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This ...
 370-593 3.23e-65

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanins; This subfamily contains the INPP5c domains of two human synaptojanins, synaptojanin 1 (Synj1) and synaptojanin 2 (Synj2), and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs). They belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, Synjs contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25 (a mitochondrial outer membrane protein). Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197323 [Multi-domain]  Cd Length: 328  Bit Score: 217.26  E-value: 3.23e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 370 QSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDgdKQRR 449
Cdd:cd09089   92 HKYVLLTSEQLVGVCLFVFVRPQHAPFIRDVAVDTVKTGLGGAAGNKGAVAIRFLLHSTSLCFVCSHFAAGQSQ--VKER 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 450 NSDVYEILRRTQFSSvidadqPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEGWK 529
Cdd:cd09089  170 NEDFAEIARKLSFPM------GRTLDSHDYVFWCGDFNYRIDLPNDEVKELVRNGDWLKLLEFDQLTKQKAAGNVFKGFL 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 530 EGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW---------------------LGKGiKQLCYNRAEIRVS 588
Cdd:cd09089  244 EGEINFAPTYKYDLFSDDY-----DTSEKCRTPAWTDRVLWrrrkwpsdkteeslvetndptWNPG-TLLYYGRAELKTS 317


                 ....*
gi 359474593 589 DHRPV 593
Cdd:cd09089  318 DHRPV 322
IPPc smart00128
Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+) ...
 364-601 5.49e-65

Inositol polyphosphate phosphatase, catalytic domain homologues; Mg(2+)-dependent/Li(+)-sensitive enzymes.


Pssm-ID: 214525 [Multi-domain]  Cd Length: 306  Bit Score: 215.68  E-value: 5.49e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   364 DCMKSRQSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGhkD 443
Cdd:smart00128  73 SSLNGDGQYNVLAKVYLVGILVLVFVKANHLVYIKDVETFTVKTGMGGLWGNKGAVAVRFKLSDTSFCFVNSHLAAG--A 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   444 GDKQRRNSDVYEILRRTQFSsvidADQPETIPSHDQIFWFGDLNYRLNMLDAE-IRKLVARKKWDELINSDQLSKELRSG 522
Cdd:smart00128 151 SNVEQRNQDYKTILRALSFP----ERALLSQFDHDVVFWFGDLNFRLDSPSYEeVRRKISKKEFDDLLEKDQLNRQREAG 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593   523 HVFEGWKEGVIDFPPTYKYE-INSDRYVGenpkeGEKKRSPAWCDRILW--LGKGIKQLC--YNRAEIRVSDHRPVSSNF 597
Cdd:smart00128 227 KVFKGFQEGPITFPPTYKYDsVGTETYDT-----SEKKRVPAWCDRILYrsNGPELIQLSeyHSGMEITTSDHKPVFATF 301


                   ....
gi 359474593   598 MVEV 601
Cdd:smart00128 302 RLKV 305
INPP5c_INPP5J-like cd09094
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate ...
 357-597 1.55e-52

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of inositol polyphosphate 5-phosphatase J and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase J (INPP5J), also known as PIB5PA or PIPP, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5J hydrolyzes PI(4,5)P2, I(1,4,5)P3, and I(1,3,4,5)P4 at ruffling membranes. These proteins contain a C-terminal, SKIP carboxyl homology domain (SKICH), which may direct plasma membrane ruffle localization.


Pssm-ID: 197328  Cd Length: 300  Bit Score: 182.57  E-value: 1.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 357 FKDGENKDCMK--SRQSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVC 434
Cdd:cd09094   55 FDDPWSDLFMDilSPKGYVKVSSIRLQGLLLLVFVKIQHLPFIRDVQTNYTRTGLGGYWGNKGAVTVRFSLYGHMICFLN 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 435 SHLTSgHKDGDKQRRNsDVYEILRRTQFssviDADQPETIPSHDQIFWFGDLNYRLNMLDAE-IRKLVARKKWDELINSD 513
Cdd:cd09094  135 CHLPA-HMEKWEQRID-DFETILSTQVF----NECNTPSILDHDYVFWFGDLNFRIEDVSIEfVRELVNSKKYHLLLEKD 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 514 QLSKELRSGHVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW----------LGKGIKQLCYN-R 582
Cdd:cd09094  209 QLNMAKRKEEAFQGFQEGPLNFAPTYKFDLGTDEY-----DTSGKKRKPAWTDRILWkvnpdasteeKFLSITQTSYKsH 283

                        250
                 ....*....|....*
gi 359474593 583 AEIRVSDHRPVSSNF 597
Cdd:cd09094  284 MEYGISDHKPVTAQF 298
INPP5c_Synj1 cd09098
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This ...
 370-593 3.01e-52

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 1; This subfamily contains the INPP5c domains of human synaptojanin 1 (Synj1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj1 occurs as two main isoforms: a brain enriched 145 KDa protein (Synj1-145) and a ubiquitously expressed 170KDa protein (Synj1-170). Synj1-145 participates in clathrin-mediated endocytosis. The primary substrate of the Synj1-145 INPP5c domain is PI(4,5)P2, which it converts to PI4P. Synj1-145 may work with membrane curvature sensors/generators (such as endophilin) to remove PI(4,5)P2 from curved membranes. The recruitment of the INPP5c domain of Synj1-145 to endophilin-induced membranes leads to a fragmentation and condensation of these structures. The PI(4,5)P2 to PI4P conversion may cooperate with dynamin to produce membrane fission. In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro.


Pssm-ID: 197332  Cd Length: 336  Bit Score: 182.93  E-value: 3.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 370 QSYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDgdKQRR 449
Cdd:cd09098   91 QKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQ--VKER 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 450 NSDVYEILRRTQFSsvidadQPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEGWK 529
Cdd:cd09098  169 NEDFIEIARKLSFP------MGRMLFSHDYVFWCGDFNYRIDIPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFL 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 530 EGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILW------LGKGIKQL-----------------------CY 580
Cdd:cd09098  243 EGKLDFAPTYKYDLFSDDY-----DTSEKCRTPAWTDRVLWrrrkwpFDRSAEDLdllnasfpdnskeqytwspgtllHY 317

                        250
                 ....*....|...
gi 359474593 581 NRAEIRVSDHRPV 593
Cdd:cd09098  318 GRAELKTSDHRPV 330
INPP5c_Synj2 cd09099
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This ...
 372-601 6.67e-48

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of synaptojanin 2; This subfamily contains the INPP5c domains of human synaptojanin 2 (Synj2) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Synj2 can hydrolyze phosphatidylinositol diphosphate (PIP2) to phosphatidylinositol phosphate (PIP). In addition to this INPP5c domain, these proteins contain an N-terminal Sac1-like domain; the Sac1 domain can dephosphorylate a variety of phosphoinositides in vitro. Synj2 occurs as multiple alternative splice variants in various tissues. These variants share the INPP5c domain and the Sac1 domain. Synj2A is recruited to the mitochondria via its interaction with OMP25, a mitochondrial outer membrane protein. Synj2B is found at nerve terminals in the brain and at the spermatid manchette in testis. Synj2B undergoes further alternative splicing to give 2B1 and 2B2. In clathrin-mediated endocytosis, Synj2 participates in the formation of clathrin-coated pits, and perhaps also in vesicle decoating. Rac1 GTPase regulates the intracellular localization of Synj2 forms, but not Synj1. Synj2 may contribute to the role of Rac1 in cell migration and invasion, and is a potential target for therapeutic intervention in malignant tumors.


Pssm-ID: 197333  Cd Length: 336  Bit Score: 170.97  E-value: 6.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 372 YVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDgdKQRRNS 451
Cdd:cd09099   93 YILLTSAQLVGVCLFIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVAIRFQFYSTSFCFICSHLTAGQNQ--VKERNE 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 452 DVYEILRRTQFSSvidadqPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEGWKEG 531
Cdd:cd09099  171 DYKEITQKLSFPM------GRNVFSHDYVFWCGDFNYRIDLTYEEVFYFIKRQDWKKLLEFDQLQLQKSSGKIFKDFHEG 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 532 VIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGK----------------------GIKQ-------LCYNR 582
Cdd:cd09099  245 TINFGPTYKYDVGSEAY-----DTSDKCRTPAWTDRVLWWRKkwpfektageinlldsdldfdtKIRHtwtpgalMYYGR 319

                        250
                 ....*....|....*....
gi 359474593 583 AEIRVSDHRPVSSnfMVEV 601
Cdd:cd09099  320 AELQASDHRPVLA--IVEV 336
COG5411 COG5411
Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];
348-609 7.95e-47

Phosphatidylinositol 5-phosphate phosphatase [Signal transduction mechanisms];


Pssm-ID: 227698 [Multi-domain]  Cd Length: 460  Bit Score: 171.50  E-value: 7.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 348 SLIEIPEHQFKDGENKDCMKSRQS---YVRIVSKQMVGIYISVWVRKRlrrhiNNLKVSPVG-----VGLMGYMGNKGSV 419
Cdd:COG5411   82 SADPYDRLRIWESKVLDCLNGAQSdekYSLLRSPQLGGILLRVFSLAT-----NLPVVKPVSgtvkkTGFGGSSSNKGAV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 420 SVSMSVFQTRICFVCSHLTSGHKDGDKqrRNSDVYEILRRTQFSSvidadqPETIPSHDQIFWFGDLNYRLNMLDAEIRK 499
Cdd:COG5411  157 AIRFNYERTSFCFVNSHLAAGVNNIEE--RIFDYRSIASNICFSR------GLRIYDHDTIFWLGDLNYRVTSTNEEVRP 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 500 LVARKKW--DELINSDQLSKELRSGHVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGKGIKQ 577
Cdd:COG5411  229 EIASDDGrlDKLFEYDQLLWEMEVGNVFPGFKEPVITFPPTYKFDYGTDEY-----DTSDKGRIPSWTDRILYKSEQLTP 303

                        250       260       270
                 ....*....|....*....|....*....|...
gi 359474593 578 LCYNRAE-IRVSDHRPVSSNFMVEVEVFDHRKL 609
Cdd:COG5411  304 HSYSSIPhLMISDHRPVYATFRAKIKVVDPSKK 336
INPP5c_INPP5E-like cd09095
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol ...
 371-599 1.52e-37

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of Inositol polyphosphate-5-phosphatase E and related proteins; INPP5c domain of Inositol polyphosphate-5-phosphatase E (also called type IV or 72 kDa 5-phosphatase), rat pharbin, and related proteins. This subfamily belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. INPP5E hydrolyzes the 5-phosphate from PI(3,5)P2, PI(4,5)P2 and PI(3,4,5)P3, forming PI3P, PI4P, and PI(3,4)P2, respectively. It is a very potent PI(3,4,5)P3 5-phosphatase. Its intracellular localization is chiefly cytosolic, with pronounced perinuclear/Golgi localization. INPP5E also has an N-terminal proline rich domain (PRD) and a C-terminal CAAX motif. This protein is expressed in a variety of tissues, including the breast, brain, testis, and haemopoietic cells. It is differentially expressed in several cancers, for example, it is up-regulated in cervical cancer and down-regulated in stomach cancer. It is a candidate target for therapeutics of obesity and related disorders, as it is expressed in the hypothalamus, and following insulin stimulation, it undergoes tyrosine phosphorylation, associates with insulin receptor substrate-1, -2, and PI3-kinase, and become active as a 5-phosphatase. INPP5E may play a role, along with other 5-phosphatases SHIP2 and SKIP, in regulating glucose homoeostasis and energy metabolism. Mice deficient in INPPE5 develop a multi-organ disorder associated with structural defects of the primary cilium.


Pssm-ID: 197329  Cd Length: 298  Bit Score: 141.41  E-value: 1.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 371 SYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHkdGDKQRRN 450
Cdd:cd09095   65 SHVLLHSASHGVLHLAVFIRRDLIWFCSEVESATVTTRIVSQIKTKGALAISFTFFGTSFLFITSHFTSGD--GKVKERV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 451 SDVYEI-----LRRTQFSSVIDADQPETIPSHDQIFWFGDLNYRLNMLDAEIRKLVARKK---WDELINSDQLSKELRSG 522
Cdd:cd09095  143 LDYNKIiqalnLPRNVPTNPYKSESGDVTTRFDEVFWFGDFNFRLSGPRHLVDALINQGQevdVSALLQHDQLTREMSKG 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 523 HVFEGWKEGVIDFPPTYKYEINSDRYvgenpKEGEKKRSPAWCDRILWLGK---GIKQLCYNRAE-IRVSDHRPVSSNFM 598
Cdd:cd09095  223 SIFKGFQEAPIHFPPTYKFDIGSDVY-----DTSSKQRVPSYTDRILYRSRqkgDVCCLKYNSCPsIKTSDHRPVFALFR 297


                 .
gi 359474593 599 V 599
Cdd:cd09095  298 V 298
INPP5c_SHIP2-INPPL1 cd09101
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 372-599 1.54e-35

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol 5-phosphatase-2 and related proteins; This subfamily contains the INPP5c domain of SHIP2 (SH2 domain containing inositol 5-phosphatase-2, also called INPPL1) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP2 catalyzes the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. SHIP2 is an inhibitor of the insulin signaling pathway. It is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. Its interacting partners include filamin/actin, p130Cas, Shc, Vinexin, Interesectin 1, and c-Jun NH2-terminal kinase (JNK)-interacting protein 1 (JIP1). A large variety of extracellular stimuli appear to lead to the tyrosine phosphorylation of SHIP2, including epidermal growth factor (EGF), platelet-derived growth factor (PDGF), insulin, macrophage colony-stimulating factor (M-CSF) and hepatocyte growth factor (HGF). SHIP2 is localized to the cytosol in quiescent cells; following growth factor stimulation and /or cell adhesion, it relocalizes to membrane ruffles. In addition to this INPP5c domain, SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate for conferring a predisposition for type 2 diabetes; it has been suggested that suppression of SHIP2 may be of benefit in the treatment of obesity and thereby prevent type 2 diabetes. SHIP2 and SHIP1 have little overlap in their in vivo functions.


Pssm-ID: 197335  Cd Length: 304  Bit Score: 135.87  E-value: 1.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 372 YVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKDgdKQRRNS 451
Cdd:cd09101   74 YQPIALQCLWNIKMVVLVKPEHENRISHVHTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEK--THRRNQ 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 452 DVYEILRRTQFS----SVIDADQPETipshdQIFWFGDLNYRLNMLDAEIRKLVARKKWDELINSDQLSKELRSGHVFEG 527
Cdd:cd09101  152 NYLDILRSLSLGdkqlNAFDISLRFT-----HLFWFGDLNYRLDMDIQEILNYITRKEFDPLLAVDQLNLEREKNKVFLR 226

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 359474593 528 WKEGVIDFPPTYKYEINS-DRYVGENPK-EGEKKRSPAWCDRILWLGKGIKQLCYNR----AEIRVSDHRPVSSNFMV 599
Cdd:cd09101  227 FREEEISFPPTYRYERGSrDTYMWQKQKtTGMRTNVPSWCDRILWKSYPETHIVCNSygctDDIVTSDHSPVFGTFEV 304
INPP5c_SHIP cd09091
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 346-599 1.88e-35

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and -2, and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D), and SHIP2 (also known as INPPL1). It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. Both SHIP1 and -2 catalyze the dephosphorylation of the PI, phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3], to phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2]. SHIP1 also converts inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4] to inositol-1,3,4-polyphosphate [I(1,3,4)P3]. SHIP1 and SHIP2 have little overlap in their in vivo functions. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. SHIP2 is as an inhibitor of the insulin signaling pathway, and is implicated in actin structure remodeling, cell adhesion and cell spreading, receptor endocytosis and degradation, and in the JIP1-mediated JNK pathway. SHIP2 is widely expressed, most prominently in brain, heart and in skeletal muscle. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD), while SHIP2 has an N-terminal SH2 domain, a C-terminal proline-rich domain (PRD), which includes a WW-domain binding motif (PPLP), an NPXY motif, and a sterile alpha motif (SAM) domain. The gene encoding SHIP2 is a candidate gene for conferring a predisposition for type 2 diabetes.


Pssm-ID: 197325  Cd Length: 307  Bit Score: 135.84  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 346 DESLIEIPEHQFKDGENKDCMKSRQ---------------SYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLM 410
Cdd:cd09091   33 DDVADYIPHDIYVIGTQEDPLGEKEwldllrhslkeltslDYKPIAMQTLWNIRIVVLAKPEHENRISHVCTSSVKTGIA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 411 GYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKdgDKQRRNSDVYEILRrtqFSSVIDADQPETIPSH--DQIFWFGDLNY 488
Cdd:cd09091  113 NTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSE--KKLRRNQNYLNILR---FLSLGDKKLSAFNITHrfTHLFWLGDLNY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 489 RLNMLDAEIRKLVARKK---WDELINSDQLSKELRSGHVFEGWKEGVIDFPPTYKYEINS-DRYVGENPK-EGEKKRSPA 563
Cdd:cd09091  188 RLDLPIQEAENIIQKIEqqqFEPLLRHDQLNLEREEHKVFLRFSEEEITFPPTYRYERGSrDTYAYTKQKaTGVKYNLPS 267

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 359474593 564 WCDRILWlgKGIKQ---LCYNRA---EIRVSDHRPVSSNFMV 599
Cdd:cd09091  268 WCDRILW--KSYPEthiICQSYGctdDIVTSDHSPVFGTFEV 307
INPP5c_SHIP1-INPP5D cd09100
Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing ...
 371-599 2.30e-31

Catalytic inositol polyphosphate 5-phosphatase (INPP5c) domain of SH2 domain containing inositol polyphosphate 5-phosphatase-1 and related proteins; This subfamily contains the INPP5c domain of SHIP1 (SH2 domain containing inositol polyphosphate 5-phosphatase-1, also known as SHIP/INPP5D) and related proteins. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. SHIP1's enzymic activity is restricted to phosphatidylinositol 3,4,5-trisphosphate [PI (3,4,5)P3] and inositol-1,3,4,5- polyphosphate [I(1,3,4,5)P4]. It converts these two phosphoinositides to phosphatidylinositol 3,4-bisphosphate [PI (3,4)P2] and inositol-1,3,4-polyphosphate [I(1,3,4)P3], respectively. SHIP1 is a negative regulator of cell growth and plays a major part in mediating the inhibitory signaling in B cells; it is predominantly expressed in hematopoietic cells. In addition to this INPP5c domain, SHIP1 has an N-terminal SH2 domain, two NPXY motifs, and a C-terminal proline-rich region (PRD). SHIP1's phosphorylated NPXY motifs interact with proteins with phosphotyrosine binding (PTB) domains, and facilitate the translocation of SHIP1 to the plasma membrane to hydrolyze PI(3,4,5)P3. SHIP1 generally acts to oppose the activity of phosphatidylinositol 3-kinase (PI3K). It acts as a negative signaling molecule, reducing the levels of PI(3,4,5)P3, thereby removing the latter as a membrane-targeting signal for PH domain-containing effector molecules. SHIP1 may also, in certain contexts, amplify PI3K signals. SHIP1 and SHIP2 have little overlap in their in vivo functions.


Pssm-ID: 197334  Cd Length: 307  Bit Score: 124.33  E-value: 2.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 371 SYVRIVSKQMVGIYISVWVRKRLRRHINNLKVSPVGVGLMGYMGNKGSVSVSMSVFQTRICFVCSHLTSGHKdgDKQRRN 450
Cdd:cd09100   73 SFKVIAIQTLWNIRIVVLAKPEHENRISHICTDSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNSHLTSGSE--KKLRRN 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 451 SDVYEILRrtqFSSVIDADQPETIPSH--DQIFWFGDLNYRLNMLDAEIRKLVAR---KKWDELINSDQLSKELRSGHVF 525
Cdd:cd09100  151 QNYFNILR---FLVLGDKKLSPFNITHrfTHLFWLGDLNYRVELPNTEAENIIQKikqQQYQELLPHDQLLIERKESKVF 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 526 EGWKEGVIDFPPTYKYEINS-DRYVGENPK-EGEKKRSPAWCDRILWlgKGIKQ---LCYN---RAEIRVSDHRPVSSNF 597
Cdd:cd09100  228 LQFEEEEITFAPTYRFERGTrERYAYTKQKaTGMKYNLPSWCDRVLW--KSYPLvhvVCQSygcTDDITTSDHSPVFATF 305


                 ..
gi 359474593 598 MV 599
Cdd:cd09100  306 EV 307
INPP5A cd09092
Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I ...
 450-607 3.94e-05

Type I inositol polyphosphate 5-phosphatase I; Type I inositol polyphosphate 5-phosphatase I (INPP5A) hydrolyzes the 5-phosphate from inositol 1,3,4,5-tetrakisphosphate [I(1,3,4,5)P4] and inositol 1,4,5-trisphosphate [I(1,4,5)P3]. It belongs to a family of Mg2+-dependent inositol polyphosphate 5-phosphatases, which hydrolyze the 5-phosphate from the inositol ring of various 5-position phosphorylated phosphoinositides (PIs) and inositol phosphates (IPs), and to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. As the substrates of INPP5A mobilize intracellular calcium ions, INPP5A is a calcium signal-terminating enzyme. In platelets, phosphorylated pleckstrin binds and activates INPP5A in a 1:1 complex, and accelerates the degradation of the calcium ion-mobilizing I(1,4,5)P3.


Pssm-ID: 197326  Cd Length: 383  Bit Score: 46.31  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 450 NSDVYEILRRTQFSSVID---ADQPETIPShdqiFWFGDLNYRLNMLdAEIRKLVAR------KKWDELINSDQLSKELR 520
Cdd:cd09092  189 SPSVYSQNRHRALGYVLErltDERFEKVPF----FVFGDFNFRLDTK-SVVETLCAKatmqtvRKADSNIVVKLEFREKD 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 359474593 521 SGHV--------------------------------FEGWK----EGVIDFPPTYKYEinsdryvgENPKEGE---KKRS 561
Cdd:cd09092  264 NDNKvvlqiekkkfdyfnqdvfrdnngkallkfdkeLEVFKdvlyELDISFPPSYPYS--------EDPEQGTqymNTRC 335

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 359474593 562 PAWCDRILwLGKGIKQLcynraEIRVSDHRPVSSNFMVEVEVFDHR 607
Cdd:cd09092  336 PAWCDRIL-MSHSAREL-----KSENEEKSVTYDMIGPNVCMGDHK 375
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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