NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2449299893|ref|XP_053656263|]
View 

LOW QUALITY PROTEIN: uncharacterized protein LOC128705033 [Cherax quadricarinatus]

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
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 10-215 1.58e-14

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 79.45  E-value: 1.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   10 KNTLNVLLNKHEVLKEANQ--VTEHGEQDVEHG-EQDVEHG-EQDVEHG-EQDVEHG-EQDVEHG-EQNVEHKQDvEHGE 82
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEanIEEDAEENVEEDaEENVEENvEENVEENvEENVEENvEENVEENvEENVEENVE-ENIE 1004

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   83 QDVELGEQDAEHEQDVEHGEQDVEHGEQDVE-HGEQDVEHGEQDVEH------EQDVE-HGEQDVEHGEQDVEH--EQNV 152
Cdd:PTZ00341  1005 ENVEENVEENIEENVEEYDEENVEEVEENVEeYDEENVEEIEENAEEnveeniEENIEeYDEENVEEIEENIEEniEENV 1084

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449299893  153 EhgeqdvEHGEQDVEHGEQDVergEQDVEhgEQNTEHVEPAVEHGEQAINNREQEEQDIEHGE 215
Cdd:PTZ00341  1085 E------ENVEENVEEIEENV---EENVE--ENAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 402-501 9.63e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


:

Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 66.03  E-value: 9.63e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   402 FSTWKRYYFTLNGRLLTYYKPqrhyqdpggqqgSPSGPQSGPKGVLDLDFLLQVTVGRRGIMKANYPFKLTCKNLPSVKL 481
Cdd:smart00233   15 KKSWKKRYFVLFNSTLLYYKS------------KKDKKSYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTSDRKTLLL 82

                            90       100
                    ....*....|....*....|
gi 2449299893   482 AAETSEDREKWVRILQDVLQ 501
Cdd:smart00233   83 QAESEEEREKWVEALRKAIA 102
2A1904 super family cl36772
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 111-374 1.68e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR00927:

Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 49.99  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  111 DVEHGEQDVEHGEQDVEHEQDVEhGEQDVEHGEQDVEHEQNVEHGEQDVEhGEQDVEHGEQDVERGEQDVEHGEQNTEHV 190
Cdd:TIGR00927  634 DVAEAEHTGERTGEEGERPTEAE-GENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEADHKGETE 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  191 EPAVEHGEQAINNREQEEQDIEHGEQAiqntadssdttRKTEQRNNSNKQGKRERQQEiRDIRETRSNKEEAKMDKNGNK 270
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEGEIETGEEG-----------EEVEDEGEGEAEGKHEVETE-GDRKETEHEGETEAEGKEDED 779

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  271 KAeESHRKEEIDQKGD------INSPNEGGSGRKSNKRGNKGTVKDKDGrTRETEQTEEQKEREQGEIKQGDKKSSERER 344
Cdd:TIGR00927  780 EG-EIQAGEDGEMKGDegaegkVEHEGETEAGEKDEHEGQSETQADDTE-VKDETGEQELNAENQGEAKQDEKGVDGGGG 857

                          250       260       270
                   ....*....|....*....|....*....|
gi 2449299893  345 GNREERIKTRERDKNNTEQKEHKSQKKTEQ 374
Cdd:TIGR00927  858 SDGGDSEEEEEEEEEEEEEEEEEEEEEEEE 887
 
Name Accession Description Interval E-value
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 10-215 1.58e-14

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 79.45  E-value: 1.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   10 KNTLNVLLNKHEVLKEANQ--VTEHGEQDVEHG-EQDVEHG-EQDVEHG-EQDVEHG-EQDVEHG-EQNVEHKQDvEHGE 82
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEanIEEDAEENVEEDaEENVEENvEENVEENvEENVEENvEENVEENvEENVEENVE-ENIE 1004

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   83 QDVELGEQDAEHEQDVEHGEQDVEHGEQDVE-HGEQDVEHGEQDVEH------EQDVE-HGEQDVEHGEQDVEH--EQNV 152
Cdd:PTZ00341  1005 ENVEENVEENIEENVEEYDEENVEEVEENVEeYDEENVEEIEENAEEnveeniEENIEeYDEENVEEIEENIEEniEENV 1084

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449299893  153 EhgeqdvEHGEQDVEHGEQDVergEQDVEhgEQNTEHVEPAVEHGEQAINNREQEEQDIEHGE 215
Cdd:PTZ00341  1085 E------ENVEENVEEIEENV---EENVE--ENAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 402-501 9.63e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 66.03  E-value: 9.63e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   402 FSTWKRYYFTLNGRLLTYYKPqrhyqdpggqqgSPSGPQSGPKGVLDLDFLLQVTVGRRGIMKANYPFKLTCKNLPSVKL 481
Cdd:smart00233   15 KKSWKKRYFVLFNSTLLYYKS------------KKDKKSYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTSDRKTLLL 82

                            90       100
                    ....*....|....*....|
gi 2449299893   482 AAETSEDREKWVRILQDVLQ 501
Cdd:smart00233   83 QAESEEEREKWVEALRKAIA 102
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 40-290 7.40e-11

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 67.33  E-value: 7.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   40 GEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVEL-GEQDAEHEQDVEHGEQDVEHGEQDVEHGEQD 118
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERkGEQEGEGEIEAKEADHKGETEAEEVEHEGET 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  119 VEHGEQDVEHEQDVEHGEQDVEHGEQDVE--HEQNVEHGEQDVEHGEQDVEHGEQDVERGE-QDVEHGE-QNTEHVEPAV 194
Cdd:TIGR00927  722 EAEGTEDEGEIETGEEGEEVEDEGEGEAEgkHEVETEGDRKETEHEGETEAEGKEDEDEGEiQAGEDGEmKGDEGAEGKV 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  195 EHGEQainnrEQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGK-RERQQEIRDIRETRSNKEEAKMDKNGNKKAE 273
Cdd:TIGR00927  802 EHEGE-----TEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEaKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEE 876

                          250
                   ....*....|....*..
gi 2449299893  274 ESHRKEEIDQKGDINSP 290
Cdd:TIGR00927  877 EEEEEEEEEEEEENEEP 893
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 402-500 2.18e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 59.11  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTLNGRLLTYYKPQRHYQDpggqqgspsgpqSGPKGVLDLDFLLQVTVGRRGIMKANYPFKLTCKNLPSVK- 480
Cdd:pfam00169   15 KKSWKKRYFVLFDGSLLYYKDDKSGKS------------KEPKGSISLSGCEVVEVVASDSPKRKFCFELRTGERTGKRt 82

                           90       100
                   ....*....|....*....|..
gi 2449299893  481 --LAAETSEDREKWVRILQDVL 500
Cdd:pfam00169   83 ylLQAESEEERKDWIKAIQSAI 104
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 402-496 3.37e-10

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 58.32  E-value: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTLNGRLLTYYKpqrhyqdpggqqgSPSGPQSGPKGVLDLDFLLQVTVGRRGimKANYPFKLTCKNLPSVKL 481
Cdd:cd00821     13 LKSWKKRWFVLFEGVLLYYK-------------SKKDSSYKPKGSIPLSGILEVEEVSPK--ERPHCFELVTPDGRTYYL 77

                           90
                   ....*....|....*
gi 2449299893  482 AAETSEDREKWVRIL 496
Cdd:cd00821     78 QADSEEERQEWLKAL 92
SMBP pfam16785
Small metal-binding protein; This histidine-rich protein binds metal ions.
 106-200 4.20e-08

Small metal-binding protein; This histidine-rich protein binds metal ions.


Pssm-ID: 407049 [Multi-domain]  Cd Length: 111  Bit Score: 52.74  E-value: 4.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  106 EHGEQDVEHGEQDVEHGEQdveheqdvEHGEQDVEHGEQDVEH---EQNVEHGEQDvEHGEQDVEHGEQDVERGEQdvEH 182
Cdd:pfam16785   25 EHLAEAIEHAEAAVAHGKD--------GHAKALVEHAEEALKHakaAAEKADGEEN-EHLDEGIKHLEEAIKHGKM--GH 93

                           90
                   ....*....|....*...
gi 2449299893  183 GEQNTEHVEPAVEHGEQA 200
Cdd:pfam16785   94 ADAATKHAEEALKHLKQA 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-284 2.95e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   55 EQDVEHGEQDVEHGEQNVEHKQdVEHGEQDVELGEQDAEHEQDvehgEQDVEHGEQDVEHGEQDVEHGEQDVEHEQdveh 134
Cdd:COG1196    238 EAELEELEAELEELEAELEELE-AELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLE---- 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  135 gEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVERGEQDVEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEHG 214
Cdd:COG1196    309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  215 EQAIQNTADSSDTTRKTEQRNNSNKQGKRERQQEIRDIRETRSNKEEAKMDKNGNKKAEESHRKEEIDQK 284
Cdd:COG1196    388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 111-374 1.68e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 49.99  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  111 DVEHGEQDVEHGEQDVEHEQDVEhGEQDVEHGEQDVEHEQNVEHGEQDVEhGEQDVEHGEQDVERGEQDVEHGEQNTEHV 190
Cdd:TIGR00927  634 DVAEAEHTGERTGEEGERPTEAE-GENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEADHKGETE 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  191 EPAVEHGEQAINNREQEEQDIEHGEQAiqntadssdttRKTEQRNNSNKQGKRERQQEiRDIRETRSNKEEAKMDKNGNK 270
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEGEIETGEEG-----------EEVEDEGEGEAEGKHEVETE-GDRKETEHEGETEAEGKEDED 779

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  271 KAeESHRKEEIDQKGD------INSPNEGGSGRKSNKRGNKGTVKDKDGrTRETEQTEEQKEREQGEIKQGDKKSSERER 344
Cdd:TIGR00927  780 EG-EIQAGEDGEMKGDegaegkVEHEGETEAGEKDEHEGQSETQADDTE-VKDETGEQELNAENQGEAKQDEKGVDGGGG 857

                          250       260       270
                   ....*....|....*....|....*....|
gi 2449299893  345 GNREERIKTRERDKNNTEQKEHKSQKKTEQ 374
Cdd:TIGR00927  858 SDGGDSEEEEEEEEEEEEEEEEEEEEEEEE 887
PTZ00121 PTZ00121
MAEBL; Provisional
 188-389 2.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  188 EHVEPAVEHGEQAINNREQEEqdIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGKRErqqEIRDIRETRSNKEEAKMDKn 267
Cdd:PTZ00121  1233 EEAKKDAEEAKKAEEERNNEE--IRKFEEARMAHFARRQAAIKAEEARKADELKKAE---EKKKADEAKKAEEKKKADE- 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  268 GNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVKDKDGRTRETEQTEEQKEREQGEIKQGDKKSSERERGNR 347
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2449299893  348 EERIKTRERDKNNTEQKEHKSQ--KKTEQRTKHKNKTQRNTEHK 389
Cdd:PTZ00121  1387 AEEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEK 1430
SMBP_like cd13840
Small metal-binding protein conserved in proteobacteria; This periplasmic protein appears ...
 106-201 2.38e-04

Small metal-binding protein conserved in proteobacteria; This periplasmic protein appears capable of binding multiple equivalents of a variety of divalent and trivalent metals, including Cu(2+) and Fe(3+) but also Mn(2+), Ni(2+), Mg(2+), and Zn(2+). It has been suggested that SMBP is a metal scavenging protein that plays a role in cellular copper management in Nitrosomonas europaea.


Pssm-ID: 260104  Cd Length: 89  Bit Score: 41.54  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  106 EHGEQDVEHGEQDVEHGeQDVEHEQDVEHGEQDVEHGE--QDVEHEQNvEHGEQDVEHGEQDVEHGEQDvergeqdveHG 183
Cdd:cd13840      3 DHLDEAIEHAEAAITHG-KAGHAKALAEHAEEALKHAKaaEKEKAEAK-KHLDEAIKHLEEAIKHGKMG---------HA 71

                           90
                   ....*....|....*...
gi 2449299893  184 EQNTEHVEPAVEHGEQAI 201
Cdd:cd13840     72 DVATKHAEEALKHLKAAN 89
 
Name Accession Description Interval E-value
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 10-215 1.58e-14

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 79.45  E-value: 1.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   10 KNTLNVLLNKHEVLKEANQ--VTEHGEQDVEHG-EQDVEHG-EQDVEHG-EQDVEHG-EQDVEHG-EQNVEHKQDvEHGE 82
Cdd:PTZ00341   926 KELKNQNENVPEHLKEHAEanIEEDAEENVEEDaEENVEENvEENVEENvEENVEENvEENVEENvEENVEENVE-ENIE 1004

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   83 QDVELGEQDAEHEQDVEHGEQDVEHGEQDVE-HGEQDVEHGEQDVEH------EQDVE-HGEQDVEHGEQDVEH--EQNV 152
Cdd:PTZ00341  1005 ENVEENVEENIEENVEEYDEENVEEVEENVEeYDEENVEEIEENAEEnveeniEENIEeYDEENVEEIEENIEEniEENV 1084

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449299893  153 EhgeqdvEHGEQDVEHGEQDVergEQDVEhgEQNTEHVEPAVEHGEQAINNREQEEQDIEHGE 215
Cdd:PTZ00341  1085 E------ENVEENVEEIEENV---EENVE--ENAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 402-501 9.63e-13

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 66.03  E-value: 9.63e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   402 FSTWKRYYFTLNGRLLTYYKPqrhyqdpggqqgSPSGPQSGPKGVLDLDFLLQVTVGRRGIMKANYPFKLTCKNLPSVKL 481
Cdd:smart00233   15 KKSWKKRYFVLFNSTLLYYKS------------KKDKKSYKPKGSIDLSGCTVREAPDPDSSKKPHCFEIKTSDRKTLLL 82

                            90       100
                    ....*....|....*....|
gi 2449299893   482 AAETSEDREKWVRILQDVLQ 501
Cdd:smart00233   83 QAESEEEREKWVEALRKAIA 102
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 40-290 7.40e-11

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 67.33  E-value: 7.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   40 GEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVEL-GEQDAEHEQDVEHGEQDVEHGEQDVEHGEQD 118
Cdd:TIGR00927  642 GERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAERkGEQEGEGEIEAKEADHKGETEAEEVEHEGET 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  119 VEHGEQDVEHEQDVEHGEQDVEHGEQDVE--HEQNVEHGEQDVEHGEQDVEHGEQDVERGE-QDVEHGE-QNTEHVEPAV 194
Cdd:TIGR00927  722 EAEGTEDEGEIETGEEGEEVEDEGEGEAEgkHEVETEGDRKETEHEGETEAEGKEDEDEGEiQAGEDGEmKGDEGAEGKV 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  195 EHGEQainnrEQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGK-RERQQEIRDIRETRSNKEEAKMDKNGNKKAE 273
Cdd:TIGR00927  802 EHEGE-----TEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEaKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEE 876

                          250
                   ....*....|....*..
gi 2449299893  274 ESHRKEEIDQKGDINSP 290
Cdd:TIGR00927  877 EEEEEEEEEEEEENEEP 893
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 402-500 2.18e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 59.11  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTLNGRLLTYYKPQRHYQDpggqqgspsgpqSGPKGVLDLDFLLQVTVGRRGIMKANYPFKLTCKNLPSVK- 480
Cdd:pfam00169   15 KKSWKKRYFVLFDGSLLYYKDDKSGKS------------KEPKGSISLSGCEVVEVVASDSPKRKFCFELRTGERTGKRt 82

                           90       100
                   ....*....|....*....|..
gi 2449299893  481 --LAAETSEDREKWVRILQDVL 500
Cdd:pfam00169   83 ylLQAESEEERKDWIKAIQSAI 104
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 402-496 3.37e-10

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 58.32  E-value: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTLNGRLLTYYKpqrhyqdpggqqgSPSGPQSGPKGVLDLDFLLQVTVGRRGimKANYPFKLTCKNLPSVKL 481
Cdd:cd00821     13 LKSWKKRWFVLFEGVLLYYK-------------SKKDSSYKPKGSIPLSGILEVEEVSPK--ERPHCFELVTPDGRTYYL 77

                           90
                   ....*....|....*
gi 2449299893  482 AAETSEDREKWVRIL 496
Cdd:cd00821     78 QADSEEERQEWLKAL 92
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 25-281 4.45e-10

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 65.02  E-value: 4.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   25 EANQVTEhGEQDvEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQnvEHKQDVEHGEQDVElGEQDAEHEQDVEHGEQD 104
Cdd:TIGR00927  650 ERPTEAE-GENG-EESGGEAEQEGETETKGENESEGEIPAERKGEQ--EGEGEIEAKEADHK-GETEAEEVEHEGETEAE 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  105 VEHGEQDVEHGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVE---HGEQDVEHgeQDVERGEQDVE 181
Cdd:TIGR00927  725 GTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEgeiQAGEDGEM--KGDEGAEGKVE 802

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  182 HGEQNTEHVEpaVEHGEQAINNREQEEQDIEHGEQAI--QNTADSSDTTRKTEQRNNSNKQGKRERQQEIRDIRETRSNK 259
Cdd:TIGR00927  803 HEGETEAGEK--DEHEGQSETQADDTEVKDETGEQELnaENQGEAKQDEKGVDGGGGSDGGDSEEEEEEEEEEEEEEEEE 880

                          250       260
                   ....*....|....*....|....*..
gi 2449299893  260 EEAKMDKNGNKKA-----EESHRKEEI 281
Cdd:TIGR00927  881 EEEEEEEEENEEPlslewPETRQKQAI 907
SMBP pfam16785
Small metal-binding protein; This histidine-rich protein binds metal ions.
 106-200 4.20e-08

Small metal-binding protein; This histidine-rich protein binds metal ions.


Pssm-ID: 407049 [Multi-domain]  Cd Length: 111  Bit Score: 52.74  E-value: 4.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  106 EHGEQDVEHGEQDVEHGEQdveheqdvEHGEQDVEHGEQDVEH---EQNVEHGEQDvEHGEQDVEHGEQDVERGEQdvEH 182
Cdd:pfam16785   25 EHLAEAIEHAEAAVAHGKD--------GHAKALVEHAEEALKHakaAAEKADGEEN-EHLDEGIKHLEEAIKHGKM--GH 93

                           90
                   ....*....|....*...
gi 2449299893  183 GEQNTEHVEPAVEHGEQA 200
Cdd:pfam16785   94 ADAATKHAEEALKHLKQA 111
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
 402-501 9.65e-07

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241436  Cd Length: 96  Bit Score: 48.45  E-value: 9.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTL-NGRLLtYYKpqrhyqdpggqqgSPSGPQSGPKGVLDLDfllqvTVGRRGIMKANYPFKLTCKNlPSVK 480
Cdd:cd13282     12 VKTWKRRWFVLkNGELF-YYK-------------SPNDVIRKPQGQIALD-----GSCEIARAEGAQTFEIVTEK-RTYY 71

                           90       100
                   ....*....|....*....|.
gi 2449299893  481 LAAETSEDREKWVRILQDVLQ 501
Cdd:cd13282     72 LTADSENDLDEWIRVIQNVLR 92
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 73-334 1.84e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 53.08  E-value: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   73 EHKQDVEHGEQDVEL---GEQDAEHEQDVEHGEQDVEHGEQDVEhGEQDVEhGEQDVEHEQDVEHGEQDVEhGEQDVEHE 149
Cdd:TIGR00927  639 EHTGERTGEEGERPTeaeGENGEESGGEAEQEGETETKGENESE-GEIPAE-RKGEQEGEGEIEAKEADHK-GETEAEEV 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  150 QNVEHGEQDVEHGEQDVEHGEQDVERGEQDvEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEHGEQAIQNTADSsdttr 229
Cdd:TIGR00927  716 EHEGETEAEGTEDEGEIETGEEGEEVEDEG-EGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDG----- 789

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  230 ktEQRNNSNKQGKRERQQEIRDIRETRSNKEEAKMDKNGNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVK 309
Cdd:TIGR00927  790 --EMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEEEE 867

                          250       260
                   ....*....|....*....|....*
gi 2449299893  310 DKDGRTRETEQTEEQKEREQGEIKQ 334
Cdd:TIGR00927  868 EEEEEEEEEEEEEEEEEEEEEENEE 892
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-284 2.95e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   55 EQDVEHGEQDVEHGEQNVEHKQdVEHGEQDVELGEQDAEHEQDvehgEQDVEHGEQDVEHGEQDVEHGEQDVEHEQdveh 134
Cdd:COG1196    238 EAELEELEAELEELEAELEELE-AELAELEAELEELRLELEEL----ELELEEAQAEEYELLAELARLEQDIARLE---- 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  135 gEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVERGEQDVEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEHG 214
Cdd:COG1196    309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  215 EQAIQNTADSSDTTRKTEQRNNSNKQGKRERQQEIRDIRETRSNKEEAKMDKNGNKKAEESHRKEEIDQK 284
Cdd:COG1196    388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
PTZ00121 PTZ00121
MAEBL; Provisional
 24-387 3.01e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 3.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   24 KEANQVTEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQDAEHEQDVEHGEQ 103
Cdd:PTZ00121  1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  104 DVEHGEQDVEHgEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEhgEQDVERGEQDVEHG 183
Cdd:PTZ00121  1419 KADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKKKAEEA 1495

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  184 EQNTEHVEPAVEHGEQAINNREQEEQDiEHGEQAIQNTADSSDTTRKTEQRNNSNKQGKRERQQEIRDIRETRSNKEEAK 263
Cdd:PTZ00121  1496 KKKADEAKKAAEAKKKADEAKKAEEAK-KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  264 MDKNGNKKAEEShRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVKDKDGRTRETEQTEEQKEREQGEIKQGDKKSSERE 343
Cdd:PTZ00121  1575 DKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 2449299893  344 RGNREERIKTRERDKNNTEQKEHKSQKKTEQRTKHKNKTQRNTE 387
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
SMBP pfam16785
Small metal-binding protein; This histidine-rich protein binds metal ions.
 127-219 4.16e-06

Small metal-binding protein; This histidine-rich protein binds metal ions.


Pssm-ID: 407049 [Multi-domain]  Cd Length: 111  Bit Score: 47.35  E-value: 4.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  127 EHEQD-VEHGEQDVEHGEQdveheqnvEHGEQDVEHGEQDVEHGeqdveRGEQDVEHGEQNtEHVEPAVEHGEQAINNRE 205
Cdd:pfam16785   25 EHLAEaIEHAEAAVAHGKD--------GHAKALVEHAEEALKHA-----KAAAEKADGEEN-EHLDEGIKHLEEAIKHGK 90

                           90
                   ....*....|....*.
gi 2449299893  206 QEEQDI--EHGEQAIQ 219
Cdd:pfam16785   91 MGHADAatKHAEEALK 106
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 75-331 5.42e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 51.53  E-value: 5.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   75 KQDVEHGEQDVELGEQDAEHEQDVEhGEQDvEHGEQDVEHGEQDVEHGEQdvEHEQDVEHGEQDVEHGEQDVEHEQNVEH 154
Cdd:TIGR00927  632 KGDVAEAEHTGERTGEEGERPTEAE-GENG-EESGGEAEQEGETETKGEN--ESEGEIPAERKGEQEGEGEIEAKEADHK 707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  155 GEQD---VEHGEQDVEHGEQDVERGEQDvEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEHGEQAIQNTADSSDTTRKT 231
Cdd:TIGR00927  708 GETEaeeVEHEGETEAEGTEDEGEIETG-EEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAG 786

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  232 EqrnNSNKQGKRERQQEIRDIRETRSNKEEAKMDKNGNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVKDK 311
Cdd:TIGR00927  787 E---DGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEAKQDEKGVDGGGGSDGGDS 863

                          250       260
                   ....*....|....*....|
gi 2449299893  312 DGRTRETEQTEEQKEREQGE 331
Cdd:TIGR00927  864 EEEEEEEEEEEEEEEEEEEE 883
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
 405-509 8.88e-06

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270094  Cd Length: 104  Bit Score: 46.17  E-value: 8.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  405 WKRYYFTLNGRLLTYYKpqrhyqDPGGQQgspsgpQSGPKGVLDLDFLLQVT---VGRrgimkaNYPFKLTCKNLPSVKL 481
Cdd:cd13275     15 WSKHWFVLRGAALKYYR------DPSAEE------AGELDGVIDLSSCTEVTelpVSR------NYGFQVKTWDGKVYVL 76

                           90       100
                   ....*....|....*....|....*...
gi 2449299893  482 AAETSEDREKWVRILQDVLQDVRQDAPT 509
Cdd:cd13275     77 SAMTSGIRTNWIQALRKAAGLPSPPALP 104
PTZ00121 PTZ00121
MAEBL; Provisional
 17-294 1.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   17 LNKHEVLKEANQVTEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEhkQDVEHGEQDVELGEQDAEHEQ 96
Cdd:PTZ00121  1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAKKAE 1616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   97 DVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHEQDVEHGEQDVE-HGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVER 175
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  176 GEQDVEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGKRERQQEIRDIRET 255
Cdd:PTZ00121  1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2449299893  256 RSNKEEAKMDKNGNKKAEESHRKEEiDQKGDINSPNEGG 294
Cdd:PTZ00121  1777 KEAVIEEELDEEDEKRRMEVDKKIK-DIFDNFANIIEGG 1814
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 111-374 1.68e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 49.99  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  111 DVEHGEQDVEHGEQDVEHEQDVEhGEQDVEHGEQDVEHEQNVEHGEQDVEhGEQDVEHGEQDVERGEQDVEHGEQNTEHV 190
Cdd:TIGR00927  634 DVAEAEHTGERTGEEGERPTEAE-GENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEADHKGETE 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  191 EPAVEHGEQAINNREQEEQDIEHGEQAiqntadssdttRKTEQRNNSNKQGKRERQQEiRDIRETRSNKEEAKMDKNGNK 270
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEGEIETGEEG-----------EEVEDEGEGEAEGKHEVETE-GDRKETEHEGETEAEGKEDED 779

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  271 KAeESHRKEEIDQKGD------INSPNEGGSGRKSNKRGNKGTVKDKDGrTRETEQTEEQKEREQGEIKQGDKKSSERER 344
Cdd:TIGR00927  780 EG-EIQAGEDGEMKGDegaegkVEHEGETEAGEKDEHEGQSETQADDTE-VKDETGEQELNAENQGEAKQDEKGVDGGGG 857

                          250       260       270
                   ....*....|....*....|....*....|
gi 2449299893  345 GNREERIKTRERDKNNTEQKEHKSQKKTEQ 374
Cdd:TIGR00927  858 SDGGDSEEEEEEEEEEEEEEEEEEEEEEEE 887
PTZ00121 PTZ00121
MAEBL; Provisional
 17-385 2.14e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   17 LNKHEVLKEANQVTEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQDAEHEQ 96
Cdd:PTZ00121  1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   97 DVEHGEQDVEHGEQDVEHGEQ-DVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVER 175
Cdd:PTZ00121  1631 EKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  176 GEQDVEHGEQ-------NTEHVEPAVEHGEQ------AINNREQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGK 242
Cdd:PTZ00121  1711 EAEEKKKAEElkkaeeeNKIKAEEAKKEAEEdkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  243 RERQQEIRDIRETRSNKE-------EAKMDKNGNKKAEESHRKEEID------------QKGDINSPNEGGSGRKSNKRG 303
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNFAniieggkEGNLVINDSKEMEDSAIKEVADsknmqleeadafEKHKFNKNNENGEDGNKEADF 1870

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  304 NKGTVKDKDgrtreteqtEEQKEREQGEIKQGDKKSSERERGNREERIKTRERDKNNTEQKEHKSQKKTEQRTKHKNKTQ 383
Cdd:PTZ00121  1871 NKEKDLKED---------DEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKISK 1941


                   ..
gi 2449299893  384 RN 385
Cdd:PTZ00121  1942 KD 1943
PTZ00121 PTZ00121
MAEBL; Provisional
 188-389 2.62e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  188 EHVEPAVEHGEQAINNREQEEqdIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGKRErqqEIRDIRETRSNKEEAKMDKn 267
Cdd:PTZ00121  1233 EEAKKDAEEAKKAEEERNNEE--IRKFEEARMAHFARRQAAIKAEEARKADELKKAE---EKKKADEAKKAEEKKKADE- 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  268 GNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVKDKDGRTRETEQTEEQKEREQGEIKQGDKKSSERERGNR 347
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2449299893  348 EERIKTRERDKNNTEQKEHKSQ--KKTEQRTKHKNKTQRNTEHK 389
Cdd:PTZ00121  1387 AEEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEK 1430
COG5137 COG5137
Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics] ...
 48-212 3.53e-05

Histone chaperone involved in gene silencing [Transcription / Chromatin structure and dynamics];


Pssm-ID: 227466 [Multi-domain]  Cd Length: 279  Bit Score: 47.68  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   48 EQDVEH--GEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEqdAEHEQDVEHGEQDVEHGEQDVEhgEQDVEHGEQd 125
Cdd:COG5137    125 KSDVEEpsEKVDEEDVEREILAEKPRVTRFNIVWDNDEDNDEAP--PAQPDVDNEEEERLEESDGREE--EEDEEVGSD- 199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  126 veheqdvEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVERGEQDVEHGEQNTEHVEPAVEHGEQAINNRE 205
Cdd:COG5137    200 -------SYGEGNRELNEEEEEEAEGSDDGEDVVDYEGERIDKKQGEEEEMEEEVINLFEIEWEEESPSEEVPRNNEESP 272


                   ....*..
gi 2449299893  206 QEEQDIE 212
Cdd:COG5137    273 AKKQKVE 279
SMBP pfam16785
Small metal-binding protein; This histidine-rich protein binds metal ions.
 31-128 4.07e-05

Small metal-binding protein; This histidine-rich protein binds metal ions.


Pssm-ID: 407049 [Multi-domain]  Cd Length: 111  Bit Score: 44.26  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   31 EHGEQDVEHGEQDVEHGEQdvEHGEQDVEHGEQDVEHGEQNVEhkqdVEHGEqdvelgeqDAEHEQD-VEHGEQDVEHGE 109
Cdd:pfam16785   25 EHLAEAIEHAEAAVAHGKD--GHAKALVEHAEEALKHAKAAAE----KADGE--------ENEHLDEgIKHLEEAIKHGK 90

                           90
                   ....*....|....*....
gi 2449299893  110 QdvEHGEQDVEHGEQDVEH 128
Cdd:pfam16785   91 M--GHADAATKHAEEALKH 107
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 19-164 6.96e-05

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 47.68  E-value: 6.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   19 KHEVLKEA-NQVTEHGEQDVEHGEQDVEHGE-QDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDvelGEQDAEHEQ 96
Cdd:TIGR00927  752 KHEVETEGdRKETEHEGETEAEGKEDEDEGEiQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQS---ETQADDTEV 828

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449299893   97 DVEHGEQDVEHGEQ-DVEHGEQDVEHGEqdvehEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQ 164
Cdd:TIGR00927  829 KDETGEQELNAENQgEAKQDEKGVDGGG-----GSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 14-195 1.24e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.09  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   14 NVLLNKHEVLKEANQVtEHGEQDVEHGEQDV-----EHGEQDVEHGEQDVEHGEQDVEH-GEQNVEHKQDVEHGEQDV-- 85
Cdd:PTZ00341   386 NSAINYYDAVKDGKYL-DDDSSDALYTDEDLlfdleKQKYMDMLDGSEDESVEDNEEEHsGDANEEELSVDEHVEEHNad 464

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   86 ELGEQDAEHEQDVEHGEQDVEHGEQDVEH-GEQDVEHGEQDVEHEQDVEhgEQDVEHGEQDVEHEQNVEHGEQDVEHGEQ 164
Cdd:PTZ00341   465 DSGEQQSDDESGEHQSVNEIVEEQSVNEHvEEPTVADIVEQETVDEHVE--EPAVDENEEQQTADEHVEEPTIAEEHVEE 542

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2449299893  165 DVEHGEQDVERGEQDVehgeQNTEHVEPAVE 195
Cdd:PTZ00341   543 EISTAEEHIEEPASDV----QQDSEAAPTIE 569
PHA03169 PHA03169
hypothetical protein; Provisional
 28-207 2.20e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.73  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   28 QVTEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGE-QDVEHGEQNVEHKQDVEHGEQDVELGEQDAEHEQDVEHGEQDVE 106
Cdd:PHA03169    70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTpSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  107 HGEQDVEHGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVERGEQDVEHGEQN 186
Cdd:PHA03169   150 APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229

                          170       180
                   ....*....|....*....|.
gi 2449299893  187 tehvepAVEHGEQAINNREQE 207
Cdd:PHA03169   230 ------AVEHEDEPTEPEREG 244
SMBP_like cd13840
Small metal-binding protein conserved in proteobacteria; This periplasmic protein appears ...
 106-201 2.38e-04

Small metal-binding protein conserved in proteobacteria; This periplasmic protein appears capable of binding multiple equivalents of a variety of divalent and trivalent metals, including Cu(2+) and Fe(3+) but also Mn(2+), Ni(2+), Mg(2+), and Zn(2+). It has been suggested that SMBP is a metal scavenging protein that plays a role in cellular copper management in Nitrosomonas europaea.


Pssm-ID: 260104  Cd Length: 89  Bit Score: 41.54  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  106 EHGEQDVEHGEQDVEHGeQDVEHEQDVEHGEQDVEHGE--QDVEHEQNvEHGEQDVEHGEQDVEHGEQDvergeqdveHG 183
Cdd:cd13840      3 DHLDEAIEHAEAAITHG-KAGHAKALAEHAEEALKHAKaaEKEKAEAK-KHLDEAIKHLEEAIKHGKMG---------HA 71

                           90
                   ....*....|....*...
gi 2449299893  184 EQNTEHVEPAVEHGEQAI 201
Cdd:cd13840     72 DVATKHAEEALKHLKAAN 89
PHA03169 PHA03169
hypothetical protein; Provisional
 30-217 2.52e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   30 TEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEqnvehKQDVEHGEQDVELGEQDAEHEQDVEHGEQDVEHGE 109
Cdd:PHA03169    65 GHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPT-----PSPSGSAEELASGLSPENTSGSSPESPASHSPPPS 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  110 QDVEHGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEqdverGEQDVEHGEQNTEH 189
Cdd:PHA03169   140 PPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTS-----SPPPQSPPDEPGEP 214

                          170       180
                   ....*....|....*....|....*...
gi 2449299893  190 VEPAVEHGEQAINNREQEEQDIEHGEQA 217
Cdd:PHA03169   215 QSPTPQQAPSPNTQQAVEHEDEPTEPER 242
PTZ00121 PTZ00121
MAEBL; Provisional
 19-387 2.56e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   19 KHEVLKEANQVTEHGEQdvEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQ--DAEHEQ 96
Cdd:PTZ00121  1225 KAEAVKKAEEAKKDAEE--AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakKAEEKK 1302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   97 DVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQN-VEHGEQDVEHGEQDVEHGEQDVER 175
Cdd:PTZ00121  1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADA 1382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  176 GEQDVEHGEQNTEHVEPAVEHGEQA--INNREQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGKRerQQEIRDIR 253
Cdd:PTZ00121  1383 AKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK--AEEAKKAE 1460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  254 ETRSNKEEAKMDKNGNKKAEESHRKEEIDQKGDinspnegGSGRKSNKRGNKGTVKDKDGRTRETEQTEEQKEREQGEIK 333
Cdd:PTZ00121  1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-------EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2449299893  334 QGDKKSSERERGNREERIKTRERDKNNTEQKEHKSQKKTEQRtkhKNKTQRNTE 387
Cdd:PTZ00121  1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED---KNMALRKAE 1584
PTZ00121 PTZ00121
MAEBL; Provisional
 23-389 5.29e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   23 LKEANQVTEHGEQDVEHGEQDVEhgEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQDAEHEQDVEHGE 102
Cdd:PTZ00121  1026 IEKIEELTEYGNNDDVLKEKDII--DEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA 1103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  103 QDVEHGEQDVEHGEQDVEHGEQDVEHEQDVEHGEqDVEHGEQ--DVEHEQNVEHGEQDVEHGEQDVEHGEQDVERGEQDV 180
Cdd:PTZ00121  1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAE-DARKAEEarKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  181 EHGE-QNTEHVEPA-----VEHGEQAINNRE-------QEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQgKRERQQ 247
Cdd:PTZ00121  1183 KAEEvRKAEELRKAedarkAEAARKAEEERKaeearkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR-KFEEAR 1261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  248 EIRDIRETRSNKEEAKMDKNGNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVKDKDGRTRETE-QTEEQKE 326
Cdd:PTZ00121  1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEA 1341

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2449299893  327 REQGEIKQGDKKSSERERGNREERIKTRERDKNNTEQKEHKSQKKTEQRTKHKNKTQRNTEHK 389
Cdd:PTZ00121  1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
PH_Boi cd13316
Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally ...
 402-496 7.18e-04

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270126  Cd Length: 97  Bit Score: 40.43  E-value: 7.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTLNGRLLTYYKPQRHYQDpggqqgspsgpqsgpKGVLDLDFLLQVTVGRRGIMKANYPFKLTCKNLPSVK- 480
Cdd:cd13316     13 YGTWKTRYFVLKGTRLYYLKSENDDKE---------------KGLIDLTGHRVVPDDSNSPFRGSYGFKLVPPAVPKVHy 77

                           90
                   ....*....|....*.
gi 2449299893  481 LAAETSEDREKWVRIL 496
Cdd:cd13316     78 FAVDEKEELREWMKAL 93
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 402-504 9.89e-04

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 40.72  E-value: 9.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  402 FSTWKRYYFTLNGRLLTYYKpqrHYQDPGGQQgspsgpqsgPKGVLDLD--FLLQVTVGRRGIM-KAN-------YPFKL 471
Cdd:cd01263     17 LGAWHRRWCVLRGGYLSFWK---YPDDEEKKK---------PIGSIDLTkcITEKVEPAPRELCaRPNtflletlRPAED 84

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2449299893  472 TCKNLPSVK----LAAETSEDREKWVRILQDVLQDVR 504
Cdd:cd01263     85 DDRDDTNEKirvlLSADTKEERIEWLSALNQTLADLR 121
PHA03169 PHA03169
hypothetical protein; Provisional
 21-192 1.22e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   21 EVLKEANQVTEHGEQDVE-------HGEQDVEHGE-QDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQDA 92
Cdd:PHA03169    70 ESDTETAEESRHGEKEERgqggpsgSGSESVGSPTpSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   93 EHEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHEQDVEHGEQdvehGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQd 172
Cdd:PHA03169   150 APPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQ----SETPTSSPPPQSPPDEPGEPQSPTPQQAPS- 224

                          170       180
                   ....*....|....*....|
gi 2449299893  173 vERGEQDVEHGEQNTEHVEP 192
Cdd:PHA03169   225 -PNTQQAVEHEDEPTEPERE 243
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 118-306 1.44e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  118 DVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDVERGEQDVEHGEQNTEHVE---PAV 194
Cdd:PRK12678    82 RAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEaraDAA 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  195 EHGEQAINNREQEEQDIE--HGEQAIQNTADSSDTTRKTEQRNNSNKQGKRERQQeiRDIRETRSNKEEAKMDKNGNKKA 272
Cdd:PRK12678   162 ERTEEEERDERRRRGDREdrQAEAERGERGRREERGRDGDDRDRRDRREQGDRRE--ERGRRDGGDRRGRRRRRDRRDAR 239

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2449299893  273 EESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKG 306
Cdd:PRK12678   240 GDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRG 273
PH_DOCK-D cd13267
Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also ...
 406-507 1.54e-03

Dedicator of cytokinesis-D subfamily Pleckstrin homology (PH) domain; DOCK-D subfamily (also called Zizimin subfamily) consists of Dock9/Zizimin1, Dock10/Zizimin3, and Dock11/Zizimin2. DOCK-D has a N-terminal DUF3398 domain, a PH-like domain, a Dock Homology Region 1, DHR1 (also called CZH1), a C2 domain, and a C-terminal DHR2 domain (also called CZH2). Zizimin1 is enriched in the brain, lung, and kidney; zizimin2 is found in B and T lymphocytes, and zizimin3 is enriched in brain, lung, spleen and thymus. Zizimin1 functions in autoinhibition and membrane targeting. Zizimin2 is an immune-related and age-regulated guanine nucleotide exchange factor, which facilitates filopodial formation through activation of Cdc42, which results in activation of cell migration. No function has been determined for Zizimin3 to date. The N-terminal half of zizimin1 binds to the GEF domain through three distinct areas, including CZH1, to inhibit the interaction with Cdc42. In addition its PH domain binds phosphoinositides and mediates zizimin1 membrane targeting. DOCK is a family of proteins involved in intracellular signalling networks. They act as guanine nucleotide exchange factors for small G proteins of the Rho family, such as Rac and Cdc42. There are 4 subfamilies of DOCK family proteins based on their sequence homology: A-D. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270087  Cd Length: 126  Bit Score: 40.39  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  406 KRYYFTL-----NGRLLTYYKPQRhyqdpggqqgspsgpQSGPKGVLDLDFLLQVtvgRRGIMKANYPFKLTCKNLPSVK 480
Cdd:cd13267     32 KRRFFHLkqlvdGSYILEFYKDEK---------------KKEAKGTIFLDSCTGV---VQNSKRRKFCFELRMQDKKSYV 93

                           90       100
                   ....*....|....*....|....*..
gi 2449299893  481 LAAETSEDREKWVRILQDVLQDVRQDA 507
Cdd:cd13267     94 LAAESEAEMDEWISKLNKILQSSKEQS 120
Semenogelin pfam05474
Semenogelin; This family consists of several mammalian secreted seminal proteins including ...
 24-247 1.94e-03

Semenogelin; This family consists of several mammalian secreted seminal proteins including semenogelin I and II. Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle secreted semenogelins (Sg). This family also includes seminal vesicle secretory protein 3A from mouse, which has been shown to be involved in the coagulation of semen resulting in the formation of the copulatory plug.


Pssm-ID: 368458 [Multi-domain]  Cd Length: 582  Bit Score: 42.94  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   24 KEANQVTEHgEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQ----NVEHKQDVeHGEQDVELgeQDAEHEQDVE 99
Cdd:pfam05474  325 KSQNQVTIH-SQDQEHGHKENKISYQSSSTEERHLNCGEKGIQKGVSkgsiSIQTEEQI-HGKSQNQV--RIPSQAQEYG 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  100 HGEQDVEHGEQDVEhgEQDVEHGEQDVEheQDVEHGEQDVEHGEQDVEHEQN-VEHGEQDVEHGEQDVEHGEQDVERGEQ 178
Cdd:pfam05474  401 HKENKISYQSSSTE--ERRLNSGEKDVQ--KGVSKGSISIQTEEKIHGKSQNqVTIPSQDQEHGHKENKMSYQSSSTEER 476

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449299893  179 DVEHGEQNTE----------HVEPAVEHGEQAinNREQEEQDIEHGEQAIQNTADSSDttrkTEQRNNSNKQGKRERQQ 247
Cdd:pfam05474  477 RLNYGGKSTQkdvsqssisfQIEKLVEGKSQI--QTPNPNQDQWSGQNAKGKSGQSAD----SKQDLLSHEQKGRYKQE 549
PHA03169 PHA03169
hypothetical protein; Provisional
 47-223 2.72e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   47 GEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVE------------LGEQDAEHEQDVEHG--EQDVEHGEQDV 112
Cdd:PHA03169    48 PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERgqggpsgsgsesVGSPTPSPSGSAEELasGLSPENTSGSS 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  113 EHGEQDVEHGEQDVEHEQDVEHGE--------QDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQDvERGEQDVEHGE 184
Cdd:PHA03169   128 PESPASHSPPPSPPSHPGPHEPAPpeshnpspNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQS-ETPTSSPPPQS 206

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2449299893  185 QNTEHVEPAVEHGEQAINNREQEEqdIEHGEQAIQNTAD 223
Cdd:PHA03169   207 PPDEPGEPQSPTPQQAPSPNTQQA--VEHEDEPTEPERE 243
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
55-258 2.79e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   55 EQDVEHGEQDVEHGEQNVEHKQdvEHGEQDVELGEQDAE-HEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEhEQDVE 133
Cdd:COG4913    241 HEALEDAREQIELLEPIRELAE--RYAAARERLAELEYLrAALRLWFAQRRLELLEAELEELRAELARLEAELE-RLEAR 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  134 HGEQDVEhgEQDVEHEQNvEHGEQDVEHGEQDVEHGEQDVERGEQDVEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEH 213
Cdd:COG4913    318 LDALREE--LDELEAQIR-GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2449299893  214 GEQAIQNTADSSDTTRKTEQRnNSNKQgKRERQQEIRDIRETRSN 258
Cdd:COG4913    395 ALEEELEALEEALAEAEAALR-DLRRE-LRELEAEIASLERRKSN 437
PHA03169 PHA03169
hypothetical protein; Provisional
 33-243 3.10e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   33 GEQDVEHGEQDVEHGEQDVEHGEQDVEhGEQDVEHGEQNvEHKQDVEHGEQDVELGEQDAEHEQDVEHG--EQDVEHGEQ 110
Cdd:PHA03169    48 PPAPTTSGPQVRAVAEQGHRQTESDTE-TAEESRHGEKE-ERGQGGPSGSGSESVGSPTPSPSGSAEELasGLSPENTSG 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  111 DVEHGEQDVEHGEQDVEHEQDVEHGEqDVEHGEQDVEHEQnvehgEQDVEHGEQDVEHGEQDVERGEQDVEHGEQnTEHV 190
Cdd:PHA03169   126 SSPESPASHSPPPSPPSHPGPHEPAP-PESHNPSPNQQPS-----SFLQPSHEDSPEEPEPPTSEPEPDSPGPPQ-SETP 198

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2449299893  191 EPAVEHGEQAINNREQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNKQGKR 243
Cdd:PHA03169   199 TSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHR 251
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
 401-500 4.19e-03

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270083  Cd Length: 114  Bit Score: 38.90  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  401 AFSTWKRYYFTLNGRLLTYY------KPQRHYQDPGGQQGS-PSGPQSGPKgvldldFLLQVTVGRRGIMKANypfkltc 473
Cdd:cd13263     15 IVKNWQQRWFVLRGDQLYYYkdeddtKPQGTIPLPGNKVKEvPFNPEEPGK------FLFEIIPGGGGDRMTS------- 81

                           90       100
                   ....*....|....*....|....*..
gi 2449299893  474 kNLPSVKLAAETSEDREKWVRILQDVL 500
Cdd:cd13263     82 -NHDSYLLMANSQAEMEEWVKVIRRVI 107
PTZ00121 PTZ00121
MAEBL; Provisional
 10-384 6.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 6.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   10 KNTLNVLLNKHEVLKEANQVTEHGEQDVEHGEQdvehgEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELgE 89
Cdd:PTZ00121  1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-----LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA-K 1450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   90 QDAEHEQDVEHGEQDVEHGEQdVEHGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDV--- 166
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakk 1529

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  167 --EHGEQDVERGEQDVEHGEQ--NTEHVEPA--VEHGEQAINNREQEEQDIEHGEQAIQNTADSSDTTRKTEQRNNSNK- 239
Cdd:PTZ00121  1530 aeEAKKADEAKKAEEKKKADElkKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKa 1609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  240 -QGKRERQQEIRDIRETRSNKEEAKMDKNGNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRGNKGTVKDKDgrTRET 318
Cdd:PTZ00121  1610 eEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDE 1687

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449299893  319 EQTEEQKEREQGEIKQGD--KKSSERERGNREERIKTRERDKNNTEQ---KEHKSQKKTEQRTK---HKNKTQR 384
Cdd:PTZ00121  1688 KKAAEALKKEAEEAKKAEelKKKEAEEKKKAEELKKAEEENKIKAEEakkEAEEDKKKAEEAKKdeeEKKKIAH 1761
PHA03169 PHA03169
hypothetical protein; Provisional
 32-235 6.96e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   32 HGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQDaEHEQDVEHGEQDVEHGEQD 111
Cdd:PHA03169    26 HGGTREQAGRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKE-ERGQGGPSGSGSESVGSPT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  112 VEHGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDVEHEQNVEHGEQDVEHGEQDVEHGEQ--DVERGEQDVEHGEQNTEH 189
Cdd:PHA03169   105 PSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSsfLQPSHEDSPEEPEPPTSE 184

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2449299893  190 VEPAVEHGEQAinnrEQEEQDIEHGEQAIQNTADSSDTTRKTEQRN 235
Cdd:PHA03169   185 PEPDSPGPPQS----ETPTSSPPPQSPPDEPGEPQSPTPQQAPSPN 226
PTZ00438 PTZ00438
gamete antigen 27/25-like protein; Provisional
 82-166 8.46e-03

gamete antigen 27/25-like protein; Provisional


Pssm-ID: 185618  Cd Length: 374  Bit Score: 40.43  E-value: 8.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   82 EQDVELGEQDAEHEQDVEHGEQDVEHGEQDVEhGEQDVEHGEQDVEHEQDVEHGEQDVEHGEQDvEHEQNVEHGEQDVEH 161
Cdd:PTZ00438    85 ENDVELEGLNIIVKNEEERGTQKEEEEDEDVE-EIEEVEEVEVVEEEYDDDEDSEKDDEKESDA-EGDENELAGEYIIEE 162


                   ....*
gi 2449299893  162 GEQDV 166
Cdd:PTZ00438   163 VDDDV 167
PTZ00121 PTZ00121
MAEBL; Provisional
 19-377 9.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 9.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   19 KHEVLKEANQVTEHGEQDVEHGEQDVEHGE-QDVEHGEQDVEHGEQDVEHGEQNVEHKQDVEHGEQDVELGEQD----AE 93
Cdd:PTZ00121  1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeakkAE 1531

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893   94 HEQDVEHGEQDVEHGEQDVEHGEQDVEHGEQDVEHEQdVEHGEQDVEHGEQDVEHEQNVEhgEQDVEHGEQDVEHGEQDV 173
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE-AKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMK 1608

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  174 ERGEQDVEHGEQNTEHVEPAVEHGEQAINNREQEEQDIEHGEQaiqntadssdtTRKTEQRNNSNK-QGKRERQQEIRDI 252
Cdd:PTZ00121  1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-----------LKKAEEENKIKAaEEAKKAEEDKKKA 1677

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449299893  253 RETRSNKEEAKMDKNGNKKAEESHRKEEIDQKGDINSPNEGGSGRKSNKRgNKGTVKDKDGRTRETEQTEEQKEREQGEI 332
Cdd:PTZ00121  1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE-NKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2449299893  333 KQGDKKSSERERGNREERIKTRERDKNNTEQKEHKSQKKTEQRTK 377
Cdd:PTZ00121  1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH