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Conserved domains on  [gi|768021416|ref|XP_011527995|]
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intersectin-1 isoform X17 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
INTAP pfam16617
Intersectin and clathrin adaptor AP2 binding region; INTAP is a natively unstructured region ...
798-904 1.85e-61

Intersectin and clathrin adaptor AP2 binding region; INTAP is a natively unstructured region of intersectin 1 proteins, lying between the first pair of SH3 domains, that binds to the clathrin adaptor AP2. This binding forms an intersectin-AP2 complex that functions as an important regulator of clathrin-mediated SV recycling in synapses.


:

Pssm-ID: 435467  Cd Length: 115  Bit Score: 204.34  E-value: 1.85e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   798 KIPENEVPAPVKPVTDSTsaPAPKLALRETPA-PLAV-TSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLT 875
Cdd:pfam16617    1 KIPESEVPASVKPAADST--AAPKVALRETPTtPLAPpTSSESSTASNNWADFSSTWPTNSSEKAETDNWDAWAAQPSLT 78
                           90       100
                   ....*....|....*....|....*....
gi 768021416   876 VPSAGQLRQRSAFTPATATGSSPSPVLGQ 904
Cdd:pfam16617   79 VPSAGQLRQRSAFTPATVTGSSPSPVLGQ 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
214-309 1.38e-44

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 155.90  E-value: 1.38e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    214 EWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQ 293
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 768021416    294 PLPPVLPPEYIPPSFR 309
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
SH3_Intersectin1_1 cd11987
First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
744-798 1.75e-37

First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212920 [Multi-domain]  Cd Length: 55  Bit Score: 133.97  E-value: 1.75e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11987     1 YYRALYPFEARSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 55
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
14-108 6.87e-36

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 130.86  E-value: 6.87e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416     14 IWAITVEERAKHDQQFHSLKP-ISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGY 92
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 768021416     93 QLPSALPPVMKQQPVA 108
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
363-684 2.42e-18

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.77  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  363 LELEKRRQALLEQQRKEQERLAQLERAEQERKERERqEQERKRQLELEKQLEKQrelerqreeerrkeIERREAAKRELE 442
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEA--------------QAEEYELLAELA 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  443 R-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRI 521
Cdd:COG1196   299 RlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  522 AEithlqqqlqesqqmlgrlipEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEID 601
Cdd:COG1196   379 EE--------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  602 IFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEK 681
Cdd:COG1196   439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                  ...
gi 768021416  682 LKR 684
Cdd:COG1196   519 LRG 521
 
Name Accession Description Interval E-value
INTAP pfam16617
Intersectin and clathrin adaptor AP2 binding region; INTAP is a natively unstructured region ...
798-904 1.85e-61

Intersectin and clathrin adaptor AP2 binding region; INTAP is a natively unstructured region of intersectin 1 proteins, lying between the first pair of SH3 domains, that binds to the clathrin adaptor AP2. This binding forms an intersectin-AP2 complex that functions as an important regulator of clathrin-mediated SV recycling in synapses.


Pssm-ID: 435467  Cd Length: 115  Bit Score: 204.34  E-value: 1.85e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   798 KIPENEVPAPVKPVTDSTsaPAPKLALRETPA-PLAV-TSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLT 875
Cdd:pfam16617    1 KIPESEVPASVKPAADST--AAPKVALRETPTtPLAPpTSSESSTASNNWADFSSTWPTNSSEKAETDNWDAWAAQPSLT 78
                           90       100
                   ....*....|....*....|....*....
gi 768021416   876 VPSAGQLRQRSAFTPATATGSSPSPVLGQ 904
Cdd:pfam16617   79 VPSAGQLRQRSAFTPATVTGSSPSPVLGQ 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
214-309 1.38e-44

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 155.90  E-value: 1.38e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    214 EWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQ 293
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 768021416    294 PLPPVLPPEYIPPSFR 309
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
SH3_Intersectin1_1 cd11987
First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
744-798 1.75e-37

First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212920 [Multi-domain]  Cd Length: 55  Bit Score: 133.97  E-value: 1.75e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11987     1 YYRALYPFEARSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 55
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
14-108 6.87e-36

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 130.86  E-value: 6.87e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416     14 IWAITVEERAKHDQQFHSLKP-ISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGY 92
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 768021416     93 QLPSALPPVMKQQPVA 108
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
225-291 1.20e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 100.76  E-value: 1.20e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  225 YRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMS 291
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
26-90 1.71e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 100.37  E-value: 1.71e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416   26 DQQFHSLKPI-SGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQ 90
Cdd:cd00052     2 DQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
363-684 2.42e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.77  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  363 LELEKRRQALLEQQRKEQERLAQLERAEQERKERERqEQERKRQLELEKQLEKQrelerqreeerrkeIERREAAKRELE 442
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEA--------------QAEEYELLAELA 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  443 R-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRI 521
Cdd:COG1196   299 RlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  522 AEithlqqqlqesqqmlgrlipEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEID 601
Cdd:COG1196   379 EE--------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  602 IFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEK 681
Cdd:COG1196   439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                  ...
gi 768021416  682 LKR 684
Cdd:COG1196   519 LRG 521
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
224-307 9.94e-16

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 73.95  E-value: 9.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   224 KYRQLFNSHdKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSG--QPLPPVLPP 301
Cdd:pfam12763   11 KYWEIFSGL-KPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELPD 89

                   ....*.
gi 768021416   302 EYIPPS 307
Cdd:pfam12763   90 WLVPGS 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-638 1.71e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 1.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLPV---TFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQER-----KRQ 406
Cdd:TIGR02168  218 LKAELRELELALLVlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   407 LELEKQLEKQRELERqreeerrkeierreAAKRELER-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEAL 485
Cdd:TIGR02168  298 SRLEQQKQILRERLA--------------NLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   486 NDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDsL 565
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-L 442
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416   566 VTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELR-EIHNKQQLQKQKSMEAERLKQKEQERK 638
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQaRLDSLERLQENLEGFSEGVKALLKNQS 516
PTZ00121 PTZ00121
MAEBL; Provisional
331-738 2.09e-15

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 81.73  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  331 EEPVLEDEQQQLEKKLPVtfeDKKRENFERGNLELEKRRQallEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE 410
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEA---AEKKKEEAKKKADAAKKKA---EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  411 KQLEKQRELERQREEERRKEIERReaAKRELERQRQLE-----WERNRRQELLNQRNKEQEDivVLKAKKKTLEFELEAL 485
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEeakkkAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKAD 1500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  486 NDKKHQLEGKLQDiRCRLTTQRQEIESTNKSRELRIAEitHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSL 565
Cdd:PTZ00121 1501 EAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  566 VTLKRALEAK--ELARQHLRDQLDEVEK-----------ETRSKLQEIDIFNNQLKELREIHNKQQLQKQKS-----MEA 627
Cdd:PTZ00121 1578 MALRKAEEAKkaEEARIEEVMKLYEEEKkmkaeeakkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkAEE 1657
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  628 ERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRP----RKLHEEEK-----LKREESVKKKDGEEKGK 698
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKkkaeeLKKAEEENKIKAEEAKK 1737
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 768021416  699 QEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKGPLTISAQE 738
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
21-99 3.84e-15

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 72.02  E-value: 3.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    21 ERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQ--LPSAL 98
Cdd:pfam12763    8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIadVPDEL 87

                   .
gi 768021416    99 P 99
Cdd:pfam12763   88 P 88
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
741-797 3.90e-15

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 70.26  E-value: 3.90e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416    741 KVVYYRALYPFESRSHDEITIQPGDIVMVDEsqTGEPGWLGGELK-GKTGWFPANYAE 797
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLE--KSDDGWWKGRLGrGKEGLFPSNYVE 56
SH3_9 pfam14604
Variant SH3 domain;
747-797 7.71e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 63.79  E-value: 7.71e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   747 ALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:pfam14604    1 ALYPYEPKDDDELSLQRGDVITVIEES--EDGWWEGINTGRTGLVPANYVE 49
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
366-686 3.06e-12

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 71.16  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   366 EKRRQALLE------QQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQrelerqreeerRKEIERREAAKR 439
Cdd:pfam02463  152 PERRLEIEEeaagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-----------ALEYYQLKEKLE 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   440 ELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKK---TLEFELEALNDKKHQLEGKLQDIrcrlttQRQEIESTNKS 516
Cdd:pfam02463  221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKqeiEKEEEKLAQVLKENKEEEKEKKL------QEEELKLLAKE 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   517 RELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRD---SLVTLKRALEAKE---------LARQHLRD 584
Cdd:pfam02463  295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEkelKELEIKREAEEEEeeeleklqeKLEQLEEE 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   585 QLDEVEKETRSKLQEIDIFNNQL----KELREIHNKQQLQKQKSMEAERLKQKEqERKIIELEKQKEEAQRRAQERdkqw 660
Cdd:pfam02463  375 LLAKKKLESERLSSAAKLKEEELelksEEEKEAQLLLELARQLEDLLKEEKKEE-LEILEEEEESIELKQGKLTEE---- 449
                          330       340
                   ....*....|....*....|....*.
gi 768021416   661 lEHVQQEDEHQRPRKLHEEEKLKREE 686
Cdd:pfam02463  450 -KEELEKQELKLLKDELELKKSEDLL 474
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
331-414 6.55e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.03  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  331 EEPVLEDEQQQLEKKLpvtfEDKKReNFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE 410
Cdd:cd16269   213 ERKLLEEQQRELEQKL----EDQER-SYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287

                  ....
gi 768021416  411 KQLE 414
Cdd:cd16269   288 RSLK 291
PHA03247 PHA03247
large tegument protein UL36; Provisional
805-995 4.44e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  805 PAPVKPVTDSTSAPAPKLAlrETPAPLAVTSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSlTVPSAGQLRQ 884
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPT--PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA-RPARPPTTAG 2765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  885 RSAFTPATATGSSPSPVLGQPDFLLHPSMRLGHMQPRIVLLFPDPLQCSTSRLLPMLRPRPGVPFLRSPSCQSPSHPSRP 964
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 768021416  965 ISDA-------APSVKFTLMPPGRIHPCflfIPAVNSR 995
Cdd:PHA03247 2846 PPPSlplggsvAPGGDVRRRPPSRSPAA---KPAAPAR 2880
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
335-416 1.26e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 1.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    335 LEDEQQQLEKKLpvtfeDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 414
Cdd:smart00935   23 LEKEFKKRQAEL-----EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKIL 97

                    ..
gi 768021416    415 KQ 416
Cdd:smart00935   98 DK 99
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
212-284 1.28e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021416  212 VAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMH 284
Cdd:COG5126    58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
 
Name Accession Description Interval E-value
INTAP pfam16617
Intersectin and clathrin adaptor AP2 binding region; INTAP is a natively unstructured region ...
798-904 1.85e-61

Intersectin and clathrin adaptor AP2 binding region; INTAP is a natively unstructured region of intersectin 1 proteins, lying between the first pair of SH3 domains, that binds to the clathrin adaptor AP2. This binding forms an intersectin-AP2 complex that functions as an important regulator of clathrin-mediated SV recycling in synapses.


Pssm-ID: 435467  Cd Length: 115  Bit Score: 204.34  E-value: 1.85e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   798 KIPENEVPAPVKPVTDSTsaPAPKLALRETPA-PLAV-TSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSLT 875
Cdd:pfam16617    1 KIPESEVPASVKPAADST--AAPKVALRETPTtPLAPpTSSESSTASNNWADFSSTWPTNSSEKAETDNWDAWAAQPSLT 78
                           90       100
                   ....*....|....*....|....*....
gi 768021416   876 VPSAGQLRQRSAFTPATATGSSPSPVLGQ 904
Cdd:pfam16617   79 VPSAGQLRQRSAFTPATVTGSSPSPVLGQ 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
214-309 1.38e-44

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 155.90  E-value: 1.38e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    214 EWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSGQ 293
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKNQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 768021416    294 PLPPVLPPEYIPPSFR 309
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
SH3_Intersectin1_1 cd11987
First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
744-798 1.75e-37

First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212920 [Multi-domain]  Cd Length: 55  Bit Score: 133.97  E-value: 1.75e-37
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11987     1 YYRALYPFEARSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 55
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
14-108 6.87e-36

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 130.86  E-value: 6.87e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416     14 IWAITVEERAKHDQQFHSLKP-ISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGY 92
Cdd:smart00027    1 PWAISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                            90
                    ....*....|....*.
gi 768021416     93 QLPSALPPVMKQQPVA 108
Cdd:smart00027   81 PIPASLPPSLIPPSKR 96
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
744-798 3.72e-32

First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212770 [Multi-domain]  Cd Length: 55  Bit Score: 119.00  E-value: 3.72e-32
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11836     1 KYRALYAFEARNPDEISFQPGDIIQVDESQVAEPGWLAGELKGKTGWFPANYVEK 55
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
225-291 1.20e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 100.76  E-value: 1.20e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  225 YRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMS 291
Cdd:cd00052     1 YDQIFRSLDPDGDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
26-90 1.71e-25

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 100.37  E-value: 1.71e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416   26 DQQFHSLKPI-SGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQ 90
Cdd:cd00052     2 DQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
SH3_Intersectin2_1 cd11988
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
743-798 6.53e-23

First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212921 [Multi-domain]  Cd Length: 57  Bit Score: 92.63  E-value: 6.53e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  743 VYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11988     2 VNYRALYPFEARNHDEMSFNAGDIIQVDEKTVGEPGWLYGSFQGNFGWFPCNYVEK 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
363-684 2.42e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.77  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  363 LELEKRRQALLEQQRKEQERLAQLERAEQERKERERqEQERKRQLELEKQLEKQrelerqreeerrkeIERREAAKRELE 442
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAEL-EELRLELEELELELEEA--------------QAEEYELLAELA 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  443 R-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRI 521
Cdd:COG1196   299 RlEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  522 AEithlqqqlqesqqmlgrlipEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEID 601
Cdd:COG1196   379 EE--------------------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  602 IFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEK 681
Cdd:COG1196   439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518

                  ...
gi 768021416  682 LKR 684
Cdd:COG1196   519 LRG 521
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
408-728 6.56e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 83.06  E-value: 6.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  408 ELEKQLEKqrelerqreeerrkeierreaakreLERQ-------RQLEWERNRRQ--ELLNQRNKEQEDIVVLKAKKKTL 478
Cdd:COG1196   197 ELERQLEP-------------------------LERQaekaeryRELKEELKELEaeLLLLKLRELEAELEELEAELEEL 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  479 EFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQ-VQQ 557
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAElEEE 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  558 NSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDifnnQLKELREIHNKQQLQKQKSMEAERLKQKEQER 637
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEELLEALRAAAELAAQLEELEE 407
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  638 KIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAK 717
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
                         330
                  ....*....|.
gi 768021416  718 PAVQAPWSTAE 728
Cdd:COG1196   488 EAAARLLLLLE 498
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
224-307 9.94e-16

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 73.95  E-value: 9.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   224 KYRQLFNSHdKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMHLIDVAMSG--QPLPPVLPP 301
Cdd:pfam12763   11 KYWEIFSGL-KPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELPD 89

                   ....*.
gi 768021416   302 EYIPPS 307
Cdd:pfam12763   90 WLVPGS 95
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
335-638 1.71e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.64  E-value: 1.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLPV---TFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQER-----KRQ 406
Cdd:TIGR02168  218 LKAELRELELALLVlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   407 LELEKQLEKQRELERqreeerrkeierreAAKRELER-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEAL 485
Cdd:TIGR02168  298 SRLEQQKQILRERLA--------------NLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   486 NDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDsL 565
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-L 442
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416   566 VTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELR-EIHNKQQLQKQKSMEAERLKQKEQERK 638
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQaRLDSLERLQENLEGFSEGVKALLKNQS 516
PTZ00121 PTZ00121
MAEBL; Provisional
331-738 2.09e-15

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 81.73  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  331 EEPVLEDEQQQLEKKLPVtfeDKKRENFERGNLELEKRRQallEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE 410
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEA---AEKKKEEAKKKADAAKKKA---EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  411 KQLEKQRELERQREEERRKEIERReaAKRELERQRQLE-----WERNRRQELLNQRNKEQEDivVLKAKKKTLEFELEAL 485
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEeakkkAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKAD 1500
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  486 NDKKHQLEGKLQDiRCRLTTQRQEIESTNKSRELRIAEitHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSL 565
Cdd:PTZ00121 1501 EAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKKAD--EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  566 VTLKRALEAK--ELARQHLRDQLDEVEK-----------ETRSKLQEIDIFNNQLKELREIHNKQQLQKQKS-----MEA 627
Cdd:PTZ00121 1578 MALRKAEEAKkaEEARIEEVMKLYEEEKkmkaeeakkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkAEE 1657
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  628 ERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRP----RKLHEEEK-----LKREESVKKKDGEEKGK 698
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelKKKEAEEKkkaeeLKKAEEENKIKAEEAKK 1737
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 768021416  699 QEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKGPLTISAQE 738
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
348-659 2.38e-15

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 2.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   348 VTFEDKKREN--FERGNlELEKrrqalLEQQRKEQERLA------------QLERAEQERKERERQEQERKRQL-ELEKQ 412
Cdd:TIGR02168  661 ITGGSAKTNSsiLERRR-EIEE-----LEEKIEELEEKIaelekalaelrkELEELEEELEQLRKELEELSRQIsALRKD 734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   413 LEK-QRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQ 491
Cdd:TIGR02168  735 LARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   492 LEGKLQDIRCRLTTQRQEIESTNKS---RELRIAEITHLQQQLQESQQMLGRLIPEkqiLNDQLKQVQQnslhrdslvtl 568
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELIEE---LESELEALLN----------- 880
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   569 krALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQK-SMEAERLKQKEQERKIIELEKQKE 647
Cdd:TIGR02168  881 --ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTLEEAEA 958
                          330
                   ....*....|..
gi 768021416   648 EAQRRAQERDKQ 659
Cdd:TIGR02168  959 LENKIEDDEEEA 970
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
21-99 3.84e-15

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 72.02  E-value: 3.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    21 ERAKHDQQFHSLKPISGFITGDQARNFFFQSGLPQPVLAQIWALADMNNDGRMDQVEFSIAMKLIKLKLQGYQ--LPSAL 98
Cdd:pfam12763    8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNIadVPDEL 87

                   .
gi 768021416    99 P 99
Cdd:pfam12763   88 P 88
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
741-797 3.90e-15

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 70.26  E-value: 3.90e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416    741 KVVYYRALYPFESRSHDEITIQPGDIVMVDEsqTGEPGWLGGELK-GKTGWFPANYAE 797
Cdd:smart00326    1 EGPQVRALYDYTAQDPDELSFKKGDIITVLE--KSDDGWWKGRLGrGKEGLFPSNYVE 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
355-703 4.90e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.98  E-value: 4.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  355 RENFERGNL---ELEKRRQALlEQQR---------KEQERLAQLERAEQERKERERQEQERKRQL-ELEKQLEKQReler 421
Cdd:COG1196   185 EENLERLEDilgELERQLEPL-ERQAekaeryrelKEELKELEAELLLLKLRELEAELEELEAELeELEAELEELE---- 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  422 qreeerrkeierreAAKRELERQRQLEweRNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQdirc 501
Cdd:COG1196   260 --------------AELAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE---- 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  502 RLTTQRQEIEstnksrelriAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQnslhrdSLVTLKRALEAKELARQH 581
Cdd:COG1196   320 ELEEELAELE----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEE------ALLEAEAELAEAEEELEE 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  582 LRDQLDEVEKETRSKLQEIdifnNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWL 661
Cdd:COG1196   384 LAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 768021416  662 EHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQD 703
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
746-797 7.71e-15

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 69.68  E-value: 7.71e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11823     3 KALYSYTANREDELSLQPGDIIEVHEKQ--DDGWWLGELNGKKGIFPATYVE 52
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
335-708 1.55e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.44  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 414
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  415 KQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDkkHQLEG 494
Cdd:COG1196   469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE--AALAA 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  495 KLQDIRCRLTTQRQEIESTNKSRELRIAEI----------THLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDS 564
Cdd:COG1196   547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkiraraALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  565 LVTLkRALEAKELARQH---LRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIE 641
Cdd:COG1196   627 LVAA-RLEAALRRAVTLagrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  642 LEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRL 708
Cdd:COG1196   706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
PTZ00121 PTZ00121
MAEBL; Provisional
328-759 1.57e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 78.64  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  328 RLPEEPVLEDEQQQLEKKLPVTfEDKKRENFERGNLELEKRRqallEQQRKEQERLAQleRAEQERKERERQEQERKRQl 407
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKA----EEAKKKADAAKK--KAEEAKKAAEAAKAEAEAA- 1355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  408 elEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQ----RNKEQEDIVVLKAKKKTLEFELE 483
Cdd:PTZ00121 1356 --ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadelKKAAAAKKKADEAKKKAEEKKKA 1433
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  484 ALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRD 563
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  564 SLVTLKRALEAKELARQHLRDQLDEVEK-ETRSKLQEIdifnNQLKELREIHNKQQLQKQKSME---------AERLKQK 633
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKaEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEedknmalrkAEEAKKA 1589
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  634 EQER-----KIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHqrpRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRL 708
Cdd:PTZ00121 1590 EEARieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE---KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  709 FHQHQEPAKPAVQAPWSTAEKGP----LTISAQENVKVVYYRALYPFESRSHDEI 759
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEEDEKKaaeaLKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
PTZ00121 PTZ00121
MAEBL; Provisional
351-730 5.49e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 77.10  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  351 EDKKRENfERGNLELEKRRQALLEQQRKEQERLAQLER-AEQERK--ERERQEQERKRQLELEKQLEK-----QRELERQ 422
Cdd:PTZ00121 1402 EDKKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEAKKkAEEAKKadEAKKKAEEAKKAEEAKKKAEEakkadEAKKKAE 1480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  423 REEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDiVVLKAKKKTLEFELEALNDKKHQLEGKLQDiRCR 502
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAE-ELK 1558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  503 LTTQRQEIESTNKSRE-----LRIAEITHLQQQLQESQQMLgRLIPEKQILNDQLKQVQQNSLHRDSLvtlKRALEAKEL 577
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEdknmaLRKAEEAKKAEEARIEEVMK-LYEEEKKMKAEEAKKAEEAKIKAEEL---KKAEEEKKK 1634
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  578 ARQHLRDQLDEVEK--ETRSKLQEIDIFNNQLKElREIHNKQQLQKQKSMEAERLKQKEQERKIIElEKQKEEAQRRAQE 655
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAK-KAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAKKAEELKKKEA 1712
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  656 RDKQWLEHVQQEDEHqrpRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKG 730
Cdd:PTZ00121 1713 EEKKKAEELKKAEEE---NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
PTZ00121 PTZ00121
MAEBL; Provisional
326-686 6.56e-14

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 76.72  E-value: 6.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  326 DQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERE-RQEQERK 404
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEaKKAEEAK 1534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  405 RQLELEKQLEKQRELERQREEERRKEIErreaaKRELERQRQLEWERN---RRQELLNQRNKEQ-EDIVVLKAKKKTLEF 480
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEE-----KKKAEEAKKAEEDKNmalRKAEEAKKAEEARiEEVMKLYEEEKKMKA 1609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  481 E----LEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEithlqqqlqesqqmlgrliPEKQILNDQLKqvq 556
Cdd:PTZ00121 1610 EeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE-------------------EENKIKAAEEA--- 1667
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  557 qnslhrdslvtlKRALEAKELARQHLRDQLDEVEKETRSKLQEidifnNQLKELREIHNKQQLQKQKsmeAERLKQKEQE 636
Cdd:PTZ00121 1668 ------------KKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-----EEAKKAEELKKKEAEEKKK---AEELKKAEEE 1727
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  637 RKII--ELEKQKEEAQRRAQ-----ERDKQWLEHVQQEDEHQRPRKLHEEEKLKREE 686
Cdd:PTZ00121 1728 NKIKaeEAKKEAEEDKKKAEeakkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
439-713 2.34e-13

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 74.71  E-value: 2.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   439 RELERQ---------------------RQLEWE---------RNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDK 488
Cdd:TIGR02168  196 NELERQlkslerqaekaerykelkaelRELELAllvlrleelREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   489 KHQLEGKLQDIRCRLTTQRQEIEstnksrelriaeithlqqqlqesqqmlgRLIPEKQILNDQLKQVQQNSLHRD-SLVT 567
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEIS----------------------------RLEQQKQILRERLANLERQLEELEaQLEE 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   568 LKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHN--KQQLQKQKSMEAERLKQKEQERK-IIELEK 644
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLETLRSKVAQLELQIASLNNeIERLEA 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   645 QKEEAQRRAQERDKQWLEHVQQEDEHQR-------PRKLHEEEKLK-----REESVKKKDGEEKGKQEAQDKLGRLFHQH 712
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKKLEEAELkelqaelEELEEELEELQeelerLEEALEELREELEEAEQALDAAERELAQL 487

                   .
gi 768021416   713 Q 713
Cdd:TIGR02168  488 Q 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
350-685 2.74e-13

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 74.33  E-value: 2.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   350 FEDKKRENFErgnlELEKRRQALLEQQRKEQERLAQLERAEQER--KERERQEQERKRQLEL-EKQLEKQRELERQREEE 426
Cdd:TIGR02169  168 FDRKKEKALE----ELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYEGyELLKEKEALERQKEAIE 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   427 RRKEIERREAAKRELERQrQLEWERNRRQELLNQRNKE-----QEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDirc 501
Cdd:TIGR02169  244 RQLASLEEELEKLTEEIS-ELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELED--- 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   502 rLTTQRQEIESTNKSRELRIAEIThlqqqlqesqqmlgRLIPEKQILNDQLKQVQQNSlhRDSLVTLKRALEAKELARQH 581
Cdd:TIGR02169  320 -AEERLAKLEAEIDKLLAEIEELE--------------REIEEERKRRDKLTEEYAEL--KEELEDLRAELEEVDKEFAE 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   582 LRDQLDEVEKetrsklqEIDIFNNQLKEL-REIHNKQQLQKQKSMEAERLKQK-------------EQERKIIELEKQKE 647
Cdd:TIGR02169  383 TRDELKDYRE-------KLEKLKREINELkRELDRLQEELQRLSEELADLNAAiagieakineleeEKEDKALEIKKQEW 455
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 768021416   648 EAQRRAQERDKQWLEHVQQEDEHQRPRKlhEEEKLKRE 685
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEK--ELSKLQRE 491
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
744-797 3.14e-13

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 65.06  E-value: 3.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11875     1 KARVLFDYEAENEDELTLREGDIVTILSKDCEDKGWWKGELNGKRGVFPDNFVE 54
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
744-795 5.21e-13

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 64.41  E-value: 5.21e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDEsqTGEPGWLGGEL-KGKTGWFPANY 795
Cdd:cd00174     1 YARALYDYEAQDDDELSFKKGDIITVLE--KDDDGWWEGELnGGREGLFPANY 51
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
330-685 5.49e-13

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 73.17  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  330 PEEPVLEDEQQQLEK------KLPVTFEDKKRENFER-GNL--------ELEKRRQALLEQQRKEQERLAQLERAEQERK 394
Cdd:PRK03918  214 SELPELREELEKLEKevkeleELKEEIEELEKELESLeGSKrkleekirELEERIEELKKEIEELEEKVKELKELKEKAE 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  395 ERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKA- 473
Cdd:PRK03918  294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEe 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  474 -----KKKT------LEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKS-RELRIAEITHLQQQLQESQQMLGRL 541
Cdd:PRK03918  374 lerlkKRLTgltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRELTEEHRKEL 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  542 IPE-----KQILNDQLKQVQQNSLHRDSLVTLKRAL-EAKELARQH-LRDQLDEVEKETRS-KLQEIDIFNNQLKELREI 613
Cdd:PRK03918  454 LEEytaelKRIEKELKEIEEKERKLRKELRELEKVLkKESELIKLKeLAEQLKELEEKLKKyNLEELEKKAEEYEKLKEK 533
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021416  614 HNKQQlQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQwLEHVQQEDEHQRPRKLHEEEKLKRE 685
Cdd:PRK03918  534 LIKLK-GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE-LEELGFESVEELEERLKELEPFYNE 603
SH3_9 pfam14604
Variant SH3 domain;
747-797 7.71e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 63.79  E-value: 7.71e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   747 ALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:pfam14604    1 ALYPYEPKDDDELSLQRGDVITVIEES--EDGWWEGINTGRTGLVPANYVE 49
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
335-720 9.55e-13

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 72.36  E-value: 9.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLpvtfEDKKRENFERGNlELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKrqlELEKQLE 414
Cdd:TIGR04523  340 LNEQISQLKKEL----TNSESENSEKQR-ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE---KLNQQKD 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   415 KQRELERQReeerrkeierreaaKRELERQRQlewernrrqELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEG 494
Cdd:TIGR04523  412 EQIKKLQQE--------------KELLEKEIE---------RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   495 KLQDIRCRLTTQRQEIESTNKSRELRIAEIThlqqqlqesqqmlgRLIPEKQILNDQLKQVQQNSlhrDSLVTLKRALEA 574
Cdd:TIGR04523  469 QLKVLSRSINKIKQNLEQKQKELKSKEKELK--------------KLNEEKKELEEKVKDLTKKI---SSLKEKIEKLES 531
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   575 ----KELARQHLRDQLDEVEKE-TRSKLQ-EIDIFNNQLKELReiHNKQQLQKQKSMEAERLKQKEQERKiiELEKQKEE 648
Cdd:TIGR04523  532 ekkeKESKISDLEDELNKDDFElKKENLEkEIDEKNKEIEELK--QTQKSLKKKQEEKQELIDQKEKEKK--DLIKEIEE 607
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021416   649 AQRRAQERDKQwLEHVQQEDEhqrprKLHEEEKlkreesvkkkdgeekGKQEAQDKLGRLFHQHQEPAKPAV 720
Cdd:TIGR04523  608 KEKKISSLEKE-LEKAKKENE-----KLSSIIK---------------NIKSKKNKLKQEVKQIKETIKEIR 658
PTZ00121 PTZ00121
MAEBL; Provisional
351-688 1.35e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 72.48  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  351 EDKKRENFERGNLELEK----------RRQALL--EQQRKEQErlaqLERAEQERKERE-RQEQERKRQLELEKQLEKQR 417
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKfeearmahfaRRQAAIkaEEARKADE----LKKAEEKKKADEaKKAEEKKKADEAKKKAEEAK 1315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  418 ELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEdivvlkaKKKTLEFELEALNDKKHQLEGKLQ 497
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-------KAEAAEKKKEEAKKKADAAKKKAE 1388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  498 DIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQmlgrlipEKQILNDQLKQVQQNSlhrdslvtlKRALEAKEL 577
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA-------EEKKKADEAKKKAEEA---------KKADEAKKK 1452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  578 ARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKsmeAERLKQKEQERKIIELEKQKEEAQ-----RR 652
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKKAEEAKkadeaKK 1529
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 768021416  653 AQERDKQwlEHVQQEDEHQRPRKLHEEEKLKREESV 688
Cdd:PTZ00121 1530 AEEAKKA--DEAKKAEEKKKADELKKAEELKKAEEK 1563
SH3_CD2AP_3 cd12056
Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ...
744-796 1.55e-12

Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CD2AP. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212989 [Multi-domain]  Cd Length: 57  Bit Score: 63.30  E-value: 1.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYA 796
Cdd:cd12056     3 YCKALFHYEGTNEDELDFKEGEIILIISKDTGEPGWWKGELNGKEGVFPDNFV 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
335-686 1.66e-12

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 71.34  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQL-ELEKQL 413
Cdd:COG4717   100 LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELaELQEEL 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  414 EKQRELERQREEERRKEierreaAKRELERQRQlewernRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLE 493
Cdd:COG4717   180 EELLEQLSLATEEELQD------LAEELEELQQ------RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  494 GK----LQDIRCRLTTQRQEIESTnksrELRIAEIThlQQQLQESQQMLGRLIPEKQILNDQLKQVQ----QNSLHRDSL 565
Cdd:COG4717   248 ARllllIAAALLALLGLGGSLLSL----ILTIAGVL--FLVLGLLALLFLLLAREKASLGKEAEELQalpaLEELEEEEL 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  566 VTLKRALEAK-ELARQHLRDQLDEVEkETRSKLQEIDIFNNQLKELREIHNKQQLQKQK--SMEAERLKQKEQERKIIEL 642
Cdd:COG4717   322 EELLAALGLPpDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALLAEAgvEDEEELRAALEQAEEYQEL 400
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 768021416  643 EKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHE-EEKLKREE 686
Cdd:COG4717   401 KEELEELEEQLEELLGELEELLEALDEEELEEELEElEEELEELE 445
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
745-797 2.05e-12

Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212810 [Multi-domain]  Cd Length: 53  Bit Score: 62.72  E-value: 2.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11877     2 VRAKFNFEGTNEDELSFDKGDIITV--TQVVEGGWWEGTLNGKTGWFPSNYVK 52
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
366-686 3.06e-12

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 71.16  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   366 EKRRQALLE------QQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQrelerqreeerRKEIERREAAKR 439
Cdd:pfam02463  152 PERRLEIEEeaagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-----------ALEYYQLKEKLE 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   440 ELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKK---TLEFELEALNDKKHQLEGKLQDIrcrlttQRQEIESTNKS 516
Cdd:pfam02463  221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKqeiEKEEEKLAQVLKENKEEEKEKKL------QEEELKLLAKE 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   517 RELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRD---SLVTLKRALEAKE---------LARQHLRD 584
Cdd:pfam02463  295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEkelKELEIKREAEEEEeeeleklqeKLEQLEEE 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   585 QLDEVEKETRSKLQEIDIFNNQL----KELREIHNKQQLQKQKSMEAERLKQKEqERKIIELEKQKEEAQRRAQERdkqw 660
Cdd:pfam02463  375 LLAKKKLESERLSSAAKLKEEELelksEEEKEAQLLLELARQLEDLLKEEKKEE-LEILEEEEESIELKQGKLTEE---- 449
                          330       340
                   ....*....|....*....|....*.
gi 768021416   661 lEHVQQEDEHQRPRKLHEEEKLKREE 686
Cdd:pfam02463  450 -KEELEKQELKLLKDELELKKSEDLL 474
PTZ00121 PTZ00121
MAEBL; Provisional
326-729 4.11e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.94  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  326 DQRLPEEPVLEDEQQQLEKKLPVtfEDKKRENFERgnlELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKR 405
Cdd:PTZ00121 1126 DARKAEEARKAEDARKAEEARKA--EDAKRVEIAR---KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDAR 1200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  406 QLELEKQLEKQRELERQREEERrkeierreaaKRELERQRQLEWERNRRQEllnQRNKEQEDIVVLKAKKKTLEFELEAL 485
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAED----------AKKAEAVKKAEEAKKDAEE---AKKAEEERNNEEIRKFEEARMAHFAR 1267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  486 NDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSL 565
Cdd:PTZ00121 1268 RQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA 1347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  566 VTLKRALEAKELARQHLRDQLDEVEK-ETRSKLQEIDIFNNQLKELREIHNKQQLQKQKsmeAERLKQKEQERKIIELEK 644
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKKeEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK---ADELKKAAAAKKKADEAK 1424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  645 QKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPW 724
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504

                  ....*
gi 768021416  725 STAEK 729
Cdd:PTZ00121 1505 AAEAK 1509
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
744-797 4.46e-12

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 61.71  E-value: 4.46e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd12142     1 YCRVLFDYNPVAPDELALKKGDVIEVISKETEDEGWWEGELNGRRGFFPDNFVM 54
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
323-687 5.32e-12

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 70.39  E-value: 5.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   323 TSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQE 402
Cdd:pfam02463  652 VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   403 RKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKE------QEDIVVLKAKKK 476
Cdd:pfam02463  732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeklkaqEEELRALEEELK 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   477 TLEFELEALNDKKHQLEGKLQDIRCRlttQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLipEKQILNDQLKQVQ 556
Cdd:pfam02463  812 EEAELLEEEQLLIEQEEKIKEEELEE---LALELKEEQKLEKLAEEELERLEEEITKEELLQELL--LKEEELEEQKLKD 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   557 QNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELReihnkqqLQKQKSMEAERLKQKEQE 636
Cdd:pfam02463  887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-------LEEADEKEKEENNKEEEE 959
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   637 RKIIELEKQKEEAQRRaqerdkqwlehvqqeDEHQRPRKLHEEEKLKREES 687
Cdd:pfam02463  960 ERNKRLLLAKEELGKV---------------NLMAIEEFEEKEERYNKDEL 995
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
745-797 1.08e-11

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 60.78  E-value: 1.08e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11772     2 FRALYDYEAQHPDELSFEEGDLLYISDKS--DPNWWKATCGGKTGLIPSNYVE 52
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
332-707 1.13e-11

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 68.98  E-value: 1.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   332 EPVLEDEQQQLEK-----KLPVTFEDKKRENFER-------GNLELEKRRQALLEQQRKEQERlAQLERAEQERKERERQ 399
Cdd:pfam05483  362 EELLRTEQQRLEKnedqlKIITMELQKKSSELEEmtkfknnKEVELEELKKILAEDEKLLDEK-KQFEKIAEELKGKEQE 440
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   400 E----QERKRQL-ELEKQLekqreleRQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKE---------- 464
Cdd:pfam05483  441 LifllQAREKEIhDLEIQL-------TAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEltqeasdmtl 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   465 -----QEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIE-STNKSRElriaeitHLQQQLQESQQML 538
Cdd:pfam05483  514 elkkhQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEE-------NARSIEYEVLKKE 586
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   539 GRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRAL------EAKELARQHLRDQLDEVEKE-TRSKLQEI-DIFNNQL--K 608
Cdd:pfam05483  587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALkkkgsaENKQLNAYEIKVNKLELELAsAKQKFEEIiDNYQKEIedK 666
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   609 ELREIHNKQQLQKQKSMEAERLK-QKEQER----KIIE----LEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEE 679
Cdd:pfam05483  667 KISEEKLLEEVEKAKAIADEAVKlQKEIDKrcqhKIAEmvalMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI 746
                          410       420
                   ....*....|....*....|....*...
gi 768021416   680 EKLKREESVKKKDGEEKGKQEAQDKLGR 707
Cdd:pfam05483  747 ELSNIKAELLSLKKQLEIEKEEKEKLKM 774
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
363-686 1.13e-11

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 67.25  E-value: 1.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   363 LELEKRRQALLEQQRKEQERLAQLER----AEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAK 438
Cdd:pfam13868   28 IAEKKRIKAEEKEEERRLDEMMEEEReralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   439 RELERQRQLEWERNRRQELLNQRnkEQEDIVVLKAKKKTLEFELEALNDKKhqlegKLQDIRcrlttQRQEIESTNKSRE 518
Cdd:pfam13868  108 ERIQEEDQAEAEEKLEKQRQLRE--EIDEFNEEQAEWKELEKEEEREEDER-----ILEYLK-----EKAEREEEREAER 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   519 LRIAEithlqqqlqesqqmlgrlipEKQILNDQL-KQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRskl 597
Cdd:pfam13868  176 EEIEE--------------------EKEREIARLrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKAR--- 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   598 QEIDIFNNQLKELREIHNKQQLQKQKsMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEhvQQEDEHQRPRKLH 677
Cdd:pfam13868  233 QRQELQQAREEQIELKERRLAEEAER-EEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE--KQIEEREEQRAAE 309

                   ....*....
gi 768021416   678 EEEKLKREE 686
Cdd:pfam13868  310 REEELEEGE 318
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
327-659 2.09e-11

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 68.46  E-value: 2.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   327 QRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKErERQEQERKRQ 406
Cdd:pfam02463  183 ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIE 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   407 LELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVvlKAKKKTLEFELEALN 486
Cdd:pfam02463  262 KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK--KAEKELKKEKEEIEE 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   487 DKKHQLEGKLQDIRCRLTTQRQEiESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLV 566
Cdd:pfam02463  340 LEKELKELEIKREAEEEEEEELE-KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   567 TLKRALEAKELArqhlrdQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQ-KQKSMEAERLKQKEQERKIIELEKQ 645
Cdd:pfam02463  419 DLLKEEKKEELE------ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELElKKSEDLLKETQLVKLQEQLELLLSR 492
                          330
                   ....*....|....
gi 768021416   646 KEEAQRRAQERDKQ 659
Cdd:pfam02463  493 QKLEERSQKESKAR 506
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
363-726 4.76e-11

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 67.07  E-value: 4.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   363 LELEKRRQALLEQQRKEQERLAQLERAEQERKERERqEQERKRQLElEKQLEKQRELERQREEERRKEIERREAaKRELE 442
Cdd:pfam17380  275 LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR-EVERRRKLE-EAEKARQAEMDRQAAIYAEQERMAMER-ERELE 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   443 RQRQLEwernRRQELLNQRnkeQEDIVVLKAKKKTLEfelealndkKHQLEGKLQDIRCRlttqrQEIEStnkSRELRIA 522
Cdd:pfam17380  352 RIRQEE----RKRELERIR---QEEIAMEISRMRELE---------RLQMERQQKNERVR-----QELEA---ARKVKIL 407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   523 EithlqqqlqesqQMLGRLIPEKQILNDQLKQVQQNSLHRDSlvtlkRALEaKELARQHLRDQLDEVEKE---TRSKLQE 599
Cdd:pfam17380  408 E------------EERQRKIQQQKVEMEQIRAEQEEARQREV-----RRLE-EERAREMERVRLEEQERQqqvERLRQQE 469
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   600 IDIFNNQLKELREIHNKQQLQKQKSMEAERlKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEE 679
Cdd:pfam17380  470 EERKRKKLELEKEKRDRKRAEEQRRKILEK-ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM 548
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 768021416   680 EKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPWST 726
Cdd:pfam17380  549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATT 595
SH3_VAV1_2 cd11976
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ...
746-798 6.51e-11

C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The C-terminal SH3 domain of Vav1 interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212909 [Multi-domain]  Cd Length: 54  Bit Score: 58.42  E-value: 6.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVdESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11976     3 KARYDFCARDRSELSLKEGDIIKI-LNKKGQQGWWRGEIYGRVGWFPANYVEE 54
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
746-797 7.87e-11

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212815 [Multi-domain]  Cd Length: 54  Bit Score: 58.07  E-value: 7.87e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVmVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11882     3 RALYACKAEDESELSFEPGQII-TNVQPSDEPGWLEGTLNGRTGLIPENYVE 53
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
335-592 8.02e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.50  E-value: 8.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLpvTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLE--LEKQ 412
Cdd:COG1196   293 LLAELARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEeaLLEA 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  413 LEKQRELERQReeerrkeierREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQL 492
Cdd:COG1196   371 EAELAEAEEEL----------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  493 EGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQIlndqLKQVQQNSLHRDSLVTLKRAL 572
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL----LLEAEADYEGFLEGVKAALLL 516
                         250       260
                  ....*....|....*....|
gi 768021416  573 EAKELARQHLRDQLDEVEKE 592
Cdd:COG1196   517 AGLRGLAGAVAVLIGVEAAY 536
PTZ00121 PTZ00121
MAEBL; Provisional
331-683 1.48e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.93  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  331 EEPVLEDEQQQLEKKLPVTFEDKKRENFERGnlelEKRRQALLEQQRKEQERLAQLERAEQERK-------ERERQEQER 403
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKA----EEAKKADEAKKAEEKKKADELKKAEELKKaeekkkaEEAKKAEED 1575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  404 K----RQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQR--QLEWERNRRQELLNQRNKEQEDivvlKAKKKT 477
Cdd:PTZ00121 1576 KnmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEE----KKKAEE 1651
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  478 LEFELEALNDKKHQLegklqdircrlttQRQEIESTNKSRELRIAEithlqqqlqesqqmlgrlipekqilNDQLKQVQQ 557
Cdd:PTZ00121 1652 LKKAEEENKIKAAEE-------------AKKAEEDKKKAEEAKKAE-------------------------EDEKKAAEA 1693
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  558 nslhrdslvtLKRALEAKELARQHLRDQLDEVEK-ETRSKLQEIdifnNQLKeLREIHNKQQLQKQKsmeAERLKQKEQE 636
Cdd:PTZ00121 1694 ----------LKKEAEEAKKAEELKKKEAEEKKKaEELKKAEEE----NKIK-AEEAKKEAEEDKKK---AEEAKKDEEE 1755
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  637 RKIIELEKQKEEAQRRAQERDKQWL--EHVQQEDEhqrPRKLHEEEKLK 683
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDE---KRRMEVDKKIK 1801
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
375-849 3.03e-10

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 64.61  E-value: 3.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   375 QQRKEQERL--------AQLERAEQERKERERQEQERKRQLELEKqlekqrelerqreeerrkeierreaakRELERQRQ 446
Cdd:pfam02463  148 AMMKPERRLeieeeaagSRLKRKKKEALKKLIEETENLAELIIDL---------------------------EELKLQEL 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   447 LEwERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLegklqdircrLTTQRQEIESTNKSRELRIAEITH 526
Cdd:pfam02463  201 KL-KEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL----------LRDEQEEIESSKQEIEKEEEKLAQ 269
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   527 LQQQLQESQQmlgrlipEKQILNDQLKQVQQNSLhrdslvTLKRALEAKELARQHLRDQLDEVEKETRSKLQEID---IF 603
Cdd:pfam02463  270 VLKENKEEEK-------EKKLQEEELKLLAKEEE------ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKkekEE 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   604 NNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQ-WLEH---------VQQEDEHQRP 673
Cdd:pfam02463  337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLkEEELelkseeekeAQLLLELARQ 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   674 RKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKG-PLTISAQENVKVVYYRALYPFE 752
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLlKETQLVKLQEQLELLLSRQKLE 496
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   753 SRSHDEITIQPGDIVMVDESQTGEPGWLGGE--LKGKTGWFPANYAEKIPENEVPAPVKPVTDSTSAPAPKLALRETPAP 830
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISAhgRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLG 576
                          490
                   ....*....|....*....
gi 768021416   831 LAVTSSEPSTTPNNWADFS 849
Cdd:pfam02463  577 ARKLRLLIPKLKLPLKSIA 595
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
376-685 4.86e-10

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 63.93  E-value: 4.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   376 QRKEQERLAQL-ERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRkeierreaakRELER-QRQLEWERNR 453
Cdd:TIGR02169  669 SRSEPAELQRLrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE----------KEIEQlEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   454 RQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQR--------QEIESTNKSRELRIAEIT 525
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   526 HLQQQLQESQQMLGRLIPEKQILNDQLKQvQQNSLHR--DSLVTLKRALEA----KELARQHLRDQLDEVEKET---RSK 596
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKE-QIKSIEKeiENLNGKKEELEEeleeLEAALRDLESRLGDLKKERdelEAQ 897
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   597 LQEIDIFNNQLKELREIHNKQ--QLQKQKSMEAERLKQKEQERKIIELEKQKE------EAQRRAQERDKQWLEHV---- 664
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEIRALEPVnmla 977
                          330       340
                   ....*....|....*....|....
gi 768021416   665 -QQEDEHQRPRKLHEE--EKLKRE 685
Cdd:TIGR02169  978 iQEYEEVLKRLDELKEkrAKLEEE 1001
SH3_CIN85_3 cd12057
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
744-797 5.30e-10

Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212990 [Multi-domain]  Cd Length: 56  Bit Score: 56.06  E-value: 5.30e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd12057     1 YCKVLFPYEAQNEDELTIKEGDIVTLISKDCIDAGWWEGELNGRRGVFPDNFVK 54
SH3_betaPIX cd12061
Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho ...
746-799 5.83e-10

Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7) or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212994 [Multi-domain]  Cd Length: 54  Bit Score: 55.85  E-value: 5.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd12061     3 RAKFNFQQTNEDELSFSKGDVIHVTRVEEG--GWWEGTHNGRTGWFPSNYVREI 54
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
334-685 6.20e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.54  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  334 VLEDEQQQLEKKLpvtfEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLEraeQERKERerqeqeRKRQLELEKQL 413
Cdd:PRK03918  369 AKKEELERLKKRL----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---KEIKEL------KKAIEELKKAK 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  414 EKqrelerqreeerrkeierREAAKRELERQrqlewernRRQELLNQRNKEQEDIvvlKAKKKTLEFELEALNDKKHQLE 493
Cdd:PRK03918  436 GK------------------CPVCGRELTEE--------HRKELLEEYTAELKRI---EKELKEIEEKERKLRKELRELE 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  494 GKLQDIRcRLTTQRQ---EIEST-NKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQnslhrdslvtLK 569
Cdd:PRK03918  487 KVLKKES-ELIKLKElaeQLKELeEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----------LK 555
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  570 RALEAKELARQHLRDQLDEVEKETRSK-LQEIDIFNNQLKELREIHNK--------QQLQ-KQKSMEAERLKQKEQERKI 639
Cdd:PRK03918  556 KKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEPFYNEylelkdaeKELErEEKELKKLEEELDKAFEEL 635
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 768021416  640 IELEKQKEEAQRRAQErdkqwLEHVQQEDEHQRPRKLHEEekLKRE 685
Cdd:PRK03918  636 AETEKRLEELRKELEE-----LEKKYSEEEYEELREEYLE--LSRE 674
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
746-798 6.25e-10

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 55.50  E-value: 6.25e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV---DESqtgepGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11827     3 KALYAYDAQDTDELSFNEGDIIEIlkeDPS-----GWWTGRLRGKEGLFPGNYVEK 53
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
460-793 7.07e-10

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 62.15  E-value: 7.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  460 QRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLqqqlqesqqmlg 539
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER------------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  540 rlipeKQILNDQLKQVQQNSLHRDSLVTLkraLEAKELARqhLRDQLDEVEKETRSKLQEIDifnnQLKELREIHNKQQL 619
Cdd:COG3883    85 -----REELGERARALYRSGGSVSYLDVL---LGSESFSD--FLDRLSALSKIADADADLLE----ELKADKAELEAKKA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  620 QKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQ 699
Cdd:COG3883   151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  700 EAQDKLGRLFHQHQEPAKPAVQAPWSTAEKGPLTISAQENVKVVYYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGW 779
Cdd:COG3883   231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGA 310
                         330
                  ....*....|....
gi 768021416  780 LGGELKGKTGWFPA 793
Cdd:COG3883   311 GGVGSGGGAGAVVG 324
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
351-685 7.79e-10

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 62.83  E-value: 7.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   351 EDKKRENFERgnLELEKRRQALlEQQRKEQERLAQLERAEQERK-----------ERERQEQERKRQLELEKQLEKQREL 419
Cdd:pfam17380  286 ERQQQEKFEK--MEQERLRQEK-EEKAREVERRRKLEEAEKARQaemdrqaaiyaEQERMAMERERELERIRQEERKREL 362
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   420 ERQREEERRKEIERReaakRELERqrqLEWERNRRQELLNQRnkeqedivvLKAKKKTLEFELEALNDKKHQLEgKLQDI 499
Cdd:pfam17380  363 ERIRQEEIAMEISRM----RELER---LQMERQQKNERVRQE---------LEAARKVKILEEERQRKIQQQKV-EMEQI 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   500 RCRLTTQRQeiestnksRELRIAEithlqqqlQESQQMLGRLIPEKQILNDQLKQV-QQNSLHRDSLVTLKRALEAKELA 578
Cdd:pfam17380  426 RAEQEEARQ--------REVRRLE--------EERAREMERVRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDRKRA 489
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   579 RQHLRDQLDEVEKETRSKLQEidifnnqLKELREIHNKQQLQKQKSM--EAERLKQKEQERKIIELEKQKE-EAQRRAQE 655
Cdd:pfam17380  490 EEQRRKILEKELEERKQAMIE-------EERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEMEERRRiQEQMRKAT 562
                          330       340       350
                   ....*....|....*....|....*....|
gi 768021416   656 RDKQWLEHVQQEDEHQrpRKLHEEEKLKRE 685
Cdd:pfam17380  563 EERSRLEAMEREREMM--RQIVESEKARAE 590
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
741-797 8.89e-10

Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212760 [Multi-domain]  Cd Length: 52  Bit Score: 55.02  E-value: 8.89e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  741 KVVyyrALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11826     1 KVV---ALYDYTADKDDELSFQEGDIIYV--TKKNDDGWYEGVLNGVTGLFPGNYVE 52
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
746-797 1.14e-09

Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 54.73  E-value: 1.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11840     3 IALFPYTAQNEDELSFQKGDIINVLSKD--DPDWWRGELNGQTGLFPSNYVE 52
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
744-795 1.35e-09

Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212712 [Multi-domain]  Cd Length: 51  Bit Score: 54.43  E-value: 1.35e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGGELKGKTGWFPANY 795
Cdd:cd11778     1 YVEALYDYEAQGDDEISIRVGDRIAVIRGDDGS-GWTYGEINGVKGLFPTSY 51
PTZ00121 PTZ00121
MAEBL; Provisional
336-686 1.48e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  336 EDEQQQLEKKLPVTFEDKKRENFErgnlELEKRRQALLEQQRKEQErlaQLERAEQERKERERQEQERKRQLELEKQLEK 415
Cdd:PTZ00121 1078 DFDFDAKEDNRADEATEEAFGKAE----EAKKTETGKAEEARKAEE---AKKKAEDARKAEEARKAEDARKAEEARKAED 1150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  416 qrelerqreeERRKEIERREAAKRELERQRQLE----WERNRRQELLNQRN--KEQEDIVVLKAKKKTlEFELEALNDKK 489
Cdd:PTZ00121 1151 ----------AKRVEIARKAEDARKAEEARKAEdakkAEAARKAEEVRKAEelRKAEDARKAEAARKA-EEERKAEEARK 1219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  490 HQLEGKLQDIRcRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIP--EKQILNDQLKQVQQ----NSLHRD 563
Cdd:PTZ00121 1220 AEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkaEEARKADELKKAEEkkkaDEAKKA 1298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  564 SLVtlKRALEAKELARQHLR-DQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIEL 642
Cdd:PTZ00121 1299 EEK--KKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 768021416  643 EKQKEEAQRRAQERDKQwlEHVQQEDEHQRPR----KLHEEEKLKREE 686
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKA--DEAKKKAEEDKKKadelKKAAAAKKKADE 1422
SH3_UBASH3 cd11791
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called ...
745-798 1.85e-09

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called TULA (T cell Ubiquitin LigAnd) family of proteins; UBASH3 or TULA proteins are also referred to as Suppressor of T cell receptor Signaling (STS) proteins. They contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. In some vertebrates, there are two TULA family proteins, called UBASH3A (also called TULA or STS-2) and UBASH3B (also called TULA-2 or STS-1), which show partly overlapping as well as distinct functions. UBASH3B is widely expressed while UBASH3A is only found in lymphoid cells. UBASH3A facilitates apoptosis induced in T cells through its interaction with the apoptosis-inducing factor AIF. UBASH3B is an active phosphatase while UBASH3A is not. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212725 [Multi-domain]  Cd Length: 59  Bit Score: 54.61  E-value: 1.85e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQTGEP--GWLGG--ELKGKTGWFPANYAEK 798
Cdd:cd11791     2 LRVLYPYTPQEEDELELVPGDYIYVSPEELDSSsdGWVEGtsWLTGCSGLLPENYTEK 59
SH3_PACSIN cd11843
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ...
746-797 2.09e-09

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212777 [Multi-domain]  Cd Length: 53  Bit Score: 53.96  E-value: 2.09e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11843     3 RALYDYEGQESDELSFKAGDILTKLEEED-EQGWCKGRLDGRVGLYPANYVE 53
Caldesmon pfam02029
Caldesmon;
387-686 2.79e-09

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 60.65  E-value: 2.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   387 ERAEQERKERERQEQERKRQLE--------LEKQLEKQRELERQREEERRKEIERREAA------KRELERQRQLEWERN 452
Cdd:pfam02029    5 EEAARERRRRAREERRRQKEEEepsgqvteSVEPNEHNSYEEDSELKPSGQGGLDEEEAfldrtaKREERRQKRLQEALE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   453 RRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKL----------QDIRCRLTTQRQEIESTNKSRELRIA 522
Cdd:pfam02029   85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeeteirekEYQENKWSTEVRQAEEEGEEEEDKSE 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   523 EITHLQQQLQESQQMLGRLIPE--------KQILNDQLKQVQQNSLHRDSLVTlkrALEAKELARQHLRDQLDEVEKETR 594
Cdd:pfam02029  165 EAEEVPTENFAKEEVKDEKIKKekkvkyesKVFLDQKRGHPEVKSQNGEEEVT---KLKVTTKRRQGGLSQSQEREEEAE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   595 SKLQEidifNNQLKELReihnkQQLQKQKSMEAERLKQKEQERkIIELE--KQKEEAQRRAQErdkqwlehvqqedEHQR 672
Cdd:pfam02029  242 VFLEA----EQKLEELR-----RRRQEKESEEFEKLRQKQQEA-ELELEelKKKREERRKLLE-------------EEEQ 298
                          330
                   ....*....|....
gi 768021416   673 PRKLHEEEKLKREE 686
Cdd:pfam02029  299 RRKQEEAERKLREE 312
Caldesmon pfam02029
Caldesmon;
379-686 3.31e-09

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 60.65  E-value: 3.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   379 EQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERRE---------AAKRELERQRQLEW 449
Cdd:pfam02029    2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLdeeeafldrTAKREERRQKRLQE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   450 ERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKL----------QDIRCRLTTQRQEIESTNKSREL 519
Cdd:pfam02029   82 ALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeeteirekEYQENKWSTEVRQAEEEGEEEED 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   520 RIAEITHLQQQLQESQQMLGRLIPE--------KQILNDQLKQVQQNSLHRDSLVTlkrALEAKELARQHLRDQLDEVEK 591
Cdd:pfam02029  162 KSEEAEEVPTENFAKEEVKDEKIKKekkvkyesKVFLDQKRGHPEVKSQNGEEEVT---KLKVTTKRRQGGLSQSQEREE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   592 ETRSKLQEidifNNQLKELReihnkQQLQKQKSMEAERLKQKEQERkIIELE--KQKEEAQRRAQERDKQwlehvQQEDE 669
Cdd:pfam02029  239 EAEVFLEA----EQKLEELR-----RRRQEKESEEFEKLRQKQQEA-ELELEelKKKREERRKLLEEEEQ-----RRKQE 303
                          330
                   ....*....|....*..
gi 768021416   670 HQRPRKLHEEEKLKREE 686
Cdd:pfam02029  304 EAERKLREEEEKRRMKE 320
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
331-653 3.33e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 61.24  E-value: 3.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   331 EEPVLEDEQQQLEKKLPVTfeDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERA------EQERKERERQEQERK 404
Cdd:TIGR02169  731 EEEKLKERLEELEEDLSSL--EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsriPEIQAELSKLEEEVS 808
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   405 RQLELEKQLEKQRElerqreeerrkeierreaaKRELERQrQLEWERN----RRQELLNQRNKEQEDIVVLKAKKKTLEF 480
Cdd:TIGR02169  809 RIEARLREIEQKLN-------------------RLTLEKE-YLEKEIQelqeQRIDLKEQIKSIEKEIENLNGKKEELEE 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   481 ELEALNDKKHQLEGKLQDIRcrltTQRQEIESTNKSRELRIAEIthlQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSL 560
Cdd:TIGR02169  869 ELEELEAALRDLESRLGDLK----KERDELEAQLRELERKIEEL---EAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   561 HRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREihnkqqlqKQKSMEAERlkqKEQERKII 640
Cdd:TIGR02169  942 EDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE--------KRAKLEEER---KAILERIE 1010
                          330
                   ....*....|...
gi 768021416   641 ELEKQKEEAQRRA 653
Cdd:TIGR02169 1011 EYEKKKREVFMEA 1023
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
744-797 3.34e-09

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 53.48  E-value: 3.34e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGGE-LKGKTGWFPANYAE 797
Cdd:cd11763     1 KVRALYDFDSQPSGELSLRAGEVLTITRQDVGD-GWLEGRnSRGEVGLFPSSYVE 54
SH3_alphaPIX cd12060
Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho ...
746-799 3.50e-09

Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6) or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212993  Cd Length: 58  Bit Score: 53.85  E-value: 3.50e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd12060     5 KARFNFKQTNEDELSVCKGDIIYVTRVEEG--GWWEGTLNGKTGWFPSNYVREI 56
SH3_CD2AP-like_1 cd11873
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ...
745-798 5.15e-09

First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212806 [Multi-domain]  Cd Length: 53  Bit Score: 53.04  E-value: 5.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVmVDESQTgEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11873     2 VIVEFDYDAEEPDELTLKVGDII-TNVKKM-EEGWWEGTLNGKRGMFPDNFVKV 53
SH3_MLK4 cd12058
Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), ...
745-795 5.15e-09

Src Homology 3 domain of Mixed Lineage Kinase 4; MLK4 is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. MLK4 contains an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212991 [Multi-domain]  Cd Length: 58  Bit Score: 53.02  E-value: 5.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMV---DESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd12058     2 WTALYDYEASGEDELSLRRGDVVEVlsqDAAVSGDDGWWAGKIRHRLGIFPANY 55
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
338-713 6.62e-09

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 59.98  E-value: 6.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   338 EQQQLEKKLPVTFEDKKRENFER--GNLELEKRRQALLEQQRKE-----QERLAQLERAEQERKERERQEQERKRQLELE 410
Cdd:TIGR00618  268 RIEELRAQEAVLEETQERINRARkaAPLAAHIKAVTQIEQQAQRihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   411 KQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKH 490
Cdd:TIGR00618  348 QTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   491 QLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGrlipEKQILNDQLKQVQQNSLHR-DSLVTLK 569
Cdd:TIGR00618  428 HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ----TKEQIHLQETRKKAVVLARlLELQEEP 503
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   570 RALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREI-HNKQQLQKQksmeAERLKQKEQErkiielEKQKEE 648
Cdd:TIGR00618  504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVyHQLTSERKQ----RASLKEQMQE------IQQSFS 573
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416   649 AQRRAQERDKQWLEHVQQEDEHQRP--RKLHEEEKLKREESvkkkDGEEKGKQEAQDKLGRLFHQHQ 713
Cdd:TIGR00618  574 ILTQCDNRSKEDIPNLQNITVRLQDltEKLSEAEDMLACEQ----HALLRKLQPEQDLQDVRLHLQQ 636
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
330-517 8.40e-09

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 59.19  E-value: 8.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   330 PEEPV-LEDEQQQLEKKLPVTFEDKKRENFERGN---LELEKRRQALLEQQRKEQErlaQLERAEQERKERERQEQERKR 405
Cdd:pfam15709  311 SEEERsEEDPSKALLEKREQEKASRDRLRAERAEmrrLEVERKRREQEEQRRLQQE---QLERAEKMREELELEQQRRFE 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   406 QLELEKQlekQRELERQREEERRKEIERREAAKRELERQRQLEWERnRRQELlnQRNKEQEDIVVLKAKKKTL-EFELEA 484
Cdd:pfam15709  388 EIRLRKQ---RLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRR-KLQEL--QRKKQQEEAERAEAEKQRQkELEMQL 461
                          170       180       190
                   ....*....|....*....|....*....|...
gi 768021416   485 LNDKKHQLEGKLQDircRLTTQRQEIESTNKSR 517
Cdd:pfam15709  462 AEEQKRLMEMAEEE---RLEYQRQKQEAEEKAR 491
SH3_VAV_2 cd11830
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ...
747-798 8.47e-09

C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212764 [Multi-domain]  Cd Length: 54  Bit Score: 52.63  E-value: 8.47e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11830     4 ARYDFCARDMRELSLKEGDVVKI-YNKKGQQGWWRGEINGRIGWFPSTYVEE 54
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
436-653 8.47e-09

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 58.62  E-value: 8.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  436 AAKRELER-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIestn 514
Cdd:COG4942    31 QLQQEIAElEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL---- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  515 kSRELRIAEITHLQQQLQESQQMLG------RLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKelaRQHLRDQLDE 588
Cdd:COG4942   107 -AELLRALYRLGRQPPLALLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAE---RAELEALLAE 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  589 VEKETRSKLQEIDIFNNQLKELreihNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRA 653
Cdd:COG4942   183 LEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
SH3_Cortactin cd11959
Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src ...
747-797 9.20e-09

Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src kinase. It is an actin regulatory protein that binds to the Arp2/3 complex and stabilizes branched actin filaments. It is involved in cellular processes that affect cell motility, adhesion, migration, endocytosis, and invasion. It is expressed ubiquitously except in hematopoietic cells, where the homolog hematopoietic lineage cell-specific 1 (HS1) is expressed instead. Cortactin contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region interacts with the Arp2/3 complex and F-actin, and is crucial in regulating branched actin assembly. Cortactin also serves as a scaffold and provides a bridge to the actin cytoskeleton for membrane trafficking and signaling proteins that bind to its SH3 domain. Binding partners for the SH3 domain of cortactin include dynamin2, N-WASp, MIM, FGD1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212892 [Multi-domain]  Cd Length: 53  Bit Score: 52.42  E-value: 9.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  747 ALYPFESRSHDEITIQPGDIV----MVDEsqtgepGWLGGELKGKTGWFPANYAE 797
Cdd:cd11959     4 ALYDYQAADDDEISFDPDDIItnieMIDE------GWWRGVCRGKYGLFPANYVE 52
SH3_Eve1_5 cd11818
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
746-795 1.04e-08

Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212752 [Multi-domain]  Cd Length: 50  Bit Score: 52.10  E-value: 1.04e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpgWLGGELKGKTGWFPANY 795
Cdd:cd11818     3 RALYDFTGENEDELSFKAGDIITELESIDEE--WMSGELRGKSGIFPKNF 50
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
746-793 1.21e-08

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 51.82  E-value: 1.21e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 768021416   746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELK-GKTGWFPA 793
Cdd:pfam00018    1 VALYDYTAQEPDELSFKKGDIIIVLEKS--EDGWWKGRNKgGKEGLIPS 47
SH3_MLK1-3 cd12059
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ...
744-795 1.21e-08

Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212992 [Multi-domain]  Cd Length: 58  Bit Score: 52.08  E-value: 1.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMV---DESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd12059     1 VWTAVFDYEASAEDELTLRRGDRVEVlskDSAVSGDEGWWTGKINDRVGIFPSNY 55
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
335-687 1.77e-08

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 58.49  E-value: 1.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLpvtfeDKKRENFERGNLELEKRRQALL---EQQRKEQERLA----QLERAEQERKERERQEQERKRQL 407
Cdd:TIGR04523  223 LKKQNNQLKDNI-----EKKQQEINEKTTEISNTQTQLNqlkDEQNKIKKQLSekqkELEQNNKKIKELEKQLNQLKSEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   408 -------------ELEKQLEKQRELERQREEERRKEIERREAAKREL---------------ERQRQLEWERNRRQELLN 459
Cdd:TIGR04523  298 sdlnnqkeqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIsqlkkeltnsesensEKQRELEEKQNEIEKLKK 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   460 QRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEIThlqqqlqesqqmlg 539
Cdd:TIGR04523  378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-------------- 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   540 RLIPEKQILNDQLKQVQQnslHRDSlvtLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREihNKQQL 619
Cdd:TIGR04523  444 DLTNQDSVKELIIKNLDN---TRES---LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE--KVKDL 515
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416   620 QKQKSMEAERLKQ-----KEQERKIIELEKQKEEAQrraQERDKQWLEHVQQEDEhQRPRKLHEE-EKLKREES 687
Cdd:TIGR04523  516 TKKISSLKEKIEKlesekKEKESKISDLEDELNKDD---FELKKENLEKEIDEKN-KEIEELKQTqKSLKKKQE 585
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
745-798 2.54e-08

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 51.11  E-value: 2.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11766     2 AVVKFNYEAQREDELSLRKGDRVLVLEKSSD--GWWRGECNGQVGWFPSNYVTE 53
SH3_VAV2_2 cd11977
C-terminal (or second) Src homology 3 domain of VAV2 protein; VAV2 is widely expressed and ...
747-798 2.57e-08

C-terminal (or second) Src homology 3 domain of VAV2 protein; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212910 [Multi-domain]  Cd Length: 58  Bit Score: 51.17  E-value: 2.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11977     5 ARYNFAARDMRELSLREGDVVRIYSRIGGDQGWWKGETNGRIGWFPSTYVEE 56
SH3_ephexin1_like cd11793
Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange ...
747-797 2.57e-08

Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange factors; Members of this family contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and C-terminal SH3 domains. They include the Rho guanine nucleotide exchange factors ARHGEF5, ARHGEF16, ARHGEF19, ARHGEF26, ARHGEF27 (also called ephexin-1), and similar proteins, and are also called ephexins because they interact directly with ephrin A receptors. GEFs interact with Rho GTPases via their DH domains to catalyze nucleotide exchange by stabilizing the nucleotide-free GTPase intermediate. They play important roles in neuronal development. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212727 [Multi-domain]  Cd Length: 55  Bit Score: 51.18  E-value: 2.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGE--LKGKTGWFPANYAE 797
Cdd:cd11793     4 CVHAYTAQQPDELTLEEGDVVNV--LRKMPDGWYEGErlRDGERGWFPSSYTE 54
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
745-798 2.80e-08

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 51.10  E-value: 2.80e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDEsqTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11856     2 YVAIADYEAQGDDEISLQEGEVVEVLE--KNDSGWWYVRKGDKEGWVPASYLEP 53
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
745-797 3.30e-08

Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212737 [Multi-domain]  Cd Length: 55  Bit Score: 50.72  E-value: 3.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdESQTGEpGWLGGELKGKTGWFPANYAE 797
Cdd:cd11803     3 CRALYDFEPENEGELGFKEGDIITL-TNQIDE-NWYEGMVNGQSGFFPVNYVE 53
SH3_VAV3_2 cd11978
C-terminal (or second) Src homology 3 domain of VAV3 protein; VAV3 is ubiquitously expressed ...
747-798 3.94e-08

C-terminal (or second) Src homology 3 domain of VAV3 protein; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. It has been implicated to function in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212911 [Multi-domain]  Cd Length: 56  Bit Score: 50.79  E-value: 3.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdESQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11978     5 ARYDFCARDMRELSLLKGDVVKI-YTKMSTNGWWRGEVNGRVGWFPSTYVEE 55
SH3_Intersectin_3 cd11838
Third Src homology 3 domain (or SH3C) of Intersectin; Intersectins (ITSNs) are adaptor ...
744-798 4.31e-08

Third Src homology 3 domain (or SH3C) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The third SH3 domain (or SH3C) of ITSN1 has been shown to bind many proteins including dynamin1/2, CIN85, c-Cbl, SHIP2, Reps1, synaptojanin-1, and WNK, among others. The SH3C of ITSN2 has been shown to bind the K15 protein of Kaposi's sarcoma-associated herpesvirus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212772 [Multi-domain]  Cd Length: 52  Bit Score: 50.49  E-value: 4.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDEsQTGEpgWLGGELKGKTGWFPANYAEK 798
Cdd:cd11838     1 EYIALYPYESNEPGDLTFNAGDVILVTK-KDGE--WWTGTIGDRTGIFPSNYVRP 52
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
746-799 5.94e-08

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 50.40  E-value: 5.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV---DESQTGEPGWLGG--ELKGKTGWFPANYAEKI 799
Cdd:cd11790     6 RATHDYTAEDTDELTFEKGDVILVipfDDPEEQDEGWLMGvkESTGCRGVFPENFTERI 64
SH3_GAS7 cd11829
Src homology 3 domain of Growth Arrest Specific protein 7; GAS7 is mainly expressed in the ...
746-795 6.19e-08

Src homology 3 domain of Growth Arrest Specific protein 7; GAS7 is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212763 [Multi-domain]  Cd Length: 52  Bit Score: 49.82  E-value: 6.19e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  746 RALYPFESRSHDE-ITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11829     3 RTLYAFTGEQHQQgLSFEAGELIRV--LQAPDGGWWEGEKDGLRGWFPASY 51
SH3_MLK cd11876
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), ...
747-795 6.23e-08

Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212809 [Multi-domain]  Cd Length: 58  Bit Score: 50.20  E-value: 6.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMV---DESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11876     4 ALFDYDARGEDELTLRRGQPVEVlskDAAVSGDEGWWTGKIGDKVGIFPSNY 55
SH3_Intersectin_4 cd11839
Fourth Src homology 3 domain (or SH3D) of Intersectin; Intersectins (ITSNs) are adaptor ...
746-798 6.76e-08

Fourth Src homology 3 domain (or SH3D) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fourth SH3 domain (or SH3D) of ITSN1 has been shown to bind SHIP2, Numb, CdGAP, and N-WASP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212773 [Multi-domain]  Cd Length: 58  Bit Score: 50.03  E-value: 6.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGK-----TGWFPANYAEK 798
Cdd:cd11839     3 QVIAPFTATAENQLSLAVGQLVLVRKKSPS--GWWEGELQARgkkrqIGWFPANYVKL 58
SH3_Nebulin_family_C cd11789
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins ...
745-798 6.94e-08

C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212723 [Multi-domain]  Cd Length: 55  Bit Score: 50.01  E-value: 6.94e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVM----VDEsqtgepGWLGGELK--GKTGWFPANYAEK 798
Cdd:cd11789     2 YRAMYDYAAADDDEVSFQEGDVIInveiIDD------GWMEGTVQrtGQSGMLPANYVEL 55
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
745-799 7.02e-08

C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212867 [Multi-domain]  Cd Length: 59  Bit Score: 50.00  E-value: 7.02e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVmVDESQTGEpGWLGG--ELKGKTGWFPANYAEKI 799
Cdd:cd11934     5 YRAVYDYNAADEDEVSFQDGDTI-VNVQQIDD-GWMYGtvERTGDTGMLPANYVEAI 59
SH3_Tks4_2 cd12076
Second Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also ...
745-798 7.62e-08

Second Src homology 3 domain of Tyrosine kinase substrate with four SH3 domains; Tks4, also called SH3 and PX domain-containing protein 2B (SH3PXD2B) or HOFI, is a Src substrate and scaffolding protein that plays an important role in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. It is required in the formation of functional podosomes, EGF-induced membrane ruffling, and lamellipodia generation. It plays an important role in cellular attachment and cell spreading. Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. It contains an N-terminal Phox homology (PX) domain and four SH3 domains. This model characterizes the second SH3 domain of Tks4. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213009 [Multi-domain]  Cd Length: 54  Bit Score: 49.65  E-value: 7.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd12076     3 YTVIYPYTARDQDEINLEKGAVVEV--IQKNLEGWWKIRYQGKEGWAPASYLKK 54
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
746-797 7.86e-08

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 49.62  E-value: 7.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  746 RALYPFESRSHDEITIQPGDIV----MVDEsqtgepGWLGGEL-KGKTGWFPANYAE 797
Cdd:cd11819     3 KALYDYQAAEDNEISFVEGDIItqieQIDE------GWWLGVNaKGQKGLFPANYVE 53
SH3_HS1 cd12073
Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 ...
747-797 7.91e-08

Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 (hematopoietic cell-specific Lyn substrate 1), is a cortactin homolog expressed specifically in hematopoietic cells. It is an actin regulatory protein that binds the Arp2/3 complex and stabilizes branched actin filaments. It is required for cell spreading and signaling in lymphocytes. It regulates cytoskeletal remodeling that controls lymphocyte trafficking, and it also affects tissue invasion and infiltration of leukemic B cells. Like cortactin, HS1 contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region binds the Arp2/3 complex and F-actin, while the C-terminal region acts as an adaptor or scaffold that can connect varied proteins that bind the SH3 domain within the actin network. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213006 [Multi-domain]  Cd Length: 55  Bit Score: 49.83  E-value: 7.91e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  747 ALYPFESRSHDEITIQPGDIV----MVDEsqtgepGWLGGELKGKTGWFPANYAE 797
Cdd:cd12073     5 ALYDYQGEGDDEISFDPQETItdieMVDE------GWWKGTCHGHRGLFPANYVE 53
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
746-798 8.78e-08

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 49.55  E-value: 8.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTgePGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11805     3 QALYDFNPQEPGELEFRRGDIITVLDSSD--PDWWKGELRGRVGIFPANYVQP 53
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
338-683 9.39e-08

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 55.31  E-value: 9.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   338 EQQQLEKKLpVTFEDKKREnfERGNLELEK-RRQALLEQQRKEQERL-----------AQLERAEQERKERERQEQERKR 405
Cdd:pfam13868   25 DAQIAEKKR-IKAEEKEEE--RRLDEMMEEeRERALEEEEEKEEERKeerkryrqeleEQIEEREQKRQEEYEEKLQERE 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   406 QL----------ELEKQLEKQrelerqreeerrkeiERREAAKRELERQRQlewERNRRQELLNQRNKEQEDIVVLKAKK 475
Cdd:pfam13868  102 QMdeiveriqeeDQAEAEEKL---------------EKQRQLREEIDEFNE---EQAEWKELEKEEEREEDERILEYLKE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   476 KTLEFelEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEithlqqqlqesqqmlgRLIPEKQILNDQLKQV 555
Cdd:pfam13868  164 KAERE--EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK----------------LYQEEQERKERQKERE 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   556 QQnslhrdslvtLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKsmeaERLKQKEQ 635
Cdd:pfam13868  226 EA----------EKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEK----RRMKRLEH 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 768021416   636 ERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQrpRKLHEEEKLK 683
Cdd:pfam13868  292 RRELEKQIEEREEQRAAEREEELEEGERLREEEAER--RERIEEERQK 337
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
746-798 1.22e-07

Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212754 [Multi-domain]  Cd Length: 54  Bit Score: 49.00  E-value: 1.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV-DESqtgEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11820     4 RALYDFEAAEDNELTFKAGEIITVlDDS---DPNWWKGSNHRGEGLFPANFVTA 54
SH3_Pex13p_fungal cd11771
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ...
746-797 1.25e-07

Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212705 [Multi-domain]  Cd Length: 60  Bit Score: 49.20  E-value: 1.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  746 RALYPFESRSHD-EITIQPGDIVMVDE--SQTGEP-GWLGGELK-GKTGWFPANYAE 797
Cdd:cd11771     3 RALYDFTPENPEmELSLKKGDIVAVLSktDPLGRDsEWWKGRTRdGRIGWFPSNYVE 59
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
366-687 1.37e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 55.95  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   366 EKRRQALLEQQRKEQERLAQlerAEQERKERERQEQerkrQLELEK-QLEKQRELERQREEERRKEIERREAAKRELER- 443
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQK---AESELKELEKKHQ----QLCEEKnALQEQLQAETELCAEAEEMRARLAARKQELEEi 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   444 ----QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTT---QRQEIESTNKS 516
Cdd:pfam01576   77 lhelESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLledQNSKLSKERKL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   517 RELRIAEITHLQQQLQESQQMLGRLIPEKQI----LNDQLKQVQQNslhRDSLVTLKRALEAK--ELARQH--------- 581
Cdd:pfam01576  157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKG---RQELEKAKRKLEGEstDLQEQIaelqaqiae 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   582 LRDQLDEVEKETRSKLQEID----IFNNQLKELREIHNkQQLQKQKSMEAERL--KQKEQERKII--ELEKQKEEAQrra 653
Cdd:pfam01576  234 LRAQLAKKEEELQAALARLEeetaQKNNALKKIRELEA-QISELQEDLESERAarNKAEKQRRDLgeELEALKTELE--- 309
                          330       340       350
                   ....*....|....*....|....*....|....
gi 768021416   654 qerDKQWLEHVQQEDEHQRPRKLHEEEKLKREES 687
Cdd:pfam01576  310 ---DTLDTTAAQQELRSKREQEVTELKKALEEET 340
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
342-682 1.52e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 55.75  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   342 LEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQ-----ERLAQLERAEQERkeRERQEQERKRQLELEKQLEKQ 416
Cdd:TIGR00618  175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpdtyhERKQVLEKELKHL--REALQQTQQSHAYLTQKREAQ 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   417 relerqreeerrkeierreaaKRELERQRQLEWERNRRQELLNQ--RNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEG 494
Cdd:TIGR00618  253 ---------------------EEQLKKQQLLKQLRARIEELRAQeaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   495 KLQDIRCRLTT-----------QRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQI-LNDQLKQVQQNSLHR 562
Cdd:TIGR00618  312 IHTELQSKMRSrakllmkraahVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtLTQHIHTLQQQKTTL 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   563 DSLVTLKRALEAKELARQHLRDQLDEVEKETRSKL------QEIDIFNNQLKELrEIHNKQQLQKQKSMEAERLKQKEQE 636
Cdd:TIGR00618  392 TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLahakkqQELQQRYAELCAA-AITCTAQCEKLEKIHLQESAQSLKE 470
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 768021416   637 RKiiELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRP---RKLHEEEKL 682
Cdd:TIGR00618  471 RE--QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcgSCIHPNPAR 517
SH3_DNMBP_C2_like cd11800
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ...
744-798 1.60e-07

Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. Also included in this subfamily is the second C-terminal SH3 domain of Rho guanine nucleotide exchange factor 37 (ARHGEF37), whose function is still unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212734 [Multi-domain]  Cd Length: 57  Bit Score: 48.91  E-value: 1.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQ--TGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11800     1 YYYALYTFEARSPGELSVTEGQVVTVLEKHdlKGNPEWWLVEDRGKQGYVPSNYLAK 57
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
366-495 1.64e-07

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 51.58  E-value: 1.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   366 EKRRQALLEQQRKEQERLAQLERAEQERKE-RERQEQERKRQLELEKQLEKQRELERQREEERrkeierreaAKRELERQ 444
Cdd:pfam05672   18 EKRRQAREQREREEQERLEKEEEERLRKEElRRRAEEERARREEEARRLEEERRREEEERQRK---------AEEEAEER 88
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   445 RQLEWERNRRQEllnQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGK 495
Cdd:pfam05672   89 EQREQEEQERLQ---KQKEEAEAKAREEAERQRQEREKIMQQEEQERLERK 136
SH3_Stac_1 cd11833
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) ...
744-798 1.69e-07

First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing (Stac) proteins; Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. This model represents the first C-terminal SH3 domain of Stac1 and Stac3, and the single C-terminal SH3 domain of Stac2. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212767 [Multi-domain]  Cd Length: 53  Bit Score: 48.65  E-value: 1.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEpgWLGGELKGKTGWFPANYAEK 798
Cdd:cd11833     1 TYVALYKFKPQENEDLEMRPGDKITLLDDSNED--WWKGKIEDRVGFFPANFVQR 53
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
587-704 1.73e-07

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 54.96  E-value: 1.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   587 DEVEKETRSKLQEIDIFNNQLKELR----EIHNKQQLQKQKSMEAERLKQKEQERKIIEL--EKQKEEAQRRAQERDKQW 660
Cdd:pfam15709  376 EELELEQQRRFEEIRLRKQRLEEERqrqeEEERKQRLQLQAAQERARQQQEEFRRKLQELqrKKQQEEAERAEAEKQRQK 455
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 768021416   661 LEHVQQEDEHQRPRKLHEEEKLkrEESVKKKDGEEKGKQEAQDK 704
Cdd:pfam15709  456 ELEMQLAEEQKRLMEMAEEERL--EYQRQKQEAEEKARLEAEER 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
336-648 1.88e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   336 EDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQL--ERAEQERkERERQEQERKRQLELEKQL 413
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeeELAEAEA-EIEELEAQIEQLKEELKAL 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   414 EKQrelerqreeerrkeierREAAKRELERQRQ-LEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNdkkHQL 492
Cdd:TIGR02168  802 REA-----------------LDELRAELTLLNEeAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA---AEI 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   493 EgklqdircRLTTQRQEIEStnksrelriaEITHlqqqlqesqqmlgrlipekqILNDQLKQVQQNSLHRDSLVTLKRAL 572
Cdd:TIGR02168  862 E--------ELEELIEELES----------ELEA--------------------LLNERASLEEALALLRSELEELSEEL 903
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   573 EAKELARQHLRDQLDEV-EKETRSKLQEIDIfnnqlkELREIHNKQQLQKQKSMEAERLKQK---------EQERKIIEL 642
Cdd:TIGR02168  904 RELESKRSELRRELEELrEKLAQLELRLEGL------EVRIDNLQERLSEEYSLTLEEAEALenkieddeeEARRRLKRL 977

                   ....*.
gi 768021416   643 EKQKEE 648
Cdd:TIGR02168  978 ENKIKE 983
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
744-797 2.08e-07

Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212817 [Multi-domain]  Cd Length: 56  Bit Score: 48.48  E-value: 2.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIV-MVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11884     1 YVVAVRAYITRDQTLLSFHKGDVIkLLPKEGPLDPGWLFGTLDGRSGAFPKEYVQ 55
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
331-592 2.75e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 54.74  E-value: 2.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   331 EEPVLEDEQQQLEKklpVTFEDKKRENfergnlelEKRRQallEQQRKEQERLAQLERAEQERK---ERERQEQERKRQL 407
Cdd:pfam17380  339 QERMAMERERELER---IRQEERKREL--------ERIRQ---EEIAMEISRMRELERLQMERQqknERVRQELEAARKV 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   408 ELEKQlEKQRELERQREEERRKEIERREAAK-----------RELERQRQLEWERNRRQELLNQRNKEQedivvlkaKKK 476
Cdd:pfam17380  405 KILEE-ERQRKIQQQKVEMEQIRAEQEEARQrevrrleeeraREMERVRLEEQERQQQVERLRQQEEER--------KRK 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   477 TLEFELEAlNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQmlgRLIPE----KQILNDQL 552
Cdd:pfam17380  476 KLELEKEK-RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER---RREAEeerrKQQEMEER 551
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 768021416   553 KQVQQNSLhrdsLVTLKRA-LEAKELARQHLRdQLDEVEKE 592
Cdd:pfam17380  552 RRIQEQMR----KATEERSrLEAMEREREMMR-QIVESEKA 587
SH3_GRAF2 cd12065
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 2; GRAF2, also ...
746-797 3.01e-07

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase 2; GRAF2, also called Rho GTPase activating protein 10 (ARHGAP10) or PS-GAP, is a GAP with activity towards Cdc42 and RhoA. It regulates caspase-activated p21-activated protein kinase-2 (PAK-2p34). GRAF2 interacts with PAK-2p34, leading to its stabilization and decrease of cell death. It is highly expressed in skeletal muscle, and is involved in alpha-catenin recruitment at cell-cell junctions. GRAF2 contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212998 [Multi-domain]  Cd Length: 54  Bit Score: 48.06  E-value: 3.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIvMVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd12065     3 KAVYPCEAEHSSELSFEVGAI-FEDVTLSREPGWLEGTLNGKRGLIPENYVE 53
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
746-797 3.38e-07

Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212807 [Multi-domain]  Cd Length: 53  Bit Score: 47.71  E-value: 3.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  746 RALYPFESRSHDEITIQPGDIV-MVDESqtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11874     3 KVLFSYTPQNEDELELKVGDTIeVLGEV---EEGWWEGKLNGKVGVFPSNFVK 52
SH3_Nebulin_C cd11933
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ...
745-799 3.77e-07

C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212866 [Multi-domain]  Cd Length: 58  Bit Score: 48.08  E-value: 3.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMvdESQTGEPGWLGGELK--GKTGWFPANYAEKI 799
Cdd:cd11933     4 FRAMYDYRAADDDEVSFKDGDTIV--NVQTIDEGWMYGTVQrtGKTGMLPANYVEAI 58
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
743-797 4.00e-07

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212931 [Multi-domain]  Cd Length: 56  Bit Score: 47.64  E-value: 4.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  743 VYYRALYPFESRSHDEITIQPGDIVMVDESQTgEPGWLGGEL-KGKTGWFPANYAE 797
Cdd:cd11998     1 VRVRALYDYDGQEQDELSFKAGDELTKLEDED-EQGWCKGRLdSGQVGLYPANYVE 55
SH3_Nebulette_C cd11935
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a ...
745-799 4.09e-07

C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three nebulin repeats, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212868 [Multi-domain]  Cd Length: 58  Bit Score: 47.69  E-value: 4.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMvdESQTGEPGWLGGELK--GKTGWFPANYAEKI 799
Cdd:cd11935     3 YRAMYDYSAQDEDEVSFRDGDYIV--NVQPIDEGWMYGTVQrtGRTGMLPANYIEFV 57
SH3_Sorbs_1 cd11781
First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ...
746-797 4.31e-07

First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the first SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212715 [Multi-domain]  Cd Length: 53  Bit Score: 47.72  E-value: 4.31e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpgWLGGELKGKTGWFPANYAE 797
Cdd:cd11781     3 RALYPFKAQSAKELSLKKGDIIYIRRQIDKN--WYEGEHNGRVGIFPASYVE 52
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
746-795 4.39e-07

Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212897 [Multi-domain]  Cd Length: 55  Bit Score: 47.64  E-value: 4.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV-DESqtgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11964     4 RAIYDFEAAEDNELTFKAGDIITIlDDS---DPNWWKGETPQGTGLFPSNF 51
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
374-686 4.56e-07

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 53.12  E-value: 4.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   374 EQQRKEQERLAQLERAEQERKERERQEQ-ERKRQLELEKQLE------KQRELERQREEERRKEIERREAAKRELERQRQ 446
Cdd:pfam15558   20 EQRMRELQQQAALAWEELRRRDQKRQETlERERRLLLQQSQEqwqaekEQRKARLGREERRRADRREKQVIEKESRWREQ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   447 LEWERNRRQELLNQRNKEQEdivvlkAKKKTLEFEL----EALNDKKHQLEGKLQDI--RCRLTTQRQEIESTNKSRELR 520
Cdd:pfam15558  100 AEDQENQRQEKLERARQEAE------QRKQCQEQRLkekeEELQALREQNSLQLQERleEACHKRQLKEREEQKKVQENN 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   521 IAEithlqqqlqesqqmlgrlipekqILNDQLKQVQQNSLHRDSLVTLKRALEAKelarqHLRDQldevekETRSKLQEI 600
Cdd:pfam15558  174 LSE-----------------------LLNHQARKVLVDCQAKAEELLRRLSLEQS-----LQRSQ------ENYEQLVEE 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   601 difnnQLKELREIHNKQQLQKQKSME-AERLKQKEQERK--IIELEKQK-EEAQRRAQERDKQWLEHVQQ-----EDEHQ 671
Cdd:pfam15558  220 -----RHRELREKAQKEEEQFQRAKWrAEEKEEERQEHKeaLAELADRKiQQARQVAHKTVQDKAQRARElnlerEKNHH 294
                          330
                   ....*....|....*.
gi 768021416   672 RPR-KLHEEEKLKREE 686
Cdd:pfam15558  295 ILKlKVEKEEKCHREG 310
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
370-686 4.62e-07

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 54.20  E-value: 4.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   370 QALLEQQRKEQERLAQLERAEQ------ERKERERQEQERKRQLELEKQLEKQ--RELERQREEERRKEIERREAAKREL 441
Cdd:TIGR00618  156 QFLKAKSKEKKELLMNLFPLDQytqlalMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREAL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   442 ERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLE-----GKLQDIRCRLTTQRQEIESTNKS 516
Cdd:TIGR00618  236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   517 RELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLR---DQLDEVEKET 593
Cdd:TIGR00618  316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqQQKTTLTQKL 395
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   594 RSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQER---------KIIELEKQKEEAQRRAQERDKQWLEHV 664
Cdd:TIGR00618  396 QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYaelcaaaitCTAQCEKLEKIHLQESAQSLKEREQQL 475
                          330       340
                   ....*....|....*....|...
gi 768021416   665 QQ-EDEHQRPRKLHEEEKLKREE 686
Cdd:TIGR00618  476 QTkEQIHLQETRKKAVVLARLLE 498
SH3_GRAP2_C cd11950
C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
746-797 4.86e-07

C-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also has roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRAP2 binds to different motifs found in substrate peptides including the typical PxxP motif in hematopoietic progenitor kinase 1 (HPK1), the RxxK motif in SLP-76 and HPK1, and the RxxxxK motif in phosphatase-like protein HD-PTP. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212883 [Multi-domain]  Cd Length: 53  Bit Score: 47.51  E-value: 4.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11950     3 RALYDFEALEDDELGFNSGDVIEVLDSS--NPSWWKGRLHGKLGLFPANYVA 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
334-708 7.35e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 7.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   334 VLEDEQQQLEKKLPVtfEDKKRENFERGNLELEKRRQAL----------LEQQRKEQERL-AQLERAEqERKERERQEQE 402
Cdd:TIGR02168  348 ELKEELESLEAELEE--LEAELEELESRLEELEEQLETLrskvaqlelqIASLNNEIERLeARLERLE-DRRERLQQEIE 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   403 RKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQR-QLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFE 481
Cdd:TIGR02168  425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELReELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   482 LEAL-NDKKHQ---------------------------LEGKLQDIRCR-LTTQRQEIESTNKSRELRIA---------- 522
Cdd:TIGR02168  505 SEGVkALLKNQsglsgilgvlselisvdegyeaaieaaLGGRLQAVVVEnLNAAKKAIAFLKQNELGRVTflpldsikgt 584
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   523 --EITHLQQQLQESQQMLGRLIPEKQ------ILNDQLKQV-----------QQNSLHRD-SLVTLK-----------RA 571
Cdd:TIGR02168  585 eiQGNDREILKNIEGFLGVAKDLVKFdpklrkALSYLLGGVlvvddldnaleLAKKLRPGyRIVTLDgdlvrpggvitGG 664
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   572 LEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELReihnKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQR 651
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416   652 RAQERDKQWlehVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRL 708
Cdd:TIGR02168  741 EVEQLEERI---AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
384-686 7.40e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.22  E-value: 7.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  384 AQLERAEQERKE-RERQEQERKRQLELEKQLEKqrelerqreeerrkeierrEAAKRELERQrQLEWERNRRQELLNQRN 462
Cdd:COG1340     8 SSLEELEEKIEElREEIEELKEKRDELNEELKE-------------------LAEKRDELNA-QVKELREEAQELREKRD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  463 KEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCR---LTTQRQEIE-----------STNKSREL--RIAEIth 526
Cdd:COG1340    68 ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAggsIDKLRKEIErlewrqqtevlSPEEEKELveKIKEL-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  527 lqqqlqesqqmlgrlipeKQILNDQLKQVQQnslHRDSLVTLKRALEAKELARQH------LRDQLDEVEKETRSKLQEI 600
Cdd:COG1340   146 ------------------EKELEKAKKALEK---NEKLKELRAELKELRKEAEEIhkkikeLAEEAQELHEEMIELYKEA 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  601 DIFNnqlKELREIHnKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAqrraqeRDKQWLEHVQQEDEHQRPRKLHEEE 680
Cdd:COG1340   205 DELR---KEADELH-KEIVEAQEKADELHEEIIELQKELRELRKELKKL------RKKQRALKREKEKEELEEKAEEIFE 274

                  ....*.
gi 768021416  681 KLKREE 686
Cdd:COG1340   275 KLKKGE 280
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
453-680 7.46e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  453 RRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQ 532
Cdd:COG4372    11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  533 ESQQMLGRLIPEKQILNDQLKQVQQnslhrdSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELRE 612
Cdd:COG4372    91 AAQAELAQAQEELESLQEEAEELQE------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  613 IHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEE 680
Cdd:COG4372   165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
747-795 8.01e-07

Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212746 [Multi-domain]  Cd Length: 52  Bit Score: 46.74  E-value: 8.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11812     4 ALYDYTANRSDELTIHRGDIIRV-LYKDNDNWWFGSLVNGQQGYFPANY 51
CEP63 pfam17045
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ...
336-576 9.90e-07

Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.


Pssm-ID: 465338 [Multi-domain]  Cd Length: 264  Bit Score: 51.36  E-value: 9.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   336 EDEQQQLEKKLPVTFEDKKREnFERGNLELEKR----------RQALLEQQRKEQERL-AQLERAEQERKE--RERQEQE 402
Cdd:pfam17045    5 EAELQELMKQIDIMVAHKKSE-WEGQTRALETRldireeellsARNTLERKHKEIGLLrQQLEELEKGKQElvAKYEQQL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   403 RKRQLEL-------EKQLEKQRELERQREEERRKEIERREAAKRELE--RQRQLEWERnrrqellnQRNKEQEDIVVLKA 473
Cdd:pfam17045   84 QKLQEELsklkrsyEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEefRQKSLEWEQ--------QRLQYQQQVASLEA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   474 KKKTLEFELE---------ALNDKKHQLEGKLQDIRcRLTTQRQEIESTNKSRELriaEITHLQQQLQESQQMLGRLIPE 544
Cdd:pfam17045  156 QRKALAEQSSliqsaayqvQLEGRKQCLEASQSEIQ-RLRSKLERAQDSLCAQEL---ELERLRMRVSELGDSNRKLLEE 231
                          250       260       270
                   ....*....|....*....|....*....|...
gi 768021416   545 KQILNDQLKQVQ-QNSLHRDSLVTLKRALEAKE 576
Cdd:pfam17045  232 QQRLLEELRMSQrQLQVLQNELMELKATLQSQD 264
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
338-662 1.00e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 52.82  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   338 EQQQLEKKLPVTFEDKKRENFE--RGNLELEKRRQALLEQQRKE-------QERLAQLERAEQERKERERQEQERKRQL- 407
Cdd:pfam05557    3 ELIESKARLSQLQNEKKQMELEhkRARIELEKKASALKRQLDREsdrnqelQKRIRLLEKREAEAEEALREQAELNRLKk 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   408 ----ELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQedivvlKAKKKTLEFELE 483
Cdd:pfam05557   83 kyleALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLL------KAKASEAEQLRQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   484 ALNDKKHQL---EGKLQDIRCRLTTQRQ--EIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQL----KQ 554
Cdd:pfam05557  157 NLEKQQSSLaeaEQRIKELEFEIQSQEQdsEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVedlkRK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   555 VQQNSLHRDSLVTLKRALEA--------KELARQH---------LRDQLDEVEKETRSKLQEIDIFNNQLKELReihnKQ 617
Cdd:pfam05557  237 LEREEKYREEAATLELEKEKleqelqswVKLAQDTglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQLE----KA 312
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   618 QLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRR----AQERD--KQWLE 662
Cdd:pfam05557  313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvlllTKERDgyRAILE 363
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
747-795 1.04e-06

N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212881 [Multi-domain]  Cd Length: 54  Bit Score: 46.73  E-value: 1.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQTgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11948     4 ALYSFQATESDELPFQKGDILKILNMED-DQNWYKAELQGREGYIPKNY 51
SH3_Sorbs_3 cd11780
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) ...
745-798 1.06e-06

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the third SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212714 [Multi-domain]  Cd Length: 55  Bit Score: 46.53  E-value: 1.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGG--ELKGKTGWFPANYAEK 798
Cdd:cd11780     2 YRALYSYTPQNEDELELREGDIVYV--MEKCDDGWFVGtsERTGLFGTFPGNYVAR 55
SH3_CD2AP_1 cd12053
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ...
749-799 1.09e-06

First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CD2AP. SH3A binds to the PXXXPR motif present in c-Cbl and the cytoplasmic domain of cell adhesion protein CD2. Its interaction with CD2 anchors CD2 at sites of cell contact. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212986  Cd Length: 56  Bit Score: 46.37  E-value: 1.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  749 YPFESRSHDEITIQPGDIVMvDESQTGEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd12053     6 YDYDAVHEDELTIRVGEIIR-NVKKLEEEGWLEGELNGRRGMFPDNFVKEI 55
PTZ00121 PTZ00121
MAEBL; Provisional
307-668 1.14e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  307 SFRRVRSGSGISVISSTSVDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQAllEQQRKEQerlaQL 386
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA--EEKKKAE----EL 1652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  387 ERAEQERKERerQEQERKRQlELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLnQRNKEQE 466
Cdd:PTZ00121 1653 KKAEEENKIK--AAEEAKKA-EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL-KKAEEEN 1728
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  467 DIVVLKAKKKTLEFELEALNDKKHqlEGKLQDIRCRLTTQRQEIESTNKSRELRIAEithlqqqLQESQQMLGRLIPEKQ 546
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-------ELDEEDEKRRMEVDKK 1799
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  547 I--LNDQLKQVQQNSLHRDSLVTLKRAL---EAKELA--RQHLRDQLDEVEKETRSK--------------LQEIDIFNN 605
Cdd:PTZ00121 1800 IkdIFDNFANIIEGGKEGNLVINDSKEMedsAIKEVAdsKNMQLEEADAFEKHKFNKnnengedgnkeadfNKEKDLKED 1879
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  606 QLKELREIHNKQQLQKQkSMEAERLKQ--KEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQED 668
Cdd:PTZ00121 1880 DEEEIEEADEIEKIDKD-DIEREIPNNnmAGKNNDIIDDKLDKDEYIKRDAEETREEIIKISKKD 1943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
335-652 1.48e-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: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKlpvtfEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 414
Cdd:COG1196   426 LEEALAELEEE-----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  415 KQRELERQREEERRKEIERRE----------------------AAKRELERQRQLEWERNRRQELLNQRNK--------- 463
Cdd:COG1196   501 ADYEGFLEGVKAALLLAGLRGlagavavligveaayeaaleaaLAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpld 580
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  464 --EQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIR--CRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLG 539
Cdd:COG1196   581 kiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGdtLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  540 RLIPEKQILNDQLKQVQQN--SLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQ 617
Cdd:COG1196   661 SLTGGSRRELLAALLEAEAelEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 768021416  618 QLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRR 652
Cdd:COG1196   741 LLEEEELLEEEALEELPEPPDLEELERELERLERE 775
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
325-415 1.63e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 52.43  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  325 VDQRLPEEPVLEDEQQQlEKKLPVTFEDKKR-ENFERGNLE-LEKRRQALLEQQRKEQERLAQlERAEQERKERERQEQ- 401
Cdd:PTZ00266  430 VDKDHAERARIEKENAH-RKALEMKILEKKRiERLEREERErLERERMERIERERLERERLER-ERLERDRLERDRLDRl 507
                          90
                  ....*....|....*
gi 768021416  402 ERKRQLELEK-QLEK 415
Cdd:PTZ00266  508 ERERVDRLERdRLEK 522
SH3_SH3RF_1 cd11786
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ...
744-797 1.79e-06

First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212720 [Multi-domain]  Cd Length: 53  Bit Score: 45.82  E-value: 1.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVM----VDESqtgepgWLGGELKGKTGWFPANYAE 797
Cdd:cd11786     1 CAKALYNYEGKEPGDLSFKKGDIILlrkrIDEN------WYHGECNGKQGFFPASYVQ 52
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
327-708 1.81e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  327 QRLPEEPVLEDEQQQLEKKLPVTFedKKRENFERgnlELEKRRQALLEQQRKEQERLAQ--LERAEQERKERERQEQERK 404
Cdd:PRK02224  248 ERREELETLEAEIEDLRETIAETE--REREELAE---EVRDLRERLEELEEERDDLLAEagLDDADAEAVEARREELEDR 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  405 RQlELEKQLEKQRELERQREEErrkeierreaAKRELERQRQLEwERNrrQELLNQRNKEQEDIVVLKAKKKTLEFELEA 484
Cdd:PRK02224  323 DE-ELRDRLEECRVAAQAHNEE----------AESLREDADDLE-ERA--EELREEAAELESELEEAREAVEDRREEIEE 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  485 LNDKKHQLEGKLQDIrcrlTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLK-----QVQQNS 559
Cdd:PRK02224  389 LEEEIEELRERFGDA----PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGS 464
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  560 LHRDSLVTLKRALEAKELARQHLRDQLDEVEKETrsklqeidifnNQLKELREIHNK-QQLQKQKSMEAERLKQK----- 633
Cdd:PRK02224  465 PHVETIEEDRERVEELEAELEDLEEEVEEVEERL-----------ERAEDLVEAEDRiERLEERREDLEELIAERretie 533
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  634 EQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEK--LKRE-ESVKKKDGEEKGKQEAQDKLGRL 708
Cdd:PRK02224  534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLaeLKERiESLERIRTLLAAIADAEDEIERL 611
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
335-612 1.91e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.99  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLP------VTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERA------EQERKErerqEQE 402
Cdd:TIGR02169  249 LEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSiaekerELEDAE----ERL 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   403 RKRQLELEKQLEKqrelerqreeerrkeierREAAKRELERQR----QLEWE----RNRRQELLNQRNKEQEDIVVLKAK 474
Cdd:TIGR02169  325 AKLEAEIDKLLAE------------------IEELEREIEEERkrrdKLTEEyaelKEELEDLRAELEEVDKEFAETRDE 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   475 KKTLEFELEALNDKKHQLEG---KLQDIRCRLTTQRQEIESTNKSRELRIAEithlqqqlqesqqmlgrLIPEKQILNDQ 551
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKReldRLQEELQRLSEELADLNAAIAGIEAKINE-----------------LEEEKEDKALE 449
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021416   552 LKQVQQNslhrdsLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELRE 612
Cdd:TIGR02169  450 IKKQEWK------LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
SH3_Intersectin1_3 cd11991
Third Src homology 3 domain (or SH3C) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
745-795 1.98e-06

Third Src homology 3 domain (or SH3C) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The third SH3 domain (or SH3C) of ITSN1 has been shown to bind many proteins including dynamin1/2, CIN85, c-Cbl, SHIP2, Reps1, synaptojanin-1, and WNK, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212924  Cd Length: 52  Bit Score: 45.74  E-value: 1.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESqtgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11991     2 YVAMYTYESNEQGDLTFQQGDVILVTKK---DGDWWTGTVGDKTGVFPSNY 49
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
327-519 2.09e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.66  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   327 QRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFergnleLEKRRQALLEQQ-------RKEQE--RLAQLERAEQERK--- 394
Cdd:pfam17380  375 SRMRELERLQMERQQKNERVRQELEAARKVKI------LEEERQRKIQQQkvemeqiRAEQEeaRQREVRRLEEERArem 448
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   395 ERERQE-QERKRQLELEKQLEKQRELERQREEERRKEIERREAAKR-----ELERQRQLEWERNRRQELLNQRNKEQEDI 468
Cdd:pfam17380  449 ERVRLEeQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEERKRKLLEKEMEERQKA 528
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   469 VVLKAKKKtlEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSREL 519
Cdd:pfam17380  529 IYEEERRR--EAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
325-524 2.27e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   325 VDQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFERGnlELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERK 404
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   405 RQLELEKQLEKQRELERQREEERRKEIERREAAKRElERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEA 484
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 768021416   485 LNDKKHQLEGKLQDIRCRLTTQRQEIESTnksrELRIAEI 524
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGL----EVRIDNL 941
SH3_SNX33 cd11896
Src Homology 3 domain of Sorting Nexin 33; SNX33 interacts with Wiskott-Aldrich syndrome ...
746-797 2.33e-06

Src Homology 3 domain of Sorting Nexin 33; SNX33 interacts with Wiskott-Aldrich syndrome protein (WASP) and plays a role in the maintenance of cell shape and cell cycle progression. It modulates the shedding and endocytosis of cellular prion protein (PrP(c)) and amyloid precursor protein (APP). SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX33 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212829 [Multi-domain]  Cd Length: 55  Bit Score: 45.72  E-value: 2.33e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPG-DIVMVDESQTGepGWLGGE-LKGKTGWFPANYAE 797
Cdd:cd11896     3 RALYSFQSENKEEINIQENeELVIFSENSLD--GWLQGQnSRGETGLFPASYVE 54
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
587-688 2.39e-06

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 48.51  E-value: 2.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   587 DEVEKETRSKLQEI-DIFNNQLKELREIHNKQQLQKQKSM-EAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHV 664
Cdd:pfam15346   33 DEIEAEVERRVEEArKIMEKQVLEELEREREAELEEERRKeEEERKKREELERILEENNRKIEEAQRKEAEERLAMLEEQ 112
                           90       100
                   ....*....|....*....|....
gi 768021416   665 QQEDEHQRPRKLHEEEKLKREESV 688
Cdd:pfam15346  113 RRMKEERQRREKEEEEREKREQQK 136
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
562-686 2.44e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.92  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  562 RDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREihNKQQLQKQKSMEAERLKQKEQERKIIE 641
Cdd:COG1579    37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--NKEYEALQKEIESLKRRISDLEDEILE 114
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 768021416  642 LEKQKEEAQRRAQERDKQwLEHVQQEDEHQRPRKLHEEEKLKREE 686
Cdd:COG1579   115 LMERIEELEEELAELEAE-LAELEAELEEKKAELDEELAELEAEL 158
SH3_Abp1_eu cd11960
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ...
746-797 2.48e-06

Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212893 [Multi-domain]  Cd Length: 54  Bit Score: 45.47  E-value: 2.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVmVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11960     3 RALYDYQAADDTEISFDPGDII-TDIEQIDEGWWRGTGPDGTYGLFPANYVE 53
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
337-654 2.56e-06

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 50.81  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   337 DEQQQLEKKLPVTFEDKKRENF----ERGNLELEKRRQAL-LEQQRKEQERLAQLERAEQERKER-ERQEQERKRQLELE 410
Cdd:pfam15558   35 EELRRRDQKRQETLERERRLLLqqsqEQWQAEKEQRKARLgREERRRADRREKQVIEKESRWREQaEDQENQRQEKLERA 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   411 KQLEKQRelerqreeerrkeierreaaKRELERQ-RQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEF--ELEALND 487
Cdd:pfam15558  115 RQEAEQR--------------------KQCQEQRlKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEqkKVQENNL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   488 K---KHQLegKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDS 564
Cdd:pfam15558  175 SellNHQA--RKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEH 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   565 lvtlKRAL-EAKELARQHLRDQLDEVEKETRSKLQEIdifnNQLKELREIHNKQQLQKQKSMEAERLKQ--KEQERKIIE 641
Cdd:pfam15558  253 ----KEALaELADRKIQQARQVAHKTVQDKAQRAREL----NLEREKNHHILKLKVEKEEKCHREGIKEaiKKKEQRSEQ 324
                          330
                   ....*....|...
gi 768021416   642 LEKQKEEAQRRAQ 654
Cdd:pfam15558  325 ISREKEATLEEAR 337
SH3_DNMBP_C2 cd12141
Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and ...
743-798 2.60e-06

Second C-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba, and similar domains; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. The C-terminal SH3 domains of DNMBP bind to N-WASP and Ena/VASP proteins, which are key regulatory proteins of the actin cytoskeleton. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213017 [Multi-domain]  Cd Length: 57  Bit Score: 45.57  E-value: 2.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  743 VYYrALYPFESRSHDEITIQPGDIVMVDE--SQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd12141     1 VYY-AVYTFKARSPNELSVSANQRVRILEfsDLTGNKEWWLAEANGQKGYVPSNYIRK 57
SH3_Stac2_C cd11985
C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); ...
745-798 2.67e-06

C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 2 (Stac2); Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac2 contains a single SH3 domain at the C-terminus unlike Stac1 and Stac3, which contain two C-terminal SH3 domains. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212918  Cd Length: 53  Bit Score: 45.32  E-value: 2.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMV-DESQTgepGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11985     2 YVALYKFLPQENNDLPLQPGDRVMVvDDSNE---DWWKGKSGDRVGFFPANFVQR 53
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
451-638 2.94e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 49.54  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  451 RNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEithlqqq 530
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ------- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  531 lqesqqmlgrlipeKQIlnDQLKQvqQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKEL 610
Cdd:COG1579    96 --------------KEI--ESLKR--RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
                         170       180
                  ....*....|....*....|....*...
gi 768021416  611 REIHNKQQLQKQKSMEAERLKQKEQERK 638
Cdd:COG1579   158 LEELEAEREELAAKIPPELLALYERIRK 185
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
366-669 3.03e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  366 EKRRQALLEQQRKEQER---LAQLERAEQERKERERQ-EQERKRQLELEKQL-EKQRELERQREEERRKEIERREAAKRE 440
Cdd:COG4372    31 EQLRKALFELDKLQEELeqlREELEQAREELEQLEEElEQARSELEQLEEELeELNEQLQAAQAELAQAQEELESLQEEA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  441 LERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQdircRLTTQRQEIESTNKSREL- 519
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA----ALEQELQALSEAEAEQALd 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  520 RIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQE 599
Cdd:COG4372   187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  600 IDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDE 669
Cdd:COG4372   267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
SH3_p47phox_1 cd12021
First or N-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called ...
745-797 3.19e-06

First or N-terminal Src homology 3 domain of the p47phox subunit of NADPH oxidase, also called Neutrophil Cytosolic Factor 1; p47phox, or NCF1, is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal Phox homology (PX) domain, tandem SH3 domains (N-SH3 and C-SH3), a polybasic/autoinhibitory region, and a C-terminal proline-rich region (PRR). This model characterizes the first SH3 domain (or N-SH3) of p47phox. In its inactive state, the tandem SH3 domains interact intramolecularly with the autoinhibitory region; upon activation, the tandem SH3 domains are exposed through a conformational change, resulting in their binding to the PRR of p22phox and the activation of NADPH oxidase. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212954 [Multi-domain]  Cd Length: 53  Bit Score: 45.33  E-value: 3.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd12021     2 YRAIADYEKSSKSEMALKTGDVVEVVEKS--ENGWWFCQLKAKRGWVPASYLE 52
SH3_SH3RF_C cd11785
C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), ...
745-798 3.66e-06

C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the fourth SH3 domain, located at the C-terminus of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212719  Cd Length: 55  Bit Score: 45.15  E-value: 3.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELK--GKTGWFPANYAEK 798
Cdd:cd11785     2 YRVIVPYPPQSEAELELKEGDIVFVHKKR--EDGWFKGTLQrtGKTGLFPGSFVES 55
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
335-714 4.39e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.88  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEK-KLPVTFEDKKRENFERGNLEL-EKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERK-------- 404
Cdd:pfam05483   83 LYKEAEKIKKwKVSIEAELKQKENKLQENRKIiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnllke 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   405 ---RQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQ---------LEWERNRRQELLNQRNKE---QEDIV 469
Cdd:pfam05483  163 tcaRSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAEnarlemhfkLKEDHEKIQHLEEEYKKEindKEKQV 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   470 VL--------KAKKKTLEFELEALNDKKHQLE--GKLQDIRCRLTTQRQ-----EIESTNKSRELRIAEITHLQQQLQES 534
Cdd:pfam05483  243 SLlliqitekENKMKDLTFLLEESRDKANQLEekTKLQDENLKELIEKKdhltkELEDIKMSLQRSMSTQKALEEDLQIA 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   535 QQMLGRLIPEKQILNDQLKQVQQN-----SLHRDSLVTLKRALEAKELARQHLRDQLD----EVEKETrSKLQEIDIFNN 605
Cdd:pfam05483  323 TKTICQLTEEKEAQMEELNKAKAAhsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKS-SELEEMTKFKN 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   606 ----QLKELREIHNKQQ--LQKQKSME--AERLKQKEQERKIIELEKQKE----EAQRRAQERDKQwleHVQQEDEHQRP 673
Cdd:pfam05483  402 nkevELEELKKILAEDEklLDEKKQFEkiAEELKGKEQELIFLLQAREKEihdlEIQLTAIKTSEE---HYLKEVEDLKT 478
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 768021416   674 RKlhEEEKLKREE----SVKKKDGEEKGKQEAQDKLGRLfHQHQE 714
Cdd:pfam05483  479 EL--EKEKLKNIEltahCDKLLLENKELTQEASDMTLEL-KKHQE 520
SH3_Ysc84p_like cd11842
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the ...
744-797 4.97e-06

Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the Saccharomyces cerevisiae proteins, Ysc84p (also called LAS17-binding protein 4, Lsb4p) and Lsb3p, and similar fungal proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. Ysc84p localizes to actin patches and plays an important in actin polymerization during endocytosis. The N-terminal domain of both Ysc84p and Lsb3p can bind and bundle actin filaments. A study of the yeast SH3 domain interactome predicts that the SH3 domains of Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212776 [Multi-domain]  Cd Length: 55  Bit Score: 44.72  E-value: 4.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11842     1 KAVALYDFAGEQPGDLAFQKGDIITILKKSDSQNDWWTGRIGGREGIFPANYVE 54
SH3_PLCgamma1 cd11970
Src homology 3 domain of Phospholipase C (PLC) gamma 1; PLCgamma1 is widely expressed and is ...
746-799 5.11e-06

Src homology 3 domain of Phospholipase C (PLC) gamma 1; PLCgamma1 is widely expressed and is essential in growth and development. It is activated by the TrkA receptor tyrosine kinase and functions as a key regulator of cell differentiation. It is also the predominant PLCgamma in T cells and is required for T cell and NK cell function. PLCs catalyze the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG). Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. The SH3 domain of PLCgamma1 directly interacts with dynamin-1 and can serve as a guanine nucleotide exchange factor (GEF). It also interacts with Cbl, inhibiting its phosphorylation and activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212903  Cd Length: 60  Bit Score: 44.98  E-value: 5.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTG-WFPANYAEKI 799
Cdd:cd11970     7 KALFDYKAQREDELTFTKNAIIQNVEKQEG--GWWRGDYGGKKQlWFPSNYVEEI 59
SH3_Vinexin_1 cd11921
First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3) ...
746-799 6.19e-06

First Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212854  Cd Length: 55  Bit Score: 44.53  E-value: 6.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd11921     4 RLKFDFQAQSPKELTLQKGDIVYIHKEV--DKNWLEGEHHGRVGIFPANYVEVL 55
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
385-688 6.34e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.40  E-value: 6.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   385 QLERAEQERKERERQEQERKRQL-----ELEKqLEKQRELERQREEERRKEIERREAAKRELERQRQ--------LEWER 451
Cdd:TIGR04523  118 QKNKLEVELNKLEKQKKENKKNIdkfltEIKK-KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniqknidkIKNKL 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   452 NRRQELL------NQRNKE-QEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQdircrlTTQRQEIESTNKSrelriaei 524
Cdd:TIGR04523  197 LKLELLLsnlkkkIQKNKSlESQISELKKQNNQLKDNIEKKQQEINEKTTEIS------NTQTQLNQLKDEQ-------- 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   525 THLQQQLQESQQMLGRliPEKQI--LNDQLKQVQ------QNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSK 596
Cdd:TIGR04523  263 NKIKKQLSEKQKELEQ--NNKKIkeLEKQLNQLKseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   597 LQEIDIFNNQL-----------KELREIHNK-QQLQKQKSMEAERLKQKEQERKIIE--LEKQKEEAQRRAQERDKQWLE 662
Cdd:TIGR04523  341 NEQISQLKKELtnsesensekqRELEEKQNEiEKLKKENQSYKQEIKNLESQINDLEskIQNQEKLNQQKDEQIKKLQQE 420
                          330       340       350
                   ....*....|....*....|....*....|.
gi 768021416   663 HVQQEDEHQRPRKLHEEEK-----LKREESV 688
Cdd:TIGR04523  421 KELLEKEIERLKETIIKNNseikdLTNQDSV 451
SH3_CD2AP_2 cd12054
Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ...
746-799 6.69e-06

Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212987 [Multi-domain]  Cd Length: 55  Bit Score: 44.19  E-value: 6.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd12054     4 KVLFEYVPQNEDELELKVGDIIDINEEV--EEGWWSGTLNGKSGLFPSNFVKEL 55
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
744-799 6.76e-06

Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 44.12  E-value: 6.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416   744 YYRALYPFESRSHDEITIQPGDIVMVDEsqTGEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:pfam07653    1 YGRVIFDYVGTDKNGLTLKKGDVVKVLG--KDNDGWWEGETGGRVGLVPSTAVEEI 54
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
369-655 7.19e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 7.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  369 RQAL-LEQQRKEQERLAQLERAEQERKER-----ERQEQERKRQLELEKQLEKqrelerqreeeRrkeierreaakreLE 442
Cdd:PRK03918  152 RQILgLDDYENAYKNLGEVIKEIKRRIERlekfiKRTENIEELIKEKEKELEE-----------V-------------LR 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  443 RQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTnKSRELRIA 522
Cdd:PRK03918  208 EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL-EEKVKELK 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  523 EITHLQQqlqesqqmlgrlipEKQILNDQLKQvqqnslHRDSLVTLKRALEAKELARQHLRDQLDEVE------KETRSK 596
Cdd:PRK03918  287 ELKEKAE--------------EYIKLSEFYEE------YLDELREIEKRLSRLEEEINGIEERIKELEekeerlEELKKK 346
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416  597 LQEIDifnNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQE 655
Cdd:PRK03918  347 LKELE---KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
PRK12704 PRK12704
phosphodiesterase; Provisional
572-687 8.19e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 8.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  572 LEAKELArQHLRDqldEVEKETRSKLQEIDIFNNQLKElRE--IHNKQQLQKQKSMEAERlKQKEQERKIIELEKQKEEA 649
Cdd:PRK12704   60 LEAKEEI-HKLRN---EFEKELRERRNELQKLEKRLLQ-KEenLDRKLELLEKREEELEK-KEKELEQKQQELEKKEEEL 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  650 QRRAQERDK---------------QWLEHVQQEDEHQRPRKLHEEEKLKREES 687
Cdd:PRK12704  134 EELIEEQLQelerisgltaeeakeILLEKVEEEARHEAAVLIKEIEEEAKEEA 186
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
323-636 8.48e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 49.97  E-value: 8.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   323 TSVDQRLPEE-PVLEDEQQQLEKKLPVTFEDKK------RENFERGNLELEKRRQALLEQQRKEQErlaQLERAEQERKE 395
Cdd:TIGR00618  576 TQCDNRSKEDiPNLQNITVRLQDLTEKLSEAEDmlaceqHALLRKLQPEQDLQDVRLHLQQCSQEL---ALKLTALHALQ 652
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   396 RERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWeRNRRQELLNQRNKEQEDIVVLKAKK 475
Cdd:TIGR00618  653 LTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL-RELETHIEEYDREFNEIENASSSLG 731
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   476 KTLEFELEALNdkkhQLEGKLQDIRcRLTTQRQEIESTNKSRELRIAEIT-HLQQQLQESQQMLGRLIPEKQILNDQLK- 553
Cdd:TIGR00618  732 SDLAAREDALN----QSLKELMHQA-RTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEa 806
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   554 QVQQNSLHRDSLVTLKRALEAKELArqhlrdQLDEVEKETRSKLQEIDifnNQLKELREihNKQQLQkQKSMEAERLKQK 633
Cdd:TIGR00618  807 EIGQEIPSDEDILNLQCETLVQEEE------QFLSRLEEKSATLGEIT---HQLLKYEE--CSKQLA-QLTQEQAKIIQL 874

                   ...
gi 768021416   634 EQE 636
Cdd:TIGR00618  875 SDK 877
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
331-687 8.59e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 49.97  E-value: 8.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   331 EEPVLEDEQQQLEKKLPVTFE----DKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQ 406
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEEsielKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   407 LELEKQLEKQRELERQREEERRKEIERREAAKRELERQ--------------RQLEWERNRRQELLNQRNKEQEDIVVLK 472
Cdd:pfam02463  497 ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLgvavenykvaistaVIVEVSATADEVEERQKLVRALTELPLG 576
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   473 AKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQL 552
Cdd:pfam02463  577 ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE 656
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   553 KQVQQNSLHRDSLVTLKRALEAKELarqhLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLK- 631
Cdd:pfam02463  657 GLAEKSEVKASLSELTKELLEIQEL----QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQd 732
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021416   632 -----QKEQERKIIElEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREES 687
Cdd:pfam02463  733 kineeLKLLKQKIDE-EEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
SH3_Stac3_1 cd11986
First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 3 ...
744-795 8.72e-06

First C-terminal Src homology 3 domain of SH3 and cysteine-rich domain-containing protein 3 (Stac3); Stac proteins are putative adaptor proteins that contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. There are three mammalian members (Stac1, Stac2, and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212919 [Multi-domain]  Cd Length: 53  Bit Score: 43.74  E-value: 8.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  744 YYRALYPFESRSHDEITIQPGD-IVMVDESQTgepGWLGGELKGKTGWFPANY 795
Cdd:cd11986     1 YFVALYRFKALEKDDLDFHPGErITVIDDSNE---EWWRGKIGEKTGYFPMNF 50
SH3_SH3YL1_like cd11841
Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes ...
747-795 1.00e-05

Src homology 3 domain of SH3 domain containing Ysc84-like 1 (SH3YL1) protein; SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. It binds phosphoinositides (PIs) with high affinity through its N-terminal SYLF domain (also called DUF500). In addition, SH3YL1 contains a C-terminal SH3 domain which has been reported to bind to N-WASP, dynamin 2, and SHIP2 (a PI 5-phosphatase). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212775  Cd Length: 54  Bit Score: 43.92  E-value: 1.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11841     4 ALYSFEGQQPCDLSFQAGDRITVLTRTDSQFDWWEGRLRGRVGIFPANY 52
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
367-656 1.04e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  367 KRRQALLEQQRKE-QERLAQLERAEQERKERERQEQERKRQLE-LEKQLEKQrelerqreeerrkeiERREAAKRELERQ 444
Cdd:COG4913   609 RAKLAALEAELAElEEELAEAEERLEALEAELDALQERREALQrLAEYSWDE---------------IDVASAEREIAEL 673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  445 RQlewernRRQELLnqrnKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIEstnksRELRIAEI 524
Cdd:COG4913   674 EA------ELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD-----ELQDRLEA 738
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  525 THLQQQLQESQQMLGRLipeKQILNDQLKQVQQNSLHRDslvtLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFN 604
Cdd:COG4913   739 AEDLARLELRALLEERF---AAALGDAVERELRENLEER----IDALRARLNRAEEELERAMRAFNREWPAETADLDADL 811
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  605 NQLKELREIHNkqQLQKQKSMEAE----RLKQKEQERKIIELEKQKEEAQRRAQER 656
Cdd:COG4913   812 ESLPEYLALLD--RLEEDGLPEYEerfkELLNENSIEFVADLLSKLRRAIREIKER 865
SH3_Shank1 cd11982
Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 1; Shank1, also ...
745-794 1.04e-05

Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 1; Shank1, also called SSTRIP (Somatostatin receptor-interacting protein), is a brain-specific protein that plays a role in the construction of postsynaptic density (PSD) and the maturation of dendritic spines. Mice deficient in Shank1 show altered PSD composition, thinner PSDs, smaller dendritic spines, and weaker basal synaptic transmission, although synaptic plasticity is normal. They show increased anxiety and impaired fear memory, but also show better spatial learning. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212915 [Multi-domain]  Cd Length: 52  Bit Score: 43.85  E-value: 1.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPAN 794
Cdd:cd11982     3 FMAVKPYQSQAEGEISLSKGEKIKV--LSVGEGGFWEGQVKGRVGWFPSD 50
SH3_UBASH3A cd11937
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is ...
746-798 1.05e-05

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein A; UBASH3A is also called Cbl-Interacting Protein 4 (CLIP4), T cell Ubiquitin LigAnd (TULA), or T cell receptor Signaling (STS)-2. It is only found in lymphoid cells and exhibits weak phosphatase activity. UBASH3A facilitates T cell-induced apoptosis through interaction with the apoptosis-inducing factor AIF. It is involved in regulating the level of phosphorylation of the zeta-associated protein (ZAP)-70 tyrosine kinase. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212870 [Multi-domain]  Cd Length: 60  Bit Score: 43.85  E-value: 1.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGE--PGWLGG--ELKGKTGWFPANYAEK 798
Cdd:cd11937     4 RALFQYKPQNIDELMLSPGDYIFVDPTQQSEasEGWVIGisHRTGCRGFLPENYTER 60
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
335-685 1.13e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.40  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEK---KLPVTFEDKKrENFERgnlELEKRRQALLEQQRKEQERLAQLE-RAEQERKERErQEQERKRQLELE 410
Cdd:pfam01576  704 LEDELQATEDaklRLEVNMQALK-AQFER---DLQARDEQGEEKRRQLVKQVRELEaELEDERKQRA-QAVAAKKKLELD 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   411 -KQLEKQRELERQREEERRKEIERREAAKRELerQRQLEWERNRRQELLNQ-RNKE-------------QEDIVVLKAKK 475
Cdd:pfam01576  779 lKELEAQIDAANKGREEAVKQLKKLQAQMKDL--QRELEEARASRDEILAQsKESEkklknleaellqlQEDLAASERAR 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   476 KTLEFELEALNDK-KHQLEGK--LQDIRCRLTTQRQEIESTNKSRELRIaeithlqqqlqesqqmlgrlipekQILNDQL 552
Cdd:pfam01576  857 RQAQQERDELADEiASGASGKsaLQDEKRRLEARIAQLEEELEEEQSNT------------------------ELLNDRL 912
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   553 -KQVQQNSLHRDSLVTLKRALEAKELARQHLRDQldevEKETRSKLQEIDifnNQLK----------ELREIHNKQQLQ- 620
Cdd:pfam01576  913 rKSTLQVEQLTTELAAERSTSQKSESARQQLERQ----NKELKAKLQEME---GTVKskfkssiaalEAKIAQLEEQLEq 985
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416   621 --KQKSMEAERLKQKeqERKIIELEKQKEEAQRRAQE----------RDKQwLEHVQQEDEHQRPRKLHEEEKLKRE 685
Cdd:pfam01576  986 esRERQAANKLVRRT--EKKLKEVLLQVEDERRHADQykdqaekgnsRMKQ-LKRQLEEAEEEASRANAARRKLQRE 1059
SH3_PI3K_p85 cd11776
Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; ...
745-797 1.20e-05

Src Homology 3 domain of the p85 regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212710  Cd Length: 72  Bit Score: 44.04  E-value: 1.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVD-------------ESQTGEPGWLGG--ELKGKTGWFPANYAE 797
Cdd:cd11776     3 YRALYDYEKERDEDIILKTGDVLVVEnpellalgvpdgkETVPKPEGWLEGknERTGERGDFPGTYVE 70
SH3_Abp1_fungi_C2 cd11961
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ...
746-797 1.79e-05

Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212894 [Multi-domain]  Cd Length: 53  Bit Score: 42.90  E-value: 1.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMvdESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11961     3 KALYDYDAAEDNELSFFENDKII--NIEFVDDDWWLGECHGSRGLFPSNYVE 52
SH3_PEX13_eumet cd11864
Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and ...
746-795 1.81e-05

Src Homology 3 domain of eumetazoan Peroxisomal biogenesis factor 13; PEX13 is a peroxin and is required for protein import into the peroxisomal matrix and membrane. It is an integral membrane protein that is essential for the localization of PEX14 and the import of proteins containing the peroxisome matrix targeting signals, PTS1 and PTS2. Mutations of the PEX13 gene in humans lead to a wide range of peroxisome biogenesis disorders (PBDs), the most severe of which is known as Zellweger syndrome (ZS), a severe multisystem disorder characterized by hypotonia, psychomotor retardation, and neuronal migration defects. PEX13 contains two transmembrane regions and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212798  Cd Length: 58  Bit Score: 43.00  E-value: 1.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV--DESQTGEPGWLGGELKG-KTGWFPANY 795
Cdd:cd11864     3 RAEYDFVAESEDELSFRAGDKLRLapKELQPRVRGWLLATVDGqKIGLVPANY 55
SH3_Myosin-I_fungi cd11858
Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent ...
745-797 1.96e-05

Src homology 3 domain of Type I fungal Myosins; Type I myosins (myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Saccharomyces cerevisiae has two myosins-I, Myo3 and Myo5, which are involved in endocytosis and the polarization of the actin cytoskeleton. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212792 [Multi-domain]  Cd Length: 55  Bit Score: 43.14  E-value: 1.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQTGepGW-LGGELKG-KTGWFPANYAE 797
Cdd:cd11858     2 YKALYDFAGSVANELSLKKDDIVYIVQKEDN--GWwLAKKLDEsKEGWVPAAYLE 54
SH3_Sorbs2_1 cd11920
First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called ...
746-799 2.03e-05

First Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212853 [Multi-domain]  Cd Length: 55  Bit Score: 43.08  E-value: 2.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd11920     4 RAVYDFKAQTSKELSFKKGDTVYI--LRKIDQNWYEGEHHGRVGIFPISYVEKL 55
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
746-795 2.04e-05

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212738 [Multi-domain]  Cd Length: 52  Bit Score: 42.73  E-value: 2.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11804     3 VAKHDFKATAEDELSFKKGSILKVLNMED-DPNWYKAELDGKEGLIPKNY 51
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
366-512 2.07e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  366 EKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE---------KQLEKQrelerqreeerrkeierREA 436
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrlEQLERE-----------------IER 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  437 AKRELERQRQlewERNRRQELLNQ----RNKEQEDIVVLKAK----KKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQ 508
Cdd:COG4913   350 LERELEERER---RRARLEALLAAlglpLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDLRRELRELEA 426

                  ....
gi 768021416  509 EIES 512
Cdd:COG4913   427 EIAS 430
SH3_PACSIN3 cd11997
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); ...
743-797 2.11e-05

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212930 [Multi-domain]  Cd Length: 56  Bit Score: 43.02  E-value: 2.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  743 VYYRALYPFESRSHDEITIQPGDIVMvDESQTGEPGWLGGEL-KGKTGWFPANYAE 797
Cdd:cd11997     2 VRVRALYDYTGQEADELSFKAGEELL-KIGEEDEQGWCKGRLlSGRIGLYPANYVE 56
SH3_PI3K_p85alpha cd11910
Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol ...
745-799 2.20e-05

Src Homology 3 domain of the p85alpha regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85alpha interacts with activated FGFR3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212843  Cd Length: 75  Bit Score: 43.35  E-value: 2.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVD-------------ESQTGEPGWLGG--ELKGKTGWFPANYAEKI 799
Cdd:cd11910     4 YRALYDYKKEREEDIDLHLGDILTVNkgsllalgfsegqEARPEEIGWLNGynETTGERGDFPGTYVEYI 73
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
335-683 2.42e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLpvtfedKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERA-EQERKERERQEQERKRQLELEKQL 413
Cdd:PRK03918  174 IKRRIERLEKFI------KRTENIEELIKEKEKELEEVLREINEISSELPELREElEKLEKEVKELEELKEEIEELEKEL 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  414 EKqRELERQREEERRKeierreaakrELERQRQlewERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLE 493
Cdd:PRK03918  248 ES-LEGSKRKLEEKIR----------ELEERIE---ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  494 GKLQdircRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQL-KQVQQNSLHRD----SLVTL 568
Cdd:PRK03918  314 KRLS----RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKaKKEELERLKKRltglTPEKL 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  569 KRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQL--------QKQKSMEAERLKQKEQERKII 640
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelteeHRKELLEEYTAELKRIEKELK 469
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 768021416  641 ELEKQKEEAQRRAQERDKQwlehVQQEDEHQRPRKLHE-----EEKLK 683
Cdd:PRK03918  470 EIEEKERKLRKELRELEKV----LKKESELIKLKELAEqlkelEEKLK 513
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
364-524 2.43e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.84  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  364 ELEKRRQALLEQQRKEQERLAQLERA-EQERKERERQEQERKrqlELEKQLEKqrelerqreeerrkeierreaAKRELE 442
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDElAALEARLEAAKTELE---DLEKEIKR---------------------LELEIE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  443 RQRQLEwERNRRQELLNQRNKE----QEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRE 518
Cdd:COG1579    70 EVEARI-KKYEEQLGNVRNNKEyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148

                  ....*.
gi 768021416  519 LRIAEI 524
Cdd:COG1579   149 EELAEL 154
SH3_CIN85_1 cd12052
First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
749-795 2.57e-05

First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212985 [Multi-domain]  Cd Length: 53  Bit Score: 42.57  E-value: 2.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 768021416  749 YPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTGWFPANY 795
Cdd:cd12052     6 FDYKAQHEDELTITVGDIITKIKKDDG--GWWEGEIKGRRGLFPDNF 50
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
615-719 2.81e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.49  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  615 NKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGE 694
Cdd:PRK09510   65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
                          90       100
                  ....*....|....*....|....*
gi 768021416  695 EKGKQEAQDKlgrlfhQHQEPAKPA 719
Cdd:PRK09510  145 AKAKAEAEAK------RAAAAAKKA 163
SH3_Eve1_3 cd11816
Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
746-795 2.85e-05

Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212750 [Multi-domain]  Cd Length: 51  Bit Score: 42.39  E-value: 2.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpgWLGGELKGKTGWFPANY 795
Cdd:cd11816     3 VARFDFEGEQEDELSFSEGDVITLKEYVGEE--WAKGELNGKIGIFPLNF 50
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
335-466 2.90e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 48.02  E-value: 2.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLPVTfedKKRENFERGNLELEKRRQALLEQQRKEQERLAQLE--------RAEQERKERERQEQERKRQ 406
Cdd:pfam15709  378 LELEQQRRFEEIRLR---KQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrklqelQRKKQQEEAERAEAEKQRQ 454
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021416   407 LELEKQLEKQrelerqreeerrKEIERREAAKRELERQRQ-LEWERNRRQELLNQRNKEQE 466
Cdd:pfam15709  455 KELEMQLAEE------------QKRLMEMAEEERLEYQRQkQEAEEKARLEAEERRQKEEE 503
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
745-798 3.01e-05

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 42.36  E-value: 3.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESqtGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd11824     2 YSVLYDYTAQEDDELSISKGDVVAVIEK--GEDGWWTVERNGQKGLVPGTYLEK 53
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
350-685 3.18e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  350 FEDKKRENFERGNLELEKRRQALleQQRKEQERLAQ---LERAEQERKE----RERQEQERKRQLELEKQLEKQRELERQ 422
Cdd:PRK02224  304 LDDADAEAVEARREELEDRDEEL--RDRLEECRVAAqahNEEAESLREDaddlEERAEELREEAAELESELEEAREAVED 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  423 REEERRKEIERREAAKRELE-RQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLE---FELEALNDkkhqlEGKL-- 496
Cdd:PRK02224  382 RREEIEELEEEIEELRERFGdAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLE-----AGKCpe 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  497 --QDIR----------CR-----LTTQRQEIESTNKSRELRIAEITHLQQQlqesqqmlgrlipEKQIlnDQLKQVQQNS 559
Cdd:PRK02224  457 cgQPVEgsphvetieeDRerveeLEAELEDLEEEVEEVEERLERAEDLVEA-------------EDRI--ERLEERREDL 521
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  560 lhrDSLVTLKRA-LEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREihNKQQLQKQKSMEAERLKQKEQERK 638
Cdd:PRK02224  522 ---EELIAERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE--EVAELNSKLAELKERIESLERIRT 596
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 768021416  639 IIELEKQKEEAQRRAQERDKQWlehvqQEDEHQRPRKLHEEEKLKRE 685
Cdd:PRK02224  597 LLAAIADAEDEIERLREKREAL-----AELNDERRERLAEKRERKRE 638
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
355-461 3.18e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 48.19  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  355 RENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKqLEKQrelerqreeerrkeierr 434
Cdd:PTZ00266  432 KDHAERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLERER-LERE------------------ 492
                          90       100
                  ....*....|....*....|....*..
gi 768021416  435 EAAKRELERQRQLEWERNRRQELLNQR 461
Cdd:PTZ00266  493 RLERDRLERDRLDRLERERVDRLERDR 519
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
746-795 3.24e-05

Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212896 [Multi-domain]  Cd Length: 57  Bit Score: 42.31  E-value: 3.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV-DESQTgepGWLGGELKGKTGWFPANY 795
Cdd:cd11963     5 RALYDFEAVEDNELTFKHGEIIIVlDDSDA---NWWKGENHRGVGLFPSNF 52
SH3_Abi2 cd11972
Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It ...
747-799 3.37e-05

Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It regulates actin cytoskeletal reorganization at adherens junctions and dendritic spines, which is important in cell morphogenesis, migration, and cognitive function. Mice deficient with Abi2 show defects in orientation and migration of lens fibers, neuronal migration, dendritic spine morphology, as well as deficits in learning and memory. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212905 [Multi-domain]  Cd Length: 61  Bit Score: 42.69  E-value: 3.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd11972     7 AIYDYTKDKEDELSFQEGAIIYV--IKKNDDGWYEGVMNGVTGLFPGNYVESI 57
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
326-686 3.43e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  326 DQRLPEEPVLEDEQQQLEkklpvtfeDKKRENFERGNLELEKRRQALlEQQRKEQErlAQLERAEQERkereRQEQERKR 405
Cdd:PRK02224  173 DARLGVERVLSDQRGSLD--------QLKAQIEEKEEKDLHERLNGL-ESELAELD--EEIERYEEQR----EQARETRD 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  406 QLE--LEKQLEKQrelerQREEERRKEIERREAAKRELERQR-----QLEWERNRRQELLNQRNKEQEDIVVLKAKKKTL 478
Cdd:PRK02224  238 EADevLEEHEERR-----EELETLEAEIEDLRETIAETEREReelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAV 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  479 EFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKS---RELRIAEITHLQQQLQESQQMLGRLIPEKQ----ILNDQ 551
Cdd:PRK02224  313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEELREEAAELESELEEAREAVEDRReeieELEEE 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  552 LKQVQQNslHRDSLVTLKRALEAKELARQHlRDQLDEVEKETRSKLQEIDIFNNQLKELREIHN----KQQL-------- 619
Cdd:PRK02224  393 IEELRER--FGDAPVDLGNAEDFLEELREE-RDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVegsphvet 469
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  620 -----QKQKSMEAERLKQKEQ----ERKIIELEKQKEEAQRRaqERDKQWLEHVQQEDEHQRPRKlhEEEKLKREE 686
Cdd:PRK02224  470 ieedrERVEELEAELEDLEEEveevEERLERAEDLVEAEDRI--ERLEERREDLEELIAERRETI--EEKRERAEE 541
SH3_Intersectin_2 cd11837
Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor ...
745-795 3.47e-05

Second Src homology 3 domain (or SH3B) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212771 [Multi-domain]  Cd Length: 53  Bit Score: 42.35  E-value: 3.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11837     2 ATALYPWRAKKENHLSFAKGDIITVLEQQ--EMWWFGELEGGEEGWFPKSY 50
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
744-795 3.48e-05

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212882 [Multi-domain]  Cd Length: 53  Bit Score: 42.13  E-value: 3.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIV-MVDESqtgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11949     1 YVQALFDFDPQEDGELGFRRGDFIeVMDNS---DPNWWKGACHGQTGMFPRNY 50
SH3_Intersectin2_3 cd11992
Third Src homology 3 domain (or SH3C) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
745-795 3.60e-05

Third Src homology 3 domain (or SH3C) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The third SH3 domain (SH3C) of ITSN2 has been shown to bind the K15 protein of Kaposi's sarcoma-associated herpesvirus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212925  Cd Length: 52  Bit Score: 42.31  E-value: 3.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQtGEpgWLGGELKGKTGWFPANY 795
Cdd:cd11992     2 YIALYPYSSSEPGDLTFNEGEEILVTQKD-GE--WWTGSIEDRTGIFPSNY 49
SH3_SGSM3 cd11813
Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called ...
746-797 3.89e-05

Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called Merlin-associated protein (MAP), RUN and SH3 domain-containing protein (RUSC3), RUN and TBC1 domain-containing protein 3 (RUTBC3), Rab GTPase-activating protein 5 (RabGAP5), or Rab GAP-like protein (RabGAPLP). It is expressed ubiquitously and functions as a regulator of small G protein RAP- and RAB-mediated neuronal signaling. It is involved in modulating NGF-mediated neurite outgrowth and differentiation. It also interacts with the tumor suppressor merlin and may play a role in the merlin-associated suppression of cell growth. SGSM3 contains TBC, SH3, and RUN domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212747  Cd Length: 53  Bit Score: 42.10  E-value: 3.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDeSQTGEPGWLGgELKGKTGWFPANYAE 797
Cdd:cd11813     3 KALLDFERHDDDELGFRKNDIITII-SQKDEHCWVG-ELNGLRGWFPAKFVE 52
SH3_BOI cd11886
Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces ...
744-795 4.12e-05

Src Homology 3 domain of fungal BOI-like proteins; This subfamily includes the Saccharomyces cerevisiae proteins BOI1 and BOI2, and similar proteins. They contain an N-terminal SH3 domain, a Sterile alpha motif (SAM), and a Pleckstrin homology (PH) domain at the C-terminus. BOI1 and BOI2 interact with the SH3 domain of Bem1p, a protein involved in bud formation. They promote polarized cell growth and participates in the NoCut signaling pathway, which is involved in the control of cytokinesis. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212819  Cd Length: 55  Bit Score: 41.93  E-value: 4.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMV--DESQTGEpGW-LGGELK-GKTGWFPANY 795
Cdd:cd11886     1 LLIVIHDFNARSEDELTLKPGDKIELieDDEEFGD-GWyLGRNLRtGETGLFPVVF 55
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
745-795 4.32e-05

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 41.80  E-value: 4.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGGELK-GKTGWFPANY 795
Cdd:cd11845     2 YVALYDYEARTDDDLSFKKGDRLQILDDSDGD-WWLARHLStGKEGYIPSNY 52
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
574-686 4.45e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.11  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  574 AKELARQHlRDQLDEVEKETRSKLQEidifNNQLKELREIHNKQQlQKQKSMEAERLKQKEQErkiieleKQKEEAQRRA 653
Cdd:PRK09510   61 VEQYNRQQ-QQQKSAKRAEEQRKKKE----QQQAEELQQKQAAEQ-ERLKQLEKERLAAQEQK-------KQAEEAAKQA 127
                          90       100       110
                  ....*....|....*....|....*....|...
gi 768021416  654 QERDKQWLEHVQQEDEHQrprKLHEEEKLKREE 686
Cdd:PRK09510  128 ALKQKQAEEAAAKAAAAA---KAKAEAEAKRAA 157
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
325-474 4.65e-05

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 44.66  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   325 VDQRLPEEpvLEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALL-EQQRKEQERLAQLERAEQERKERERQEQER 403
Cdd:pfam15346   20 VAKRVEEE--LEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELeEERRKEEEERKKREELERILEENNRKIEEA 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021416   404 KRQLELEKQlekqrelerqreeerrkeierreaakRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAK 474
Cdd:pfam15346   98 QRKEAEERL--------------------------AMLEEQRRMKEERQRREKEEEEREKREQQKILNKKN 142
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
452-667 4.90e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.32  E-value: 4.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   452 NRRQELLNQRNKEQEDIVVLKAKKKTLEFEL-------EALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEI 524
Cdd:TIGR04523   33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLnkdeekiNNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   525 THLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRAlEAKELARQ--HLRDQLDEVEKETRSKLQEIDI 602
Cdd:TIGR04523  113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN-KYNDLKKQkeELENELNLLEKEKLNIQKNIDK 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416   603 FNNQL--KELREIHNKQQLQKQKSMEAERLKQKEQErkiIELEKQKEEAQRRAQERDKQwLEHVQQE 667
Cdd:TIGR04523  192 IKNKLlkLELLLSNLKKKIQKNKSLESQISELKKQN---NQLKDNIEKKQQEINEKTTE-ISNTQTQ 254
SH3_GRAF cd12064
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase; GRAF, also ...
746-797 5.22e-05

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase; GRAF, also called Rho GTPase activating protein 26 (ARHGAP26), Oligophrenin-1-like (OPHN1L) or GRAF1, is a GAP with activity towards RhoA and Cdc42 and is only weakly active towards Rac1. It influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase (FAK), which is a critical component of integrin signaling. It is essential for the major clathrin-independent endocytic pathway mediated by pleiomorphic membranes. GRAF contains an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. The SH3 domain of GRAF binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212997  Cd Length: 56  Bit Score: 42.02  E-value: 5.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGdIVMVDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd12064     4 KALYACKAEHDSELSFTAG-TVFDNVHPSQEPGWLEGTLNGKTGLIPENYVE 54
PRK12704 PRK12704
phosphodiesterase; Provisional
363-512 5.42e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  363 LELEKRRQALLEQQRKEQE---RLAQLERAEQERKERERQEQE-RKRQLELEKQLekqrelerqreeerrkeierreaaK 438
Cdd:PRK12704   34 KEAEEEAKRILEEAKKEAEaikKEALLEAKEEIHKLRNEFEKElRERRNELQKLE------------------------K 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416  439 RELERQRQLEwernRRQELLNQRNKEqedivvLKAKKKTLEFELEALNDKKHQLEGKLQDircrlttQRQEIES 512
Cdd:PRK12704   90 RLLQKEENLD----RKLELLEKREEE------LEKKEKELEQKQQELEKKEEELEELIEE-------QLQELER 146
SH3_FCHSD_1 cd11761
First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
747-798 6.29e-05

First Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212695 [Multi-domain]  Cd Length: 57  Bit Score: 41.58  E-value: 6.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGG-ELKGKTGWFPANYAEK 798
Cdd:cd11761     6 VLYSYEAQRPDELTITEGEELEVIEDGDGD-GWVKArNKSGEVGYVPENYLQF 57
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
331-414 6.55e-05

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.03  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  331 EEPVLEDEQQQLEKKLpvtfEDKKReNFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE 410
Cdd:cd16269   213 ERKLLEEQQRELEQKL----EDQER-SYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEI 287

                  ....
gi 768021416  411 KQLE 414
Cdd:cd16269   288 RSLK 291
SH3_Sla1p_1 cd11773
First Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
745-795 6.65e-05

First Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212707 [Multi-domain]  Cd Length: 57  Bit Score: 41.64  E-value: 6.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESqtGEPGWLGGELK-------GKTGWFPANY 795
Cdd:cd11773     2 YKALYDYEPQTEDELTIQEDDILYLLEK--SDDDWWKVKLKvnssdddEPVGLVPATY 57
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
335-672 6.83e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLpvTFEDKKRENFERGNLELEKRRQALLEQQRKEQ-ERLAQLERaEQERKERERQEQERKRQlELEKQL 413
Cdd:COG4913   293 LEAELEELRAEL--ARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLER-EIERLERELEERERRRA-RLEALL 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  414 EKQRELERQREEERRKEIERREAAKRELERQRqlEWERNRRQELLNQRNKeqedivvLKAKKKTLEFELEALNDKKHQLE 493
Cdd:COG4913   369 AALGLPLPASAEEFAALRAEAAALLEALEEEL--EALEEALAEAEAALRD-------LRRELRELEAEIASLERRKSNIP 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  494 GKLQDIRCRLTTQ-----------------RQE--------------------------------IESTNKSRELRIAEI 524
Cdd:COG4913   440 ARLLALRDALAEAlgldeaelpfvgelievRPEeerwrgaiervlggfaltllvppehyaaalrwVNRLHLRGRLVYERV 519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  525 THLQQQLQESQQMLGRLIPE------------KQILN-----------DQLK----------QVQQN-SLH--------- 561
Cdd:COG4913   520 RTGLPDPERPRLDPDSLAGKldfkphpfrawlEAELGrrfdyvcvdspEELRrhpraitragQVKGNgTRHekddrrrir 599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  562 ---------RDSLVTLKRALEAKELARQHLRDQLDEVEKET------RSKLQEIDIFNNQLKELREIHNK-QQLQKQK-- 623
Cdd:COG4913   600 sryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELdalqerREALQRLAEYSWDEIDVASAEREiAELEAELer 679
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  624 ----SMEAERLKQ--KEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQR 672
Cdd:COG4913   680 ldasSDDLAALEEqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
328-525 7.19e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 7.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   328 RLPEEPVLEDEQQQLEKKLPVTFEDKK--RENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERE---RQEQE 402
Cdd:TIGR02169  824 LTLEKEYLEKEIQELQEQRIDLKEQIKsiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEaqlRELER 903
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   403 RKRQLELEKQLEKQrelerqreeerrkeIERREAAKRELERQRQLEWERNRRQELlnQRNKEQEDIVVLKAKKKTLEFEL 482
Cdd:TIGR02169  904 KIEELEAQIEKKRK--------------RLSELKAKLEALEEELSEIEDPKGEDE--EIPEEELSLEDVQAELQRVEEEI 967
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416   483 EALND------------KKHQLEgkLQDIRCRLTTQRQEIestnksrELRIAEIT 525
Cdd:TIGR02169  968 RALEPvnmlaiqeyeevLKRLDE--LKEKRAKLEEERKAI-------LERIEEYE 1013
SH3_CIP4_Bzz1_like cd11777
Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains; This subfamily ...
746-796 7.25e-05

Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains; This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4) and similar proteins such as Formin Binding Protein 17 (FBP17) and FormiN Binding Protein 1-Like (FNBP1L), as well as yeast Bzz1 (or Bzz1p). CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Bzz1 is also a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Members of this subfamily contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain as well as at least one C-terminal SH3 domain. Bzz1 contains a second SH3 domain at the C-terminus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212711 [Multi-domain]  Cd Length: 55  Bit Score: 41.44  E-value: 7.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGGELK-GKTGWFPANYA 796
Cdd:cd11777     3 KALYAFVGSSEGTISMTEGEKLSLVEEDKGD-GWTRVRRDtGEEGYVPTSYI 53
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
353-659 7.57e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 7.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  353 KKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEkQLEKQrelerqreeerrkeie 432
Cdd:COG4372     5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEE---------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  433 rREAAKRELER-QRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIE 511
Cdd:COG4372    68 -LEQARSELEQlEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  512 STNKSRELRIAEITHLQQQLQESQQMLGRLIPEK--QILNDQLKQVQQNSLHRDSLVTLKRALEAKEL----ARQHLRDQ 585
Cdd:COG4372   147 EREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLPRelaeELLEAKDS 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416  586 LDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQ 659
Cdd:COG4372   227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
SH3_FCHSD_2 cd11762
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
744-793 9.75e-05

Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212696 [Multi-domain]  Cd Length: 57  Bit Score: 41.23  E-value: 9.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMV--DESQTGEPGWLGGELKGKTGWFPA 793
Cdd:cd11762     1 LVRALYDYEAQSDEELSFPEGAIIRIlrKDDNGVDDGWWEGEFNGRVGVFPS 52
SH3_Tks5_2 cd12077
Second Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also ...
745-798 1.04e-04

Second Src homology 3 domain of Tyrosine kinase substrate with five SH3 domains; Tks5, also called SH3 and PX domain-containing protein 2A (SH3PXD2A) or Five SH (FISH), is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. It binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. Tks5 contains an N-terminal Phox homology (PX) domain and five SH3 domains. This model characterizes the second SH3 domain of Tks5. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213010  Cd Length: 54  Bit Score: 40.79  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAEK 798
Cdd:cd12077     3 YVTVQPYTSQGKDEIGFEKGVTVEV--IQKNLEGWWYIRYLGKEGWAPASYLKK 54
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
367-682 1.31e-04

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 45.44  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   367 KRRQALLEQQRKEQERLAQ-LER-------AEQE-RKERER-----------QEQERKRQLELeKQLEKQRELERQREEE 426
Cdd:pfam15742    2 SSGEKLKYQQQEEVQQLRQnLQRlqilctsAEKElRYERGKnldlkqhnsllQEENIKIKAEL-KQAQQKLLDSTKMCSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   427 RRKEIerreaaKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAK-----KKTLEFE-----------LEALNDKKH 490
Cdd:pfam15742   81 LTAEW------KHCQQKIRELELEVLKQAQSIKSQNSLQEKLAQEKSRvadaeEKILELQqklehahkvclTDTCILEKK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   491 QLEGK---LQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQIlndqlkQVQQNSLHRDSLVT 567
Cdd:pfam15742  155 QLEERikeASENEAKLKQQYQEEQQKRKLLDQNVNELQQQVRSLQDKEAQLEMTNSQQQL------RIQQQEAQLKQLEN 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   568 LKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQL-KELREIHNKQQLQKQKSMEAERLKQKEQER---KIIELE 643
Cdd:pfam15742  229 EKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVLKQLdVHVRKYNEKHHHHKAKLRRAKDRLVHEVEQrdeRIKQLE 308
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 768021416   644 KQKEEAQRRAqERDKQWLEHVQQEDEH--QRPRKL----HEEEKL 682
Cdd:pfam15742  309 NEIGILQQQS-EKEKAFQKQVTAQNEIllLEKRKLleqlTEQEEL 352
SH3_SH3RF3_1 cd11928
First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ...
744-797 1.47e-04

First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF3. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212861  Cd Length: 54  Bit Score: 40.68  E-value: 1.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVM----VDESqtgepgWLGGELKGKTGWFPANYAE 797
Cdd:cd11928     2 CGKALYSYEGKEPGDLKFNKGDIIIlrrkVDEN------WYHGELNGCHGFLPASYIQ 53
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
366-501 1.53e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 43.88  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   366 EKRRQALLEQQRKEQERLAQleraEQERKERERQEQERKRQLELEKqlekqrelerqreeerrkeierreaAKRELERQR 445
Cdd:pfam09756    5 AKKRAKLELKEAKRQQREAE----EEEREEREKLEEKREEEYKERE-------------------------EREEEAEKE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416   446 QLEWERNRRQEllnQRNKEQEDIVVLKAkkktlEFELEALNDKKHQLEGKLQDIRC 501
Cdd:pfam09756   56 KEEEERKQEEE---QERKEQEEYEKLKS-----QFVVEEEGTDKLSAEDESQLLED 103
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
335-613 1.57e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLpvtfedkkrenfERGN--LELEKRRQALLEQQRKEQERLAqlERAEQERKERERQEQERKRQLELEKQ 412
Cdd:PRK02224  487 LEEEVEEVEERL------------ERAEdlVEAEDRIERLEERREDLEELIA--ERRETIEEKRERAEELRERAAELEAE 552
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  413 LEKQRELerqreeerrkeierreAAKRELERQRQLEW--ERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKH 490
Cdd:PRK02224  553 AEEKREA----------------AAEAEEEAEEAREEvaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKRE 616
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  491 QLEGKLQDIRCRLTTQRQEIestnksRELriaeithlqqqlqesqqmlgrlipEKQILNDQLKQVQQNslhrdslvtLKR 570
Cdd:PRK02224  617 ALAELNDERRERLAEKRERK------REL------------------------EAEFDEARIEEARED---------KER 657
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 768021416  571 ALEAKElarqHLRDQLDEVEkETRSKLQ-EIDIFNNQLKELREI 613
Cdd:PRK02224  658 AEEYLE----QVEEKLDELR-EERDDLQaEIGAVENELEELEEL 696
SH3_Bzz1_1 cd11912
First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
746-797 1.74e-04

First Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the first C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212845 [Multi-domain]  Cd Length: 55  Bit Score: 40.28  E-value: 1.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpGW----LGGelkGKTGWFPANYAE 797
Cdd:cd11912     3 KVLYDYTASGDDEVSISEGEEVTVLEPDDGS-GWtkvrNGS---GEEGLVPTSYIE 54
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
366-491 1.78e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 43.93  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   366 EKRRQALLEQQRKEQERLAQLERAEQ-ERKERERQEQ--ERKRQLELEKQLEKQRELERQREEERRKEIERREAAkrELE 442
Cdd:pfam13904   63 AKQRQRQKELQAQKEEREKEEQEAELrKRLAKEKYQEwlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQ--EEA 140
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 768021416   443 RQRQLEWERNRRQELLNQRNKEQEDivvlKAKKKTLEFELEALNDKKHQ 491
Cdd:pfam13904  141 KEVLQEWERKKLEQQQRKREEEQRE----QLKKEEEEQERKQLAEKAWQ 185
PRK12704 PRK12704
phosphodiesterase; Provisional
336-416 1.88e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  336 EDEQQQLEKKLPVTFE--DKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKER-ER-----QEQERKRQL 407
Cdd:PRK12704   81 RNELQKLEKRLLQKEEnlDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElERisgltAEEAKEILL 160
                          90
                  ....*....|
gi 768021416  408 E-LEKQLEKQ 416
Cdd:PRK12704  161 EkVEEEARHE 170
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
746-795 1.88e-04

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 40.34  E-value: 1.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMV---DESqtgepGWLGGEL-----KGKTGWFPANY 795
Cdd:cd11883     3 VALYDFTPKSKNQLSFKAGDIIYVlnkDPS-----GWWDGVIisssgKVKRGWFPSNY 55
SH3_UBASH3B cd11936
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B; UBASH3B, ...
746-798 1.91e-04

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing protein B; UBASH3B, also called Suppressor of T cell receptor Signaling (STS)-1 or T cell Ubiquitin LigAnd (TULA)-2 is an active phosphatase that is expressed ubiquitously. The phosphatase activity of UBASH3B is essential for its roles in the suppression of TCR signaling and the regulation of EGFR. It also interacts with Syk and functions as a negative regulator of platelet glycoprotein VI signaling. TULA proteins contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212869  Cd Length: 62  Bit Score: 40.41  E-value: 1.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVM---VDESQTGEpGWLGGE--LKGKTGWFPANYAEK 798
Cdd:cd11936     5 QVIYPYTPQNDDELELVPGDYIFmspMEQTSTSE-GWIYGTslTTGCSGLLPENYITK 61
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
370-686 2.01e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 45.42  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   370 QALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKqLEKQRELERQREEERRKEIERREAAKRELERQRQLEW 449
Cdd:TIGR00606  690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL-APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   450 ERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRiaeithlqq 529
Cdd:TIGR00606  769 EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD--------- 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   530 qlqeSQQMLGRLIpeKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKE 609
Cdd:TIGR00606  840 ----TVVSKIELN--RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   610 LRE------------IHNKQQLQKQKSME----AERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRP 673
Cdd:TIGR00606  914 LETflekdqqekeelISSKETSNKKAQDKvndiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQ 993
                          330
                   ....*....|...
gi 768021416   674 RKLHEEEKLKREE 686
Cdd:TIGR00606  994 EKINEDMRLMRQD 1006
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
327-708 2.08e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   327 QRLPEEPVLEDEQQQLEKKLPVTFEDKkRENFERGNLELEKRRQALLEQQRKEQERLAQLEraeQERKERERQEQERKRQ 406
Cdd:pfam01576   36 QQLCEEKNALQEQLQAETELCAEAEEM-RARLAARKQELEEILHELESRLEEEEERSQQLQ---NEKKKMQQHIQDLEEQ 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   407 LELEK------QLEKQRELERQREEERRKEIERREAAKRELERQ----------RQLEWERNRRQELLNQRNKEQEDIVV 470
Cdd:pfam01576  112 LDEEEaarqklQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKlleeriseftSNLAEEEEKAKSLSKLKNKHEAMISD 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   471 LKAKKKTLEFELEALNDKKHQLEGKLQDIR---CRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQI 547
Cdd:pfam01576  192 LEERLKKEEKGRQELEKAKRKLEGESTDLQeqiAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   548 LNDQLKQ-VQQNSLHRDSLVTLKRAL-EAKELARQHLRDQLDE--VEKETRSKL-QEIDIFNNQLKELREIHNKQ-QLQK 621
Cdd:pfam01576  272 QISELQEdLESERAARNKAEKQRRDLgEELEALKTELEDTLDTtaAQQELRSKReQEVTELKKALEEETRSHEAQlQEMR 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   622 QKSMEA-----ERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRpRKLH---EEEKLKREESvkkkdg 693
Cdd:pfam01576  352 QKHTQAleeltEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR-KKLEgqlQELQARLSES------ 424
                          410
                   ....*....|....*
gi 768021416   694 eEKGKQEAQDKLGRL 708
Cdd:pfam01576  425 -ERQRAELAEKLSKL 438
SH3_DNMBP_N4 cd11797
Fourth N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
744-792 2.17e-04

Fourth N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP bind the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212731  Cd Length: 50  Bit Score: 39.71  E-value: 2.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFP 792
Cdd:cd11797     1 YGVALYRFQALEPNELDFEVGDRIRI--IATLEDGWLEGELKGRRGIFP 47
SH3_Intersectin1_2 cd11989
Second Src homology 3 domain (or SH3B) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
746-797 2.19e-04

Second Src homology 3 domain (or SH3B) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN1 has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212922 [Multi-domain]  Cd Length: 52  Bit Score: 40.08  E-value: 2.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepgWLGGELKGKTGWFPANYAE 797
Cdd:cd11989     3 QALYPWRAKKDNHLNFNKNDVITVLEQQDM---WWFGEVQGQKGWFPKSYVK 51
mukB PRK04863
chromosome partition protein MukB;
351-659 2.23e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.33  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  351 EDKKRENFERGnLELEKRRQALLEQQRKEQERLAQLERAEQERKERER----------------------QEQERKRQ-- 406
Cdd:PRK04863  278 ANERRVHLEEA-LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESdleqdyqaasdhlnlvqtalrqQEKIERYQad 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  407 -LELEKQLEKQRELERQREEERRKEIERREAAKRELER-QRQLEwERNRRQELLNQRNKEQEDIVVLKAKKKTL----EF 480
Cdd:PRK04863  357 lEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDElKSQLA-DYQQALDVQQTRAIQYQQAVQALERAKQLcglpDL 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  481 ELEALNDKKHQLEGKLQDircrLTTQRQEIEstnksRELRIAEITHLQQQLQEsqqmlgrlipekQILNDQLKQVQQNSL 560
Cdd:PRK04863  436 TADNAEDWLEEFQAKEQE----ATEELLSLE-----QKLSVAQAAHSQFEQAY------------QLVRKIAGEVSRSEA 494
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  561 HRDSLVTLKRALEAKELA--RQHLRDQLDEVEKETRSKlqeidifNNQLKELREIHNKQQLQKQKSMEAERLkQKEQERK 638
Cdd:PRK04863  495 WDVARELLRRLREQRHLAeqLQQLRMRLSELEQRLRQQ-------QRAERLLAEFCKRLGKNLDDEDELEQL-QEELEAR 566
                         330       340
                  ....*....|....*....|..
gi 768021416  639 IIELEKQKEEA-QRRAQERDKQ 659
Cdd:PRK04863  567 LESLSESVSEArERRMALRQQL 588
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
335-416 2.38e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 42.90  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLpvtfeDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 414
Cdd:COG2825    48 LEKEFKKRQAEL-----QKLEKELQALQEKLQKEAATLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQELLQPIL 122

                  ..
gi 768021416  415 KQ 416
Cdd:COG2825   123 EK 124
SH3_SNX18 cd11897
Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal ...
746-797 2.52e-04

Src Homology 3 domain of Sorting nexin 18; SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. It binds FIP5 and is required for apical lumen formation. It may also play a role in axonal elongation. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNX18 also contains BAR and SH3 domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212830 [Multi-domain]  Cd Length: 55  Bit Score: 39.97  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGG-ELKGKTGWFPANYAE 797
Cdd:cd11897     3 RALYDFRSENPGEISLREHEVLSLCSEQDIE-GWLEGvNSRGDRGLFPASYVE 54
RIB43A pfam05914
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ...
375-685 2.90e-04

RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.


Pssm-ID: 461780 [Multi-domain]  Cd Length: 372  Bit Score: 44.50  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   375 QQRKEQERLAQLERAEQERKER----------------ERQEQERKRQLELEKQLEKQRELERQREEERRKEIErreaaK 438
Cdd:pfam05914    1 VDLKEAAAIERRRQREEERKSRifnarnrtigvdvealDKQVEEKKRQEAAEKAREEAFAEEMVQNDKIALMLE-----K 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   439 RELERQRQLEWE----RNRRQELLNQRNKEQEDIVVLKAKKKTLE--------------FELEALNDKKHQLEGKLQdIR 500
Cdd:pfam05914   76 REEEDRRRLNKElnefRQQHQRPETRREFDLNDPDALKKDLPARVsdddprcgpssmqkFEGEDLNREERKKLQQEQ-MR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   501 CRLTTQRQEIESTNKSRelRIAEITHlqqqlqesqqmlgrlipEKQILNDQLKQVQQNSLHRDSlvtlKRALeAKELARQ 580
Cdd:pfam05914  155 EWLEQQIEEKKQAEEEE--KHAELLY-----------------DQKRLERDRRALELAKLEEEC----RRAV-NAATKNF 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   581 HLRDQLDEVEKETRSKLQEidifnnQLKELREIH----------NKQQLQKQ-----------KSMEAERLK--QKEQER 637
Cdd:pfam05914  211 NQALAAEQAERRRLEKRQE------QEDNLAEIYnhltsdllteNPEVAQSSlgphrvipdrwKGMSPEQLKeiRKEQEQ 284
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 768021416   638 KIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRprklhEEEKLKRE 685
Cdd:pfam05914  285 QREEKERRREEEKQRDAEWDRQRLELARAALLLER-----EQQRLRRE 327
SH3_Intersectin1_5 cd11995
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
747-797 2.92e-04

Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212928 [Multi-domain]  Cd Length: 54  Bit Score: 39.55  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11995     5 GMYDYTAQNDDELAFSKGQIINVLNKE--DPDWWKGELNGQVGLFPSNYVK 53
SH3_p67phox_C cd12046
C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, ...
747-797 2.96e-04

C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, also called Neutrophil cytosol factor 2 (NCF-2), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox plays a regulatory role and contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. It binds, via its C-terminal SH3 domain, to a proline-rich region of p47phox and upon activation, this complex assembles with flavocytochrome b558, the Nox2-p22phox heterodimer. Concurrently, RacGTP translocates to the membrane and interacts with the TPR domain of p67phox, which leads to the activation of NADPH oxidase. The PB1 domain of p67phox binds to its partner PB1 domain in p40phox, and this facilitates the assembly of p47phox-p67phox at the membrane. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212979 [Multi-domain]  Cd Length: 53  Bit Score: 39.40  E-value: 2.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdESQTGEPgWLGGELKGKTGWFPANYAE 797
Cdd:cd12046     4 ALFSYEASQPEDLEFQKGDVILV-LSKVNED-WLEGQCKGKIGIFPSAFVE 52
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
550-686 3.22e-04

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 43.15  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   550 DQLKQVQQNSLHRDSLVT------LKRALEAKELARQHLRDQLDEVEKETRSKLqeidifnNQLKELREIHNKQQLQKQK 623
Cdd:pfam13904   39 TYARKLEGLKLERQPLEAyenwlaAKQRQRQKELQAQKEEREKEEQEAELRKRL-------AKEKYQEWLQRKARQQTKK 111
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021416   624 SMEAERLKQKEQERKIIELEKqKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREE 686
Cdd:pfam13904  112 REESHKQKAAESASKSLAKPE-RKVSQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEE 173
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
363-497 3.32e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 44.21  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   363 LELEKRRQALLEQQRKEQERLAQLERAEQERK-----ERERQEQERKRQLELEKQLEKQrelerqreeerrkeierreaa 437
Cdd:pfam07767  209 KKRLKEEEKLERVLEKIAESAATAEAREEKRKtkaqrNKEKRRKEEEREAKEEKALKKK--------------------- 267
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   438 KRELERQRQLewernrRQELLNQRNKEQEDIVVLKAKKKTLEFELEALndKKHQLeGKLQ 497
Cdd:pfam07767  268 LAQLERLKEI------AKEIAEKEKEREEKAEARKREKRKKKKEEKKL--RPRKL-GKHK 318
SH3_Intersectin2_5 cd11996
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
747-797 3.46e-04

Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212929 [Multi-domain]  Cd Length: 54  Bit Score: 39.58  E-value: 3.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11996     5 AMYDYTANNEDELSFSKGQLINVLNKD--DPDWWQGEINGVTGLFPSNYVK 53
SH3_Shank3 cd11984
Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 3; Shank3, also ...
747-794 3.50e-04

Src homology 3 domain of SH3 and multiple ankyrin repeat domains protein 3; Shank3, also called ProSAP2 (Proline-rich synapse-associated protein 2), is widely expressed. It plays a role in the formation of dendritic spines and synapses. Haploinsufficiency of the Shank3 gene causes the 22q13 deletion/Phelan-McDermid syndrome, and variants of Shank3 have been implicated in autism spectrum disorder, schizophrenia, and intellectual disability. Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212917  Cd Length: 52  Bit Score: 39.55  E-value: 3.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPAN 794
Cdd:cd11984     5 AVKAYSPQGEGEIQLNRGERVKV--LSIGEGGFWEGTVKGRTGWFPAD 50
SH3_GRB2_N cd11946
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
747-797 3.50e-04

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. Its N-terminal SH3 domain binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212879 [Multi-domain]  Cd Length: 56  Bit Score: 39.62  E-value: 3.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGGELKGKTGWFPANYAE 797
Cdd:cd11946     5 AKYDFKATADDELSFKRGDILKVLNEECDQ-NWYKAELNGKDGFIPKNYIE 54
SH3_Sorbs1_1 cd11919
First Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; ...
746-799 3.56e-04

First Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212852 [Multi-domain]  Cd Length: 55  Bit Score: 39.56  E-value: 3.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVdESQTGEpGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd11919     4 RAKFDFKAQTLKELPLQKGDIVYI-YKQIDQ-NWYEGEHHGRVGIFPRSYIELL 55
SH3_DNMBP_N3 cd11796
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
746-795 3.63e-04

Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212730  Cd Length: 51  Bit Score: 39.26  E-value: 3.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11796     3 RVLQDLSAQLDEELDLREGDVVTI--TGILDKGWFRGELNGRRGIFPEGF 50
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
336-457 3.78e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   336 EDEQQQLEKKLpvtfedKKRENFERGNLE--LEKRRQALLEQQRKEQERLAQLER-AEQERKERERQEQERKRQLELEKQ 412
Cdd:pfam13868  221 QKEREEAEKKA------RQRQELQQAREEqiELKERRLAEEAEREEEEFERMLRKqAEDEEIEQEEAEKRRMKRLEHRRE 294
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 768021416   413 LEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQEL 457
Cdd:pfam13868  295 LEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
PRK01156 PRK01156
chromosome segregation protein; Provisional
453-686 3.81e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 44.51  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  453 RRQELLNQR---NKEQEDIVVLKAKKKTLEFELEALNDKKHQLegklqdircrlttQRQEIESTNKSRELRIAEITHLQq 529
Cdd:PRK01156  150 QRKKILDEIleiNSLERNYDKLKDVIDMLRAEISNIDYLEEKL-------------KSSNLELENIKKQIADDEKSHSI- 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  530 qlqesqqmlgrLIPEKQILNDQLKQVQQNSLHRDSlvTLKRALEAKELArqhlrDQLDEVEKETRSKLQEIDIFNNQLKE 609
Cdd:PRK01156  216 -----------TLKEIERLSIEYNNAMDDYNNLKS--ALNELSSLEDMK-----NRYESEIKTAESDLSMELEKNNYYKE 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  610 LREIHN--------------------KQQLQKQKSM----EAERLKQKEQERKIIELEK---QKEEAQRRAQERDKQWLE 662
Cdd:PRK01156  278 LEERHMkiindpvyknrnyindyfkyKNDIENKKQIlsniDAEINKYHAIIKKLSVLQKdynDYIKKKSRYDDLNNQILE 357
                         250       260
                  ....*....|....*....|....
gi 768021416  663 HVQQEDEHQRPRKLHEEEKLKREE 686
Cdd:PRK01156  358 LEGYEMDYNSYLKSIESLKKKIEE 381
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
541-704 4.26e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.22  E-value: 4.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   541 LIP-EKQILNDQLKQVQQNSLHRDSLVtlKRALEAKELARQHLRDQLD--EVEKETRSKLQEIDIFNNQLKELREIHNKQ 617
Cdd:pfam05262  157 VIPlKKNILSGNVSDVDTDSISDKKVV--EALREDNEKGVNFRRDMTDlkERESQEDAKRAQQLKEELDKKQIDADKAQQ 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   618 QLQ-KQKSMEAER--LKQKEQERKIIELEKQKEEAQ--RRAQERDKQWLEHVQQE----DEHQRPRKLHEEEKLKREesv 688
Cdd:pfam05262  235 KADfAQDNADKQRdeVRQKQQEAKNLPKPADTSSPKedKQVAENQKREIEKAQIEikknDEEALKAKDHKAFDLKQE--- 311
                          170
                   ....*....|....*.
gi 768021416   689 kkkdgEEKGKQEAQDK 704
Cdd:pfam05262  312 -----SKASEKEAEDK 322
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
606-686 4.32e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.95  E-value: 4.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   606 QLKELREIHNKQQLQKQksmEAERLKQKEQERKIIE-LEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKR 684
Cdd:pfam05672   22 QAREQREREEQERLEKE---EEERLRKEELRRRAEEeRARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQER 98

                   ..
gi 768021416   685 EE 686
Cdd:pfam05672   99 LQ 100
PRK12705 PRK12705
hypothetical protein; Provisional
339-484 4.33e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.93  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  339 QQQLEKKLPVTFEDKKRENfERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKER---ERQEQERKRQLELEKQLEK 415
Cdd:PRK12705   28 RQRLAKEAERILQEAQKEA-EEKLEAALLEAKELLLRERNQQRQEARREREELQREEErlvQKEEQLDARAEKLDNLENQ 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416  416 QRELERQREEERRKEIERREAAKRELERQRQLEWERnRRQELLNQRNKEQEDIVVLKAKKKTLEFELEA 484
Cdd:PRK12705  107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQ-ARKLLLKLLDAELEEEKAQRVKKIEEEADLEA 174
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
335-517 4.33e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  335 LEDEQQQLEKKLPVTFEDKKRENFERGNLE-----LEKRRQALLEQQRKEQERLAQLERAEQE-RKERERQEQERKRQL- 407
Cdd:COG4942    32 LQQEIAELEKELAALKKEEKALLKQLAALErriaaLARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELLr 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  408 --------------------------------------ELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQ-LE 448
Cdd:COG4942   112 alyrlgrqpplalllspedfldavrrlqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAaLE 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416  449 WERNRRQELLNQrnkeqedivvLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSR 517
Cdd:COG4942   192 ALKAERQKLLAR----------LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
PHA03247 PHA03247
large tegument protein UL36; Provisional
805-995 4.44e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  805 PAPVKPVTDSTSAPAPKLAlrETPAPLAVTSSEPSTTPNNWADFSSTWPTSTNEKPETDNWDAWAAQPSlTVPSAGQLRQ 884
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPT--PEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA-RPARPPTTAG 2765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  885 RSAFTPATATGSSPSPVLGQPDFLLHPSMRLGHMQPRIVLLFPDPLQCSTSRLLPMLRPRPGVPFLRSPSCQSPSHPSRP 964
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP 2845
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 768021416  965 ISDA-------APSVKFTLMPPGRIHPCflfIPAVNSR 995
Cdd:PHA03247 2846 PPPSlplggsvAPGGDVRRRPPSRSPAA---KPAAPAR 2880
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
327-522 4.61e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.34  E-value: 4.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   327 QRLPEEPVLEDE---QQQLEKKLPVTFEDKKRENFERGNLELEKRRQallEQQRKEQERLAQLERAEQERKeRERQEQER 403
Cdd:pfam17380  438 RRLEEERAREMErvrLEEQERQQQVERLRQQEEERKRKKLELEKEKR---DRKRAEEQRRKILEKELEERK-QAMIEEER 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   404 KRQLeLEKQLEKQRELerqreeerrkeIErreaakrELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKtlefeLE 483
Cdd:pfam17380  514 KRKL-LEKEMEERQKA-----------IY-------EEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR-----LE 569
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 768021416   484 ALNDKKHQLegklqdircrlttqRQEIESTNKSRELRIA 522
Cdd:pfam17380  570 AMEREREMM--------------RQIVESEKARAEYEAT 594
SH3_FCHSD2_2 cd11894
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain ...
744-797 4.89e-04

Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212827  Cd Length: 56  Bit Score: 39.15  E-value: 4.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMV--DESQTGEPGWlGGELKGKTGWFPANYAE 797
Cdd:cd11894     1 FVKALYDYEGQTDDELSFPEGAIIRIlnKENQDDDGFW-EGEFNGRIGVFPSVLVE 55
SH3_Shank cd11832
Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins; Shank ...
744-793 5.06e-04

Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins; Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. They bind a variety of membrane and cytosolic proteins, and exist in alternatively spliced isoforms. They are highly enriched in postsynaptic density (PSD) where they interact with the cytoskeleton and with postsynaptic membrane receptors including NMDA and glutamate receptors. They are crucial in the construction and organization of the PSD and dendritic spines of excitatory synapses. There are three members of this family (Shank1, Shank2, Shank3) which show distinct and cell-type specific patterns of expression. Shank1 is brain-specific; Shank2 is found in neurons, glia, endocrine cells, liver, and kidney; Shank3 is widely expressed. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212766  Cd Length: 50  Bit Score: 38.96  E-value: 5.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPA 793
Cdd:cd11832     1 YFIAVKSYSPQEEGEISLHKGDRVKV--LSIGEGGFWEGSVRGRTGWFPS 48
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
746-795 5.10e-04

Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212988 [Multi-domain]  Cd Length: 53  Bit Score: 38.82  E-value: 5.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  746 RALYPFESRSHDEITIQPGDIV-MVDESqtgEPGWLGGELKGKTGWFPANY 795
Cdd:cd12055     3 QVAFSYLPQNEDELELKVGDIIeVVGEV---EEGWWEGVLNGKTGMFPSNF 50
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
746-798 5.10e-04

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 38.84  E-value: 5.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  746 RALYPFESRSHDEITIQPGDIV--MVDESQTGepgWLGGEL--KGKTGWFPANYAEK 798
Cdd:cd11779     4 KALYPHAAGGETQLSFEEGDVItlLGPEPRDG---WHYGENerSGRRGWFPIAYTEP 57
SH3_Nck1_3 cd11904
Third Src Homology 3 domain of Nck1 adaptor protein; Nck1 (also called Nckalpha) plays a ...
746-795 5.15e-04

Third Src Homology 3 domain of Nck1 adaptor protein; Nck1 (also called Nckalpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds and activates RasGAP, resulting in the downregulation of Ras. It is also involved in the signaling of endothilin-mediated inhibition of cell migration. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The third SH3 domain of Nck appears to prefer ligands with a PxAPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212837 [Multi-domain]  Cd Length: 57  Bit Score: 39.24  E-value: 5.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLG-GELKGKTGWFPANY 795
Cdd:cd11904     4 QALYPFSSSNDEELNFEKGEVMDVIEKPENDPEWWKcRKANGQVGLVPKNY 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
351-524 5.26e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  351 EDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKE 430
Cdd:COG1196   630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  431 IERREAAKRELERQRQLEWERNR-RQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDI---------- 499
Cdd:COG1196   710 AEAEEERLEEELEEEALEEQLEAeREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaiee 789
                         170       180       190
                  ....*....|....*....|....*....|..
gi 768021416  500 --RCR-----LTTQRQEIESTNKSRELRIAEI 524
Cdd:COG1196   790 yeELEerydfLSEQREDLEEARETLEEAIEEI 821
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
744-795 5.96e-04

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212884  Cd Length: 53  Bit Score: 38.63  E-value: 5.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGELKGKTGWFPANY 795
Cdd:cd11951     1 FVQAQYDFSAEDPSQLSFRRGDIIEVLDCP--DPNWWRGRISGRVGFFPRNY 50
SH3_Vinexin_3 cd11918
Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain ...
745-795 6.00e-04

Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212851 [Multi-domain]  Cd Length: 58  Bit Score: 38.79  E-value: 6.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGG--ELKGKTGWFPANY 795
Cdd:cd11918     4 YKAVYQYRPQNEDELELREGDRVDV--MQQCDDGWFVGvsRRTQKFGTFPGNY 54
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
337-596 6.46e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  337 DEQQQLEKKLpvtfedkkrenfERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQL-ELEKQLEK 415
Cdd:COG4942    20 DAAAEAEAEL------------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaALEAELAE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  416 qreLERQreeerrkeierREAAKRELERQRQLEWERNRRQellnQRNKEQEDIVVLKAKKKTLEFE-----LEALNDKKH 490
Cdd:COG4942    88 ---LEKE-----------IAELRAELEAQKEELAELLRAL----YRLGRQPPLALLLSPEDFLDAVrrlqyLKYLAPARR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  491 QLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEIthlqqqlqesQQMLGRLIPEKQILNDQLKQVQQNslhrdsLVTLKR 570
Cdd:COG4942   150 EQAEELRADLAELAALRAELEAERAELEALLAEL----------EEERAALEALKAERQKLLARLEKE------LAELAA 213
                         250       260
                  ....*....|....*....|....*.
gi 768021416  571 ALEAKELARQHLRDQLDEVEKETRSK 596
Cdd:COG4942   214 ELAELQQEAEELEALIARLEAEAAAA 239
SH3_Tks_2 cd12016
Second Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src ...
745-798 6.52e-04

Second Src homology 3 domain of Tyrosine kinase substrate (Tks) proteins; Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Vertebrates contain two Tks proteins, Tks4 (Tyr kinase substrate with four SH3 domains) and Tks5 (Tyr kinase substrate with five SH3 domains), which display partially overlapping but non-redundant functions. Both associate with the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. Tks5 interacts with N-WASP and Nck, while Tks4 is essential for the localization of MT1-MMP (membrane-type 1 matrix metalloproteinase) to invadopodia. Tks proteins contain an N-terminal Phox homology (PX) domain and four or five SH3 domains. This model characterizes the second SH3 domain of Tks proteins. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212949  Cd Length: 54  Bit Score: 38.59  E-value: 6.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQTgePGWLGGELKGKTGWFPANYAEK 798
Cdd:cd12016     3 YITTQAYKAENEDEIGFETGVVVEVIQKNL--DGWWKIRYQGKEGWAPATYLKK 54
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
563-655 6.60e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 43.04  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   563 DSLVTLKRALEAKELARQHLRDQLDEVEKETRSkLQEIDIFNNQLKELREIHNKQQL-QKQKSMEAER----------LK 631
Cdd:pfam02841  190 EAILQTDQALTAKEKAIEAERAKAEAAEAEQEL-LREKQKEEEQMMEAQERSYQEHVkQLIEKMEAEReqllaeqermLE 268
                           90       100
                   ....*....|....*....|....
gi 768021416   632 QKEQERKIIELEKQKEEAQRRAQE 655
Cdd:pfam02841  269 HKLQEQEELLKEGFKTEAESLQKE 292
SH3_PACSIN_like cd11999
Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C ...
743-797 6.77e-04

Src homology 3 domain of an unknown subfamily of proteins with similarity to Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212932 [Multi-domain]  Cd Length: 56  Bit Score: 38.77  E-value: 6.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  743 VYYRALYPFESRSHDEITIQPGDIVMVDESQTgEPGWLGG-ELKGKTGWFPANYAE 797
Cdd:cd11999     2 VRVRAVYDYTGQEPDELSFKAGEELLKVEDED-EQGWCKGvTDGGAVGLYPANYVE 56
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
478-675 6.88e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.59  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   478 LEFELEALNDKKHQLEGKLQdIRCRLTTQRqeiesTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQL---KQ 554
Cdd:pfam07111  479 LSLELEQLREERNRLDAELQ-LSAHLIQQE-----VGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLevaRQ 552
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   555 VQQNSlhRDSLVTLKRAL-EAKELARQHLRDQLDEVEKETRSKLQEIDifnNQLKELREIHNKQQLQ-KQKSMEAERLKQ 632
Cdd:pfam07111  553 GQQES--TEEAASLRQELtQQQEIYGQALQEKVAEVETRLREQLSDTK---RRLNEARREQAKAVVSlRQIQHRATQEKE 627
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 768021416   633 KEQERKIIELEKQKEEAQRRAQ-----ERDKQ-WLEHVQQEDEHQRPRK 675
Cdd:pfam07111  628 RNQELRRLQDEARKEEGQRLARrvqelERDKNlMLATLQQEGLLSRYKQ 676
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
337-503 6.91e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  337 DEQQQLEKKLPVTFEDKKREnfergnlELEKRRQALLEQQRKEQERLAQLERAEQERKERER------------------ 398
Cdd:COG4913   272 AELEYLRAALRLWFAQRRLE-------LLEAELEELRAELARLEAELERLEARLDALREELDeleaqirgnggdrleqle 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  399 QEQERkrqleLEKQLEKQRELERQREEERRKEIERREAAKRELERQRQ-----LEWERNRRQELLNQRNKEQEDIVVLKA 473
Cdd:COG4913   345 REIER-----LERELEERERRRARLEALLAALGLPLPASAEEFAALRAeaaalLEALEEELEALEEALAEAEAALRDLRR 419
                         170       180       190
                  ....*....|....*....|....*....|
gi 768021416  474 KKKTLEFELEALNDKKHQLEGKLQDIRCRL 503
Cdd:COG4913   420 ELRELEAEIASLERRKSNIPARLLALRDAL 449
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
745-795 6.98e-04

Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212717 [Multi-domain]  Cd Length: 55  Bit Score: 38.53  E-value: 6.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGGE--LKGKTGWFPANY 795
Cdd:cd11783     2 YVALYPYKPQKPDELELRKGEMYTVTEKC--QDGWFKGTslRTGQSGVFPGNY 52
EF-hand_7 pfam13499
EF-hand domain pair;
224-283 7.05e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 7.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416   224 KYRQLFNSHDKTMSGHLT----GPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAM 283
Cdd:pfam13499    3 KLKEAFKLLDSDGDGYLDveelKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SH3_ARHGEF16_26 cd11938
Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26; ...
751-797 7.12e-04

Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF16 and ARHGEF26; ARHGEF16, also called ephexin-4, acts as a GEF for RhoG, activating it by exchanging bound GDP for free GTP. RhoG is a small GTPase that is a crucial regulator of Rac in migrating cells. ARHGEF16 interacts directly with the ephrin receptor EphA2 and mediates cell migration and invasion in breast cancer cells by activating RhoG. ARHGEF26, also called SGEF (SH3 domain-containing guanine exchange factor), also activates RhoG. It is highly expressed in liver and may play a role in regulating membrane dynamics. ARHGEF16 and ARHGEF26 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212871  Cd Length: 55  Bit Score: 38.67  E-value: 7.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  751 FESRSHDEITIQPGDIVMVdeSQTGEPGWLGGEL--KGKTGWFPANYAE 797
Cdd:cd11938     8 YTAKQPDELSLQQADVVLV--LQTESDGWYYGERlrDGERGWFPSSCAK 54
RNase_Y_N pfam12072
RNase Y N-terminal region;
338-415 7.33e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.80  E-value: 7.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   338 EQQQLEKKLPVTFE--DKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKER-ER-----QEQERKRQL-E 408
Cdd:pfam12072   79 ELQRQERRLLQKEEtlDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEELIEEQRQElERisgltSEEAKEILLdE 158

                   ....*..
gi 768021416   409 LEKQLEK 415
Cdd:pfam12072  159 VEEELRH 165
SH3_PLCgamma cd11825
Src homology 3 domain of Phospholipase C (PLC) gamma; PLC catalyzes the hydrolysis of ...
746-798 7.39e-04

Src homology 3 domain of Phospholipase C (PLC) gamma; PLC catalyzes the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG) in response to various receptors. Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma catalyzes this reaction in tyrosine kinase-dependent signaling pathways. It is activated and recruited to its substrate at the membrane. Vertebrates contain two forms of PLCgamma, PLCgamma1, which is widely expressed, and PLCgamma2, which is primarily found in haematopoietic cells. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. The SH3 domain of PLCgamma1 directly interacts with dynamin-1 and can serve as a guanine nucleotide exchange factor (GEF). It also interacts with Cbl, inhibiting its phosphorylation and activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212759 [Multi-domain]  Cd Length: 54  Bit Score: 38.47  E-value: 7.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGK-TGWFPANYAEK 798
Cdd:cd11825     3 KALYDYRAQRPDELSFCKHAIITNVEKEDG--GWWRGDYGGKkQKWFPANYVEE 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
547-717 7.45e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 7.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   547 ILNDQLKQVQQNSLHR---DSLVTLKRALEAKELA---------RQHLRDQLDEVEKetrsklqEIDIFNNQLKELR-EI 613
Cdd:TIGR02169  195 EKRQQLERLRREREKAeryQALLKEKREYEGYELLkekealerqKEAIERQLASLEE-------ELEKLTEEISELEkRL 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   614 HNKQQLQKQKSMEAERLKQKEQ---ERKIIELEKQKEEAQR--RAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKR--EE 686
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEEQlrvKEKIGELEAEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEELEReiEE 347
                          170       180       190
                   ....*....|....*....|....*....|.
gi 768021416   687 SVKKKDGEEKGKQEAQDKLGRLFHQHQEPAK 717
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
332-645 8.55e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 8.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   332 EPVLEDEQQQLEKKLPVTFEDKKRENFERGNL----ELEKRRQALLEQQRKEQERLAQL--ERAEQERKERERQeQERKR 405
Cdd:TIGR00618  541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFsiltQCDNRSKEDIPNLQNITVRLQDLteKLSEAEDMLACEQ-HALLR 619
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   406 QLELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLE-WERNRRQEL------LNQRNKEQEDIVVLKAKKKTL 478
Cdd:TIGR00618  620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKellasrQLALQKMQSEKEQLTYWKEML 699
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   479 EFELEALNDkKHQLEGKL----QDIRCRLTTQRQEI--------ESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQ 546
Cdd:TIGR00618  700 AQCQTLLRE-LETHIEEYdrefNEIENASSSLGSDLaaredalnQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA 778
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   547 ILNDQLKQVQQNSLHRDSLVTLKRALEAKelARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELreiHNKQ-QLQKQKSM 625
Cdd:TIGR00618  779 ELSHLAAEIQFFNRLREEDTHLLKTLEAE--IGQEIPSDEDILNLQCETLVQEEEQFLSRLEEK---SATLgEITHQLLK 853
                          330       340
                   ....*....|....*....|....
gi 768021416   626 EAERLKQKEQ----ERKIIELEKQ 645
Cdd:TIGR00618  854 YEECSKQLAQltqeQAKIIQLSDK 877
SH3_Intersectin1_4 cd11993
Fourth Src homology 3 domain (or SH3D) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
746-797 9.33e-04

Fourth Src homology 3 domain (or SH3D) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The fourth SH3 domain (or SH3D) of ITSN1 has been shown to bind SHIP2, Numb, CdGAP, and N-WASP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212926  Cd Length: 65  Bit Score: 38.56  E-value: 9.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGepGWLGGEL-----KGKTGWFPANYAE 797
Cdd:cd11993     7 QVIASYTATGPEQLTLAPGQLILIRKKNPG--GWWEGELqargkKRQIGWFPANYVK 61
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
335-708 1.03e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 43.11  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERE--------RQEQERKRQ 406
Cdd:TIGR00606  476 LDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmltkdkmdKDEQIRKIK 555
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   407 LELEKQLEKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQedivvlkakkKTLEFELEALN 486
Cdd:TIGR00606  556 SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL----------ESKEEQLSSYE 625
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   487 DKKHQLEGKlQDIRCRLTTQRQEIESTNKSRELRIAE-------ITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNS 559
Cdd:TIGR00606  626 DKLFDVCGS-QDEESDLERLKEEIEKSSKQRAMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL 704
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   560 -LHRDSLVTLKRALEAKELARQHL-------RDQLDEVEK---ETRSKLQEIdifNNQLKELREIHNKQQLQKQKSMEAE 628
Cdd:TIGR00606  705 rLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKeipELRNKLQKV---NRDIQRLKNDIEEQETLLGTIMPEE 781
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   629 RLKQKEQ------ERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKL--KREESVKKKDGEEKGKQE 700
Cdd:TIGR00606  782 ESAKVCLtdvtimERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVvsKIELNRKLIQDQQEQIQH 861

                   ....*...
gi 768021416   701 AQDKLGRL 708
Cdd:TIGR00606  862 LKSKTNEL 869
SH3_Amphiphysin_I cd12140
Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and ...
748-799 1.06e-03

Src Homology 3 domain of Amphiphysin I; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213016  Cd Length: 72  Bit Score: 38.72  E-value: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  748 LYPFESRSHDEITIQPGDIVMVDESQTG---EPGWLGG----------ELKGKTGWFPANYAEKI 799
Cdd:cd12140     8 LHDFEAANSDELELKRGDIVLVVPSETAadqDAGWLTGvkesdwlqyrDASAYKGLFPENFTRRL 72
SH3_Nck1_2 cd11901
Second Src Homology 3 domain of Nck1 adaptor protein; Nck1 (also called Nckalpha) plays a ...
749-795 1.10e-03

Second Src Homology 3 domain of Nck1 adaptor protein; Nck1 (also called Nckalpha) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds and activates RasGAP, resulting in the downregulation of Ras. It is also involved in the signaling of endothilin-mediated inhibition of cell migration. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212834 [Multi-domain]  Cd Length: 55  Bit Score: 38.09  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 768021416  749 YPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTGWFPANY 795
Cdd:cd11901     8 FNYTAEREDELSLVKGTKVIVMEKCSD--GWWRGSYNGQVGWFPSNY 52
SH3_Sorbs1_3 cd11916
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), ...
742-797 1.16e-03

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212849 [Multi-domain]  Cd Length: 59  Bit Score: 38.05  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  742 VVYYRALYPFESRSHDEITIQPGDIvmVDESQTGEPGWLGGELK--GKTGWFPANYAE 797
Cdd:cd11916     1 AYSYQALYSYAPQNDDELELRDGDI--VDVMEKCDDGWFVGTSRrtKQFGTFPGNYVK 56
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
588-686 1.17e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.53  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   588 EVEKETRSKLQEIDIFNNQLKELREihNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQE 667
Cdd:TIGR02794   51 QANRIQQQKKPAAKKEQERQKKLEQ--QAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ 128
                           90       100
                   ....*....|....*....|....*.
gi 768021416   668 -------DEHQRPRKLHEEEKLKREE 686
Cdd:TIGR02794  129 aaeakakAEAEAERKAKEEAAKQAEE 154
SH3_Intersectin2_2 cd11990
Second Src homology 3 domain (or SH3B) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
746-795 1.23e-03

Second Src homology 3 domain (or SH3B) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The second SH3 domain (or SH3B) of ITSN2 is expected to bind protein partners, similar to ITSN1 which has been shown to bind WNK and CdGAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212923 [Multi-domain]  Cd Length: 52  Bit Score: 37.71  E-value: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQtgEPGWLGgELKGKTGWFPANY 795
Cdd:cd11990     3 QALCSWTAKKDNHLNFSKNDIITVLEQQ--ENWWFG-EVHGGRGWFPKSY 49
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
335-416 1.26e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.26  E-value: 1.26e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416    335 LEDEQQQLEKKLpvtfeDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 414
Cdd:smart00935   23 LEKEFKKRQAEL-----EKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKIL 97

                    ..
gi 768021416    415 KQ 416
Cdd:smart00935   98 DK 99
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
212-284 1.28e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021416  212 VAEWAVPQSSRLKYRQLFNSHDKTMSGHLTGPQARTILMQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMH 284
Cdd:COG5126    58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
484-707 1.29e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  484 ALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLqqqlqesqqmlgrlipEKQI--LNDQLKQVQQNslh 561
Cdd:COG4942    17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----------------ERRIaaLARRIRALEQE--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  562 rdsLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIE 641
Cdd:COG4942    78 ---LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  642 LEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGR 707
Cdd:COG4942   155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
SH3_SH3RF1_3 cd11926
Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ...
745-795 1.37e-03

Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ligase; SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212859 [Multi-domain]  Cd Length: 55  Bit Score: 37.64  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESqtGEPGWLGGEL--KGKTGWFPANY 795
Cdd:cd11926     2 YVAIYPYTPRKEDELELRKGEMFLVFER--CQDGWFKGTSmhTSKIGVFPGNY 52
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
224-284 1.47e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.91  E-value: 1.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021416  224 KYRQLFNSHDKTMSGHLTGPQARTIL--MQSSLPQAQLASIWNLSDIDQDGKLTAEEFILAMH 284
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALksLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
SH3_Bbc1 cd11887
Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces ...
746-798 1.51e-03

Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces cerevisiae Bbc1p, also called Mti1p (Myosin tail region-interacting protein), and similar proteins. Bbc1p interacts with and regulates type I myosins in yeast, Myo3p and Myo5p, which are involved in actin cytoskeletal reorganization. It also binds and inhibits Las17, a WASp family protein that functions as an activator of the Arp2/3 complex. Bbc1p contains an N-terminal SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212820 [Multi-domain]  Cd Length: 60  Bit Score: 37.71  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpgWLGGELKG-----KTGWFPANYAEK 798
Cdd:cd11887     5 KALYPYESDHEDDLNFDVGQLITVTEEEDAD--WYFGEYVDsngntKEGIFPKNFVEV 60
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
342-590 1.55e-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: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  342 LEKklPVTFE--DKKRENFE-----RGNLELEKRRQALLEQQRKEQERLA----QLERAEQERKERERQEQERKRQLeLE 410
Cdd:COG4913   218 LEE--PDTFEaaDALVEHFDdleraHEALEDAREQIELLEPIRELAERYAaareRLAELEYLRAALRLWFAQRRLEL-LE 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  411 KQLEKqrelerqreeeRRKEIERREAAKRELERQRQLEweRNRRQELLNQRNKEQ-EDIVVLKAKKKTLEFELEALNDKK 489
Cdd:COG4913   295 AELEE-----------LRAELARLEAELERLEARLDAL--REELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  490 HQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEIThlqQQLQESQQMLGRLIPEKQILNDQLKQVQQ--NSL-HRDSLV 566
Cdd:COG4913   362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRRELRELEAeiASLeRRKSNI 438
                         250       260
                  ....*....|....*....|....
gi 768021416  567 TlKRALEAKELARQHLrdQLDEVE 590
Cdd:COG4913   439 P-ARLLALRDALAEAL--GLDEAE 459
SH3_ARHGEF37_C2 cd11941
Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37; ARHGEF37 ...
747-795 1.65e-03

Second C-terminal Src homology 3 domain of Rho guanine nucleotide exchange factor 37; ARHGEF37 contains a RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. Its specific function is unknown. Its domain architecture is similar to the C-terminal half of DNMBP or Tuba, a cdc42-specific GEF that provides a functional link between dynamin, Rho GTPase signaling, and actin dynamics, and plays an important role in regulating cell junction configuration. GEFs activate small GTPases by exchanging bound GDP for free GTP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212874  Cd Length: 57  Bit Score: 37.58  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  747 ALYPFESRSHDEITIQPGDIVMVDESQ--TGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11941     4 AAYPFTARSKHEVSLQAGQPVTVLEPHdkKGSPEWSLVEVNGQRGYVPSSY 54
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
550-666 1.70e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 39.99  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   550 DQLKQVQQnsLHRDSLVTLKRALEAKELARQHLRDQLDEVEKETR----------------SKLQEIDIFNNQLKELREI 613
Cdd:TIGR02473    2 FRLQKLLD--LREKEEEQAKLELAKAQAEFERLETQLQQLIKYREeyeqqalekvgagtsaLELSNYQRFIRQLDQRIQQ 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416   614 HNKQQLQKQKSMEA--ERLKQKEQERKIIEL--EKQKEEAQRRAQERDKQWL-EHVQQ 666
Cdd:TIGR02473   80 QQQELALLQQEVEAkrERLLEARRELKALEKlkEKKQKEYRAEEAKREQKEMdELATQ 137
SH3_ARHGEF5_19 cd11940
Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19; ...
751-797 1.81e-03

Src homology 3 domain of the Rho guanine nucleotide exchange factors ARHGEF5 and ARHGEF19; ARHGEF5, also called ephexin-3 or TIM (Transforming immortalized mammary oncogene), is a potent activator of RhoA and it plays roles in regulating cell shape, adhesion, and migration. It binds to the SH3 domain of Src and is involved in regulating Src-induced podosome formation. ARHGEF19, also called ephexin-2 or WGEF (weak-similarity GEF), is highly expressed in the intestine, liver, heart and kidney. It activates RhoA, Cdc42, and Rac 1, and has been shown to activate RhoA in the Wnt-PCP (planar cell polarity) pathway. It is involved in the regulation of cell polarity and cytoskeletal reorganization. ARHGEF5 and ARHGEF19 contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and SH3 domains. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212873  Cd Length: 55  Bit Score: 37.46  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 768021416  751 FESRSHDEITIQPGDIVMVdeSQTGEPGWLGGEL--KGKTGWFPANYAE 797
Cdd:cd11940     8 YKAQENDELTLEKADIIMV--RQQSSDGWLEGVRlsDGERGWFPQSHVE 54
SH3_Nck2_2 cd11902
Second Src Homology 3 domain of Nck2 adaptor protein; Nck2 (also called Nckbeta or Growth ...
749-795 1.94e-03

Second Src Homology 3 domain of Nck2 adaptor protein; Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4) plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling. It binds neuronal signaling proteins such as ephrinB and Disabled-1 (Dab-1) exclusively. Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2, which show partly overlapping functions but also bind distinct targets. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212835 [Multi-domain]  Cd Length: 55  Bit Score: 37.29  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 768021416  749 YPFESRSHDEITIQPGDIVMVDESQTGepGWLGGELKGKTGWFPANY 795
Cdd:cd11902     7 FAYVAEREDELSLVKGSRVTVMEKCSD--GWWRGSYNGQIGWFPSNY 51
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
335-702 1.96e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLpvtfedkkrENFERGNLELEKRRQALLEQQRKEQE---RLAQLERAEQERKERERQEQERKRQlELEK 411
Cdd:TIGR00618  533 GEQTYAQLETSE---------EDVYHQLTSERKQRASLKEQMQEIQQsfsILTQCDNRSKEDIPNLQNITVRLQD-LTEK 602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   412 QLEKQRELERQREeerrkeierreaakrelERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEfELEALNDKKHQ 491
Cdd:TIGR00618  603 LSEAEDMLACEQH-----------------ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL-TLTQERVREHA 664
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   492 LEGKLQDIRCRLTTQRQEIESTNKSRELR--IAEITHLQQQLqesqqmlgRLIPEKQILNDQLKQVQQNSLHrdslvTLK 569
Cdd:TIGR00618  665 LSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQTLL--------RELETHIEEYDREFNEIENASS-----SLG 731
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   570 RALEAKELARQHLRDQLDEvEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEA 649
Cdd:TIGR00618  732 SDLAAREDALNQSLKELMH-QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 768021416   650 QRRAQERDKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQ 702
Cdd:TIGR00618  811 EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
SH3_Abi1 cd11971
Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of ...
741-799 2.06e-03

Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of actin cytoskeletal reorganization through interactions with many protein complexes. It is part of WAVE, a nucleation-promoting factor complex, that links Rac 1 activation to actin polymerization causing lamellipodia protrusion at the plasma membrane. Abi1 interact with formins to promote protrusions at the leading edge of motile cells. It also is a target of alpha4 integrin, regulating membrane protrusions at sites of integrin engagement. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212904 [Multi-domain]  Cd Length: 59  Bit Score: 37.31  E-value: 2.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416  741 KVVyyrALYPFESRSHDEITIQPGDIVMVdeSQTGEPGWLGGELKGKTGWFPANYAEKI 799
Cdd:cd11971     1 KVV---AIYDYSKDKDDELSFMEGAIIYV--IKKNDDGWYEGVCNGVTGLFPGNYVESI 54
SH3_Sorbs_2 cd11782
Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ...
746-797 2.08e-03

Second Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the second SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212716 [Multi-domain]  Cd Length: 53  Bit Score: 37.33  E-value: 2.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVM----VDESqtgepgWLGGELKGKTGWFPANYAE 797
Cdd:cd11782     3 RAKYNFNADTGVELSFRKGDVITltrrVDEN------WYEGRIGGRQGIFPVSYVQ 52
SH3_iASPP cd11952
Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called ...
742-795 2.09e-03

Src Homology 3 (SH3) domain of Inhibitor of ASPP protein (iASPP); iASPP, also called RelA-associated inhibitor (RAI), is an oncoprotein that inhibits the apoptotic transactivation potential of p53. It is upregulated in human breast cancers expressing wild-type p53, in acute leukemias regardless of the p53 mutation status, as well as in ovarian cancer where it is associated with poor patient outcome and chemoresistance. iASPP is also a binding partner and negative regulator of p65RelA, which promotes cell proliferation and inhibits apoptosis; p65RelA has the opposite effect on cell growth compared to the p53 family. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of iASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212885 [Multi-domain]  Cd Length: 56  Bit Score: 37.22  E-value: 2.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  742 VVYyrALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11952     2 VVY--ALWDYSAEFPDELSFKEGDMVTVLRKDGEGTDWWWASLCGREGYVPRNY 53
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
331-676 2.12e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.13  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   331 EEPVLEDEQQQLEKKLPVTFE--DKKRENFERGNLELEKRRQALLEQQRKE----------QERLAQL--------ERAE 390
Cdd:pfam12128  591 DVPEWAASEEELRERLDKAEEalQSAREKQAAAEEQLVQANGELEKASREEtfartalknaRLDLRRLfdekqsekDKKN 670
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   391 QERKERERQEQERKRQLELE-KQLEKQRELERQREEERrkeierreaaKRELERQRQLEWernrrQELLNQRNKEQEDIV 469
Cdd:pfam12128  671 KALAERKDSANERLNSLEAQlKQLDKKHQAWLEEQKEQ----------KREARTEKQAYW-----QVVEGALDAQLALLK 735
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   470 VLKAKKKT-LEFELEALN-DKKHQLEGKLQD--IRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQEsqqmlgRLIPEK 545
Cdd:pfam12128  736 AAIAARRSgAKAELKALEtWYKRDLASLGVDpdVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQE------TWLQRR 809
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   546 QILNDQLKQVQQNSlhRDSLVTLKRALEAKELARQHL---RDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQ 622
Cdd:pfam12128  810 PRLATQLSNIERAI--SELQQQLARLIADTKLRRAKLemeRKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGS 887
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416   623 KSmeaERLKQKEQERKIIELEKQKEE----------AQRRAQERDKQWLEHvqQEDEHQRPRKL 676
Cdd:pfam12128  888 IG---ERLAQLEDLKLKRDYLSESVKkyvehfknviADHSGSGLAETWESL--REEDHYQNDKG 946
Activator_LAG-3 pfam11498
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
606-717 2.17e-03

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.


Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 41.87  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   606 QLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQE--RDKQWLEHVQQEDE-----------HQR 672
Cdd:pfam11498  321 HIAQLAQQQNKMRLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEHQQQQMllQQQQQMHQLQQHHQmngggqfatqaHQH 400
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 768021416   673 PRKLHEEEKLKREESVKKKDGEEKGKQEAQdklgrlfHQHQEPAK 717
Cdd:pfam11498  401 AAYLQQMQHMRLQEQIQHQQQQAQHHQQAQ-------QQHQQPAQ 438
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
582-646 2.22e-03

DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.


Pssm-ID: 462906  Cd Length: 615  Bit Score: 41.92  E-value: 2.22e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021416   582 LRDQLDEVEKEtrsKLQEIDIFNNQLKELREiHNKQQLQKQKSmEAERLkqkEQERKIIELEKQK 646
Cdd:pfam09798    2 LRDKLELLQQE---KEKELEKLKNSYEELKS-SHEEELEKLKQ-EVQKL---EDEKKFLLNELRS 58
SH3_EFS cd12003
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, ...
746-801 2.34e-03

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member, Embryonal Fyn-associated Substrate; EFS is also called HEFS, CASS3 (Cas scaffolding protein family member 3) or SIN (Src-interacting protein). It was identified based on interactions with the Src kinases, Fyn and Yes. It plays a role in thymocyte development and acts as a negative regulator of T cell proliferation. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212936  Cd Length: 62  Bit Score: 37.18  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGE-PGWLGGELKGKTGWFPANYAEKIPE 801
Cdd:cd12003     4 KALYDNAAESPEELSFRRGDVLMVLKREHGSlPGWWLCSLHGQQGIAPANRLRLLPT 60
PRK12585 PRK12585
putative monovalent cation/H+ antiporter subunit G; Reviewed
582-671 2.52e-03

putative monovalent cation/H+ antiporter subunit G; Reviewed


Pssm-ID: 183610  Cd Length: 197  Bit Score: 40.44  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  582 LRDQLDEVEKETRSKLQEIDIFNNQLKELReihnkqqlQKQKSMEaERLKQKEQERKIIELEKQKEEAQrraqERDKQWL 661
Cdd:PRK12585  103 IRDQLRSVKKDDIKKKKSLIIRQEQIEKAR--------QEREELE-ERMEWERREEKIDEREDQEEQER----EREEQTI 169
                          90
                  ....*....|
gi 768021416  662 EHVQQEDEHQ 671
Cdd:PRK12585  170 EEQSDDSEHE 179
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
364-453 2.53e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 39.78  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   364 ELEKRRQALLE------QQRKEQERLAQLERaEQERKERERQEQERKRQLELE---------KQLEKQRELERQREEERR 428
Cdd:pfam15236   46 ERERKRQKALEhqnaikKQLEEKERQKKLEE-ERRRQEEQEEEERLRREREEEqkqfeeerrKQKEKEEAMTRKTQALLQ 124
                           90       100
                   ....*....|....*....|....*
gi 768021416   429 KEIERREAAKRELERQRQLEWERNR 453
Cdd:pfam15236  125 AMQKAQELAQRLKQEQRIRELAEKG 149
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
548-714 2.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  548 LNDQLKQVQQNSLHRDSLVTLKRALE---------------AKELARqhLRDQLDEVEKeTRSKLQEIDIfnnQLKELRE 612
Cdd:COG4913   626 LAEAEERLEALEAELDALQERREALQrlaeyswdeidvasaEREIAE--LEAELERLDA-SSDDLAALEE---QLEELEA 699
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  613 IHN-----KQQLQKQKSMEAERLKQKEQERKiiELEKQKEEAQRRAQERDKQWLE-HVQQEDEHQRPRKLHE--EEKLKR 684
Cdd:COG4913   700 ELEeleeeLDELKGEIGRLEKELEQAEEELD--ELQDRLEAAEDLARLELRALLEeRFAAALGDAVERELREnlEERIDA 777
                         170       180       190
                  ....*....|....*....|....*....|
gi 768021416  685 EESvkkkdgeekGKQEAQDKLGRLFHQHQE 714
Cdd:COG4913   778 LRA---------RLNRAEEELERAMRAFNR 798
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
364-635 2.62e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  364 ELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQL--ELEKQLEKqrelerqreeerrkeierreaaKREL 441
Cdd:COG1340    12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreEAQELREK----------------------RDEL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  442 -ERQRQLeweRNRRQELLNQRNKEQEDIVVLKAKKKT-----------------LEFELE--ALN-DKKHQLEGKLQDIR 500
Cdd:COG1340    70 nEKVKEL---KEERDELNEKLNELREELDELRKELAElnkaggsidklrkeierLEWRQQteVLSpEEEKELVEKIKELE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  501 CRLTTQRQEIESTNKSRELRiAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQnslHRDSLVtlKRALEAKELARQ 580
Cdd:COG1340   147 KELEKAKKALEKNEKLKELR-AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYK---EADELR--KEADELHKEIVE 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021416  581 ------HLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQ 635
Cdd:COG1340   221 aqekadELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEK 281
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
332-687 2.83e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   332 EPVLEDEQQQ---LEKKLPVTFEDKKRENFergnleleKRRQALLEQQRKEQErlAQLER---AEQERKERERQEqerkr 405
Cdd:pfam15921   77 ERVLEEYSHQvkdLQRRLNESNELHEKQKF--------YLRQSVIDLQTKLQE--MQMERdamADIRRRESQSQE----- 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   406 qlELEKQLEKQRelerqreeerrkeierreaakRELERQRQLewernrRQELLNQRNKEQEDIvvlkaKKKTLEFeleal 485
Cdd:pfam15921  142 --DLRNQLQNTV---------------------HELEAAKCL------KEDMLEDSNTQIEQL-----RKMMLSH----- 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   486 ndkkhqlEGKLQDIRCRLT---------TQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPekqiLNDQLKQVQ 556
Cdd:pfam15921  183 -------EGVLQEIRSILVdfeeasgkkIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFP----VEDQLEALK 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   557 QNSLHRDSLVTLKRALEAKELARQH------LRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERL 630
Cdd:pfam15921  252 SESQNKIELLLQQHQDRIEQLISEHeveitgLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRS 331
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416   631 KQKEQER----KIIELEKQ----KEEAQRRAQERDKQWLEHVQQEDEHQR-PRKLHEEEK---LKREES 687
Cdd:pfam15921  332 ELREAKRmyedKIEELEKQlvlaNSELTEARTERDQFSQESGNLDDQLQKlLADLHKREKelsLEKEQN 400
SH3_DBS cd11857
Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, ...
745-794 2.84e-03

Src homology 3 domain of DBL's Big Sister (DBS), a guanine nucleotide exchange factor; DBS, also called MCF2L (MCF2-transforming sequence-like protein) or OST, is a Rho GTPase guanine nucleotide exchange factor (RhoGEF), facilitating the exchange of GDP and GTP. It was originally isolated from a cDNA screen for sequences that cause malignant growth. It plays roles in regulating clathrin-mediated endocytosis and cell migration through its activation of Rac1 and Cdc42. Depending on cell type, DBS can also activate RhoA and RhoG. DBS contains a Sec14-like domain, spectrin-like repeats, a RhoGEF [or Dbl homology (DH)] domain, a Pleckstrin homology (PH) domain, and an SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212791  Cd Length: 55  Bit Score: 36.88  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIV-MVDESQTGEpgWLGGEL-KGKTGWFPAN 794
Cdd:cd11857     2 YTVVADYEKGGPDDLTVKSGDLVqLIHEGDEGQ--WLVKNLsTRKEGWVPAA 51
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
326-707 2.86e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   326 DQRLPEEpvlEDEQQ--QLEKklpVTFEDKKREnFERGNLELEKRRQALLEQQRKEQERLAQLER--AEQERKER----- 396
Cdd:pfam01576  109 EEQLDEE---EAARQklQLEK---VTTEAKIKK-LEEDILLLEDQNSKLSKERKLLEERISEFTSnlAEEEEKAKslskl 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   397 ------------ERQEQERKRQLELEK---QLEKQRELERQREEERRKEIERREA--AKRELERQRQLewerNRRQELLN 459
Cdd:pfam01576  182 knkheamisdleERLKKEEKGRQELEKakrKLEGESTDLQEQIAELQAQIAELRAqlAKKEEELQAAL----ARLEEETA 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   460 QRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIE----STNKSRELRI---AEITHLQQQLQ 532
Cdd:pfam01576  258 QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldTTAAQQELRSkreQEVTELKKALE 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   533 ESQQMLGRLIPEKQI--------LNDQLKQVQQNslhRDSLVTLKRALEA--KELA----------------RQHLRDQL 586
Cdd:pfam01576  338 EETRSHEAQLQEMRQkhtqaleeLTEQLEQAKRN---KANLEKAKQALESenAELQaelrtlqqakqdsehkRKKLEGQL 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   587 DEVE-------------KETRSKLQ-EIDIFNNQLKELR---------------EIHNKQQL----QKQKSMEAERLKQK 633
Cdd:pfam01576  415 QELQarlseserqraelAEKLSKLQsELESVSSLLNEAEgkniklskdvsslesQLQDTQELlqeeTRQKLNLSTRLRQL 494
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021416   634 EQERKIIELEKQKEEAQRRAQER-----DKQWLEHVQQEDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGR 707
Cdd:pfam01576  495 EDERNSLQEQLEEEEEAKRNVERqlstlQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
545-684 2.99e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  545 KQILNDQLKQVQQNslhRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKS 624
Cdd:COG4717    66 PELNLKELKELEEE---LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELA 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768021416  625 MEAERLKQ-KEQERKIIELEKQKEEAQRRAQERDkqwlehvQQEDEHQRPRKLHEEEKLKR 684
Cdd:COG4717   143 ELPERLEElEERLEELRELEEELEELEAELAELQ-------EELEELLEQLSLATEEELQD 196
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
576-686 3.04e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 38.73  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   576 ELARQHLRDQLDEVEKetrsklqEIDIFNNQLKELREIHNKQQLQKQKsmEAERLKQKEQE--RKIIELEKQKE--EAQR 651
Cdd:pfam17675    8 DLLLEELDKQLEDAEK-------ERDAYISFLKKLEKETPEELEELEK--ELEKLEKEEEEllQELEELEKEREelDAEL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 768021416   652 RAQERDKQWLEhvQQEDEHQRPRKLHEEEKLKREE 686
Cdd:pfam17675   79 EALEEELEALD--EEEEEFWREYNALQLQLLEFQD 111
SH3_ASAP cd11821
Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing ...
746-795 3.04e-03

Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing proteins; ASAPs are Arf GTPase activating proteins (GAPs) and they function in regulating cell growth, migration, and invasion. They contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3, but some ASAP3 proteins do not seem to harbor a C-terminal SH3 domain. ASAP1 and ASAP2 show GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but are able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212755 [Multi-domain]  Cd Length: 53  Bit Score: 36.52  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDEsqTGEPGWLGGELKGK---TGWFPANY 795
Cdd:cd11821     3 RALYDCQADNDDELTFSEGEIIVVTG--EEDDEWWEGHIEGDpsrRGVFPVSF 53
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
580-686 3.10e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  580 QHLRDQLDEVEKETRSKLQEIDIFNNQLKElreihNKQQLQKQKsmEAERLKQKEQERKIIElEKQKEEAQRRAQERDKQ 659
Cdd:PRK00409  526 EELERELEQKAEEAEALLKEAEKLKEELEE-----KKEKLQEEE--DKLLEEAEKEAQQAIK-EAKKEADEIIKELRQLQ 597
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 768021416  660 WLEHVQQ-----EDEHQR---PRKLHEEEKLKREE 686
Cdd:PRK00409  598 KGGYASVkahelIEARKRlnkANEKKEKKKKKQKE 632
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
335-708 3.14e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKL--------PVTFEDKKRENFERGNLELEKRRQALlEQQRKEQERLAQLERAEQERKER--ERQEQERK 404
Cdd:pfam12128  435 FNEEEYRLKSRLgelklrlnQATATPELLLQLENFDERIERAREEQ-EAANAEVERLQSELRQARKRRDQasEALRQASR 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   405 RQLELEKQLEkQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQ-EDIVVLKAKKKTLE---- 479
Cdd:pfam12128  514 RLEERQSALD-ELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSvGGELNLYGVKLDLKridv 592
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   480 ----FELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQilNDQLKQV 555
Cdd:pfam12128  593 pewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ--SEKDKKN 670
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   556 QQNSLHRDSLVTLKRALEAK--------ELARQHLRDQLDEVEKETRSKLQE-IDIFNNQLKELreihnKQQLQKQKSME 626
Cdd:pfam12128  671 KALAERKDSANERLNSLEAQlkqldkkhQAWLEEQKEQKREARTEKQAYWQVvEGALDAQLALL-----KAAIAARRSGA 745
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   627 AERLKQKEQERK-------------------IIELEKQKEEAQRRAQE--RDKQWLEHVQQEdehQRPRKLHEEEKLKRE 685
Cdd:pfam12128  746 KAELKALETWYKrdlaslgvdpdviaklkreIRTLERKIERIAVRRQEvlRYFDWYQETWLQ---RRPRLATQLSNIERA 822
                          410       420
                   ....*....|....*....|...
gi 768021416   686 ESvkkkdgeekgkqEAQDKLGRL 708
Cdd:pfam12128  823 IS------------ELQQQLARL 833
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
344-685 3.34e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.95  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   344 KKLPVTFED-----KKRENFERGNLELEK--------RRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELE 410
Cdd:pfam15905   17 LKGPVSFEKsqrfrKQKAAESQPNLNNSKdastpataRKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   411 KQLEKQRELERQREEERRKEIERREAAKRELERQRQlewERNRRQELLnqRNKEQEDIVvlKAKKKTLEFELEALndkKH 490
Cdd:pfam15905   97 QALEEELEKVEAKLNAAVREKTSLSASVASLEKQLL---ELTRVNELL--KAKFSEDGT--QKKMSSLSMELMKL---RN 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   491 QLEGKLQDIRCRLTTQRQEIESTNKSRELRIAEIThlqqqlqesqQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKR 570
Cdd:pfam15905  167 KLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVA----------QLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   571 ALEAKELARQHLRDQLDEveketrsKLQEIDIFNNQLKElreihNKQQLQKQksmeaerlkQKEQERKIIELEKQKEEAQ 650
Cdd:pfam15905  237 QVEKYKLDIAQLEELLKE-------KNDEIESLKQSLEE-----KEQELSKQ---------IKDLNEKCKLLESEKEELL 295
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 768021416   651 RRAQERDKQWLEHVqQEDEHQRPRKLHEEEKLKRE 685
Cdd:pfam15905  296 REYEEKEQTLNAEL-EELKEKLTLEEQEHQKLQQK 329
SH3_SKAP2 cd12045
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 2; SKAP2, also called ...
744-795 3.44e-03

Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 2; SKAP2, also called SKAP55-Related (SKAP55R) or SKAP55 homolog (SKAP-HOM or SKAP55-HOM), is an immune cell-specific adaptor protein that plays an important role in adhesion and migration of B-cells and macrophages. Binding partners include ADAP (adhesion and degranulation-promoting adaptor protein), YopH, SHPS1, and HPK1. SKAP2 has also been identified as a substrate for lymphoid-specific tyrosine phosphatase (Lyp), which has been implicated in a wide variety of autoimmune diseases. It contains a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. Like SKAP1, SKAP2 is expected to bind primarily to a proline-rich region of ADAP through its SH3 domain; its degradation may be regulated by ADAP. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212978  Cd Length: 53  Bit Score: 36.42  E-value: 3.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd12045     1 FYQGLWDCTGDQPDELSFKRGDTIYILSKEYNRFGWWVGEMKGTIGLVPKAY 52
SH3_SH3RF2_3 cd11784
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ...
745-795 3.60e-03

Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212718  Cd Length: 55  Bit Score: 36.68  E-value: 3.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVdesqTG--EPGWLGGE--LKGKTGWFPANY 795
Cdd:cd11784     2 CVALHSYSAHRPEELELQKGEGVRV----LGkfQEGWLRGLslVTGRVGIFPSNY 52
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
462-686 3.72e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 41.36  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  462 NKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQdircRLTTQRQEIESTNKSRELRIAEIthlqqqlqesqqmlgrl 541
Cdd:PTZ00440 1148 NMNLEDITLNEVNEIEIEYERILIDHIVEQINNEAK----KSKTIMEEIESYKKDIDQVKKNM----------------- 1206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  542 IPEKQILNDQLK--QVQQNSLHRDS----LVTLKRALEAKELARQHLrDQLDEVEKETRSKLQEIDIFNNQLKE-LREIH 614
Cdd:PTZ00440 1207 SKERNDHLTTFEynAYYDKATASYEnieeLTTEAKGLKGEANRSTNV-DELKEIKLQVFSYLQQVIKENNKMENaLHEIK 1285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  615 NKQQL---------------QKQKSMEAERLKQKEQErKIIELEKQKEEAQRRAQERDKQW---LEHVQQEDEHQRPRKL 676
Cdd:PTZ00440 1286 NMYEFlisidsekilkeilnSTKKAEEFSNDAKKELE-KTDNLIKQVEAKIEQAKEHKNKIygsLEDKQIDDEIKKIEQI 1364
                         250
                  ....*....|
gi 768021416  677 HEEEKLKREE 686
Cdd:PTZ00440 1365 KEEISNKRKE 1374
SH3_Abp1_fungi_C1 cd11962
First C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ...
748-797 3.98e-03

First C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212895 [Multi-domain]  Cd Length: 54  Bit Score: 36.31  E-value: 3.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  748 LYPFESRSHDEITIQPGDIVMvDESQTGEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11962     5 LYDYEKDEDNEIELVEGEIVT-NIEMVDEDWWMGTNSKGESGLFPSNYVE 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
409-655 4.07e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  409 LEKQLEKQRElerqreEERRKEIERREAAKRELERQRQlewernrrqeLLNQRNKEQEDIVVLKAKKKTLEFELEALNDK 488
Cdd:COG4717    47 LLERLEKEAD------ELFKPQGRKPELNLKELKELEE----------ELKEAEEKEEEYAELQEELEELEEELEELEAE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  489 KHQLEGKLQDIRCRLTTQRQEIESTNKSRELriaeithlqqqlqesqqmlgrlipekQILNDQLKQVQQnslHRDSLVTL 568
Cdd:COG4717   111 LEELREELEKLEKLLQLLPLYQELEALEAEL--------------------------AELPERLEELEE---RLEELREL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  569 KRALEAKELARQHLRDQLDEVEKETR-SKLQEIDIFNNQLKELREihNKQQLQKQKSMEAERLKQKEQERKIIELEKQKE 647
Cdd:COG4717   162 EEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEELEQLENELEAA 239

                  ....*...
gi 768021416  648 EAQRRAQE 655
Cdd:COG4717   240 ALEERLKE 247
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
336-513 4.15e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.60  E-value: 4.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   336 EDEQQQLEKKLPvtfEDKKRENFERgnlELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEK 415
Cdd:TIGR02794   63 AKKEQERQKKLE---QQAEEAEKQR---AAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   416 QRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRN--KEQEDIVVLKAKKKTLEFELEALNDKKHQLE 493
Cdd:TIGR02794  137 EAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAeaEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAE 216
                          170       180
                   ....*....|....*....|
gi 768021416   494 GKLQDircRLTTQRQEIEST 513
Cdd:TIGR02794  217 AAAAA---AAEAERKADEAE 233
SH3_CAS cd11844
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ...
746-794 4.19e-03

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212778  Cd Length: 56  Bit Score: 36.56  E-value: 4.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQT-GEPGWLGGELKGKTGWFPAN 794
Cdd:cd11844     3 RALYDNVAESPDELAFRRGDILTVLEQNTaGLEGWWLCSLRGRQGIAPGN 52
SH3_Sorbs2_3 cd11917
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), ...
745-799 4.44e-03

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212850 [Multi-domain]  Cd Length: 61  Bit Score: 36.51  E-value: 4.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIvmVDESQTGEPGWLGGELKGKT--GWFPANYAEKI 799
Cdd:cd11917     7 FQALYNYMPRNEDELELREGDV--IDVMEKCDDGWFVGTSRRTKffGTFPGNYVKRL 61
SH3_Src cd12008
Src homology 3 domain of Src Protein Tyrosine Kinase; Src (or c-Src) is a cytoplasmic (or ...
745-795 4.48e-03

Src homology 3 domain of Src Protein Tyrosine Kinase; Src (or c-Src) is a cytoplasmic (or non-receptor) PTK and is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212941 [Multi-domain]  Cd Length: 56  Bit Score: 36.24  E-value: 4.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDESQTGEpGWLGGELK-GKTGWFPANY 795
Cdd:cd12008     2 FVALYDYESRTETDLSFKKGERLQIVNNTEGD-WWLAHSLTtGQTGYIPSNY 52
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
335-415 4.63e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 38.71  E-value: 4.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLpvtfeDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLE 414
Cdd:pfam03938   24 LEKKFKKRQAEL-----EAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQD 98

                   .
gi 768021416   415 K 415
Cdd:pfam03938   99 K 99
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
616-686 4.68e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  616 KQQLQKQKSMEAERLK--QKEQERKI-----IELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPR-------KLHEEEK 681
Cdd:cd16269   191 QALTEKEKEIEAERAKaeAAEQERKLleeqqRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEqeralesKLKEQEA 270

                  ....*
gi 768021416  682 LKREE 686
Cdd:cd16269   271 LLEEG 275
SH3_SKAP1-like cd11866
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This ...
744-795 4.73e-03

Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This subfamily is composed of SKAP1, SKAP2, and similar proteins. SKAP1 and SKAP2 are immune cell-specific adaptor proteins that play roles in T- and B-cell adhesion, respectively, and are thus important in the migration of T- and B-cells to sites of inflammation and for movement during T-cell conjugation with antigen-presenting cells. Both SKAP1 and SKAP2 bind to ADAP (adhesion and degranulation-promoting adaptor protein), among many other binding partners. They contain a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212800  Cd Length: 53  Bit Score: 36.26  E-value: 4.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd11866     1 WYMGLWDCSGNEPDELSFKRGDLIYIISKEYDSFGWWVGELNGKVGLVPKDY 52
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
370-500 4.76e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  370 QALLEQQRKEQErlaqlERAEQERKERERQEQERKRQlELEKQLEKQRelerqreeerrkeierreaaKRELERQRQLE- 448
Cdd:cd16269   191 QALTEKEKEIEA-----ERAKAEAAEQERKLLEEQQR-ELEQKLEDQE--------------------RSYEEHLRQLKe 244
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768021416  449 -WERNRRQELlnqrnKEQEDIVVLKAKKKTLEFElEALNDKKHQLEGKLQDIR 500
Cdd:cd16269   245 kMEEERENLL-----KEQERALESKLKEQEALLE-EGFKEQAELLQEEIRSLK 291
SH3_SKAP1 cd12044
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1; SKAP1, also called SKAP55 ...
744-795 4.76e-03

Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1; SKAP1, also called SKAP55 (Src kinase-associated protein of 55kDa), is an immune cell-specific adaptor protein that plays an important role in T-cell adhesion, migration, and integrin clustering. It is expressed exclusively in T-lymphocytes, mast cells, and macrophages. Binding partners include ADAP (adhesion and degranulation-promoting adaptor protein), Fyn, Riam, RapL, and RasGRP. It contains a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212977  Cd Length: 53  Bit Score: 36.37  E-value: 4.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTGEPGWLGGELKGKTGWFPANY 795
Cdd:cd12044     1 YYQGLWDCFGDNPDELSFQRGDLIYILSKEYNMYGWWVGELNGIVGIVPKDY 52
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-504 5.00e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  295 LPPVLPPEYIPPSFRRVRSGSGISVISSTSVDQRLPEEpvLEDEQQQLEKKLPVTFEDKKRENFERGN--LELEKRRQAL 372
Cdd:COG4717   330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEeyQELKEELEEL 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  373 LEQ-QRKEQERLAQLERAEQERKERERQEQERKRQlELEKQLEKQRELERQREeerrkeierreAAKRELERQRQLEWER 451
Cdd:COG4717   408 EEQlEELLGELEELLEALDEEELEEELEELEEELE-ELEEELEELREELAELE-----------AELEQLEEDGELAELL 475
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  452 NRRQELLNQRNKEQEDIVVLKAKKKTLEFELEAL-NDKKHQLEGKLQDIRCRLT 504
Cdd:COG4717   476 QELEELKAELRELAEEWAALKLALELLEEAREEYrEERLPPVLERASEYFSRLT 529
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
356-740 5.02e-03

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 40.66  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  356 ENFERGNLELEKRRQAL---LEQQRKEQERLAQLERAEQERKE------RERQEQERKRQLELEKQLEKQRELERQREEE 426
Cdd:COG5278    79 EPYEEARAEIDELLAELrslTADNPEQQARLDELEALIDQWLAeleqviALRRAGGLEAALALVRSGEGKALMDEIRARL 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  427 RRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRcRLTTQ 506
Cdd:COG5278   159 LLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAAL-ELLAA 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  507 RQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQHLRDQL 586
Cdd:COG5278   238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  587 DEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEEAQRRAQERDKQWLEHVQQ 666
Cdd:COG5278   318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416  667 EDEHQRPRKLHEEEKLKREESVKKKDGEEKGKQEAQDKLGRLFHQHQEPAKPAVQAPWSTAEKGPLTISAQENV 740
Cdd:COG5278   398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
ClassIIa_HDAC9_Gln-rich-N cd10163
Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This ...
326-407 5.08e-03

Glutamine-rich N-terminal helical domain of HDAC9, a Class IIa histone deacetylase; This family consists of the glutamine-rich domain of histone deacetylase 9 (HDAC9). It belongs to a superfamily that consists of the glutamine-rich N-terminal helical extension to certain Class IIa histone deacetylases (HDACs), including HDAC4, HDAC5 and HDCA9; it is missing from HDAC7. This domain confers responsiveness to calcium signals and mediates interactions with transcription factors and cofactors, and it is able to repress transcription independently of the HDAC C-terminal, zinc-dependent catalytic domain. It has many intra- and inter-helical interactions which are possibly involved in reversible assembly and disassembly of proteins. HDACs regulate diverse cellular processes through enzymatic deacetylation of histone as well as non-histone proteins, in particular deacetylating N(6)-acetyl-lysine residues.


Pssm-ID: 197399 [Multi-domain]  Cd Length: 90  Bit Score: 37.43  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  326 DQRLPEEPVLEDEQQQLEKKLPVTFEDKKRENFER---GNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQE 402
Cdd:cd10163     6 EKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRqhqAQLQEHLKLQQELLAMKQQQELLEKEQKLEQQRQEQELERHR 85

                  ....*
gi 768021416  403 RKRQL 407
Cdd:cd10163    86 REQQL 90
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
371-635 5.10e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.96  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   371 ALLEQQRKEQERLAQLERAEQERKERERQE---QERKRQLELEKQL-----EKQRELERQREEERRKEIERREAAKRElE 442
Cdd:pfam10174  439 TTLEEALSEKERIIERLKEQREREDRERLEeleSLKKENKDLKEKVsalqpELTEKESSLIDLKEHASSLASSGLKKD-S 517
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   443 RQRQLEWERNRRQE----LLNQRNKEQEDIVVLKAKK------KTLEFELEALNDKKHQLEGKLQdircRLTTQRQEIES 512
Cdd:pfam10174  518 KLKSLEIAVEQKKEecskLENQLKKAHNAEEAVRTNPeindriRLLEQEVARYKEESGKAQAEVE----RLLGILREVEN 593
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   513 TNKSRELRIAEIthlqqqlqesQQMLGRLIPEKQILNDQLKQVQQnSLHRDSLVTLKRALEAKE-LARQHLRDQLDEVEK 591
Cdd:pfam10174  594 EKNDKDKKIAEL----------ESLTLRQMKEQNKKVANIKHGQQ-EMKKKGAQLLEEARRREDnLADNSQQLQLEELMG 662
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 768021416   592 ETRSKLQEIDIFNNQLKEL------REIH-NKQQLQKQKSMEaERLKQKEQ 635
Cdd:pfam10174  663 ALEKTRQELDATKARLSSTqqslaeKDGHlTNLRAERRKQLE-EILEMKQE 712
SH3_PI3K_p85beta cd11909
Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol ...
745-799 5.17e-03

Src Homology 3 domain of the p85beta regulatory subunit of Class IA Phosphatidylinositol 3-kinases; Class I PI3Ks convert PtdIns(4,5)P2 to the critical second messenger PtdIns(3,4,5)P3. They are heterodimers and exist in multiple isoforms consisting of one catalytic subunit (out of four isoforms) and one of several regulatory subunits. Class IA PI3Ks associate with the p85 regulatory subunit family, which contains SH3, RhoGAP, and SH2 domains. The p85 subunits recruit the PI3K p110 catalytic subunit to the membrane, where p110 phosphorylates inositol lipids. Vertebrates harbor two p85 isoforms, called alpha and beta. In addition to regulating the p110 subunit, p85beta binds CD28 and may be involved in the activation and differentiation of antigen-stimulated T cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212842  Cd Length: 74  Bit Score: 36.73  E-value: 5.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMV-------------DESQTGEPGWLGG--ELKGKTGWFPANYAEKI 799
Cdd:cd11909     3 YRALYPYRKEREEDIDLLPGDVLTVsraalqalgvkegGEQCPQSIGWILGlnERTKQRGDFPGTYVEFL 72
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
352-679 5.29e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  352 DKKRENFErgnlELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEerrkei 431
Cdd:PRK02224  471 EEDRERVE----ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE------ 540
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  432 eRREAAKRELERQRQlEWeRNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNdkkhqlegKLQDIRCRLTTQRQEIE 511
Cdd:PRK02224  541 -ELRERAAELEAEAE-EK-REAAAEAEEEAEEAREEVAELNSKLAELKERIESLE--------RIRTLLAAIADAEDEIE 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  512 STNKSRElriaeithlqqqlqesqqmlgrlipEKQILNDQLKQvqqnslhrdslvtlkrALEAKELARQHLRDQLDEvek 591
Cdd:PRK02224  610 RLREKRE-------------------------ALAELNDERRE----------------RLAEKRERKRELEAEFDE--- 645
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  592 etrsklqeidifnNQLKELREihNKQQLQKQKSMEAERLKQKEQERKiiELEKQ----KEEAQRRAQERDkqwlEHVQQE 667
Cdd:PRK02224  646 -------------ARIEEARE--DKERAEEYLEQVEEKLDELREERD--DLQAEigavENELEELEELRE----RREALE 704
                         330
                  ....*....|..
gi 768021416  668 DEHQRPRKLHEE 679
Cdd:PRK02224  705 NRVEALEALYDE 716
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
343-412 5.38e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 39.25  E-value: 5.38e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021416   343 EKKLPVTFEDKKRENFERGNLELE---KRRQALLEQQRKEQERLAQLERAEQERKERErQEQERKRQLELEKQ 412
Cdd:pfam09756   16 AKRQQREAEEEEREEREKLEEKREeeyKEREEREEEAEKEKEEEERKQEEEQERKEQE-EYEKLKSQFVVEEE 87
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
585-681 5.49e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 38.62  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   585 QLDEVEKETRSKLQEIDIFNNQLKELREIH--NKQQLQKQKSMEAERL-KQKEQERKIIELE----KQKEEAQRRAQERD 657
Cdd:pfam15236   43 QLEERERKRQKALEHQNAIKKQLEEKERQKklEEERRRQEEQEEEERLrREREEEQKQFEEErrkqKEKEEAMTRKTQAL 122
                           90       100
                   ....*....|....*....|....*.
gi 768021416   658 KQWLEHVQQ--EDEHQRPRKLHEEEK 681
Cdd:pfam15236  123 LQAMQKAQElaQRLKQEQRIRELAEK 148
SH3_SPIN90 cd11849
Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also ...
745-797 5.49e-03

Src homology 3 domain of SH3 protein interacting with Nck, 90 kDa (SPIN90); SPIN90 is also called NCK interacting protein with SH3 domain (NCKIPSD), Dia-interacting protein (DIP), 54 kDa vimentin-interacting protein (VIP54), or WASP-interacting SH3-domain protein (WISH). It is an F-actin binding protein that regulates actin polymerization and endocytosis. It associates with the Arp2/3 complex near actin filaments and determines filament localization at the leading edge of lamellipodia. SPIN90 is expressed in the early stages of neuronal differentiation and plays a role in regulating growth cone dynamics and neurite outgrowth. It also interacts with IRSp53 and regulates cell motility by playing a role in the formation of membrane protrusions. SPIN90 contains an N-terminal SH3 domain, a proline-rich domain, and a C-terminal VCA (verprolin-homology and cofilin-like acidic) domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212783 [Multi-domain]  Cd Length: 53  Bit Score: 36.14  E-value: 5.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDI-VMVDESQtgEPGWLGGELKGKTGWFPANYAE 797
Cdd:cd11849     2 YRALYDFKSAEPNTLSFSEGETfLLLERSN--AHWWLVTNHSGETGYVPANYVK 53
SH3_SH3RF1_1 cd11927
First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ...
746-797 5.52e-03

First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ubiquitin-protein ligase; SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212860  Cd Length: 54  Bit Score: 36.08  E-value: 5.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021416  746 RALYPFESRSHDEITIQPGDIVM----VDESqtgepgWLGGELKGKTGWFPANYAE 797
Cdd:cd11927     4 KALYNYEGKEPGDLKFSKGDIIIlrrqVDEN------WYHGEVNGIHGFFPTNFVQ 53
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
353-496 5.94e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.12  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   353 KKRENFERGNLELEKRRQALLeqqrKEQERLAQLERAEQERKERERQEQERKRQlELEKQLEKQRElerqreeerrkeie 432
Cdd:pfam15619   78 RLQEKERDLERKLKEKEAELL----RLRDQLKRLEKLSEDKNLAEREELQKKLE-QLEAKLEDKDE-------------- 138
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021416   433 rreaAKRELERQRQLEwERNRRQELLNQRNKEQEdivvLKAKKKTLEFELEALNDKKHQLEGKL 496
Cdd:pfam15619  139 ----KIQDLERKLELE-NKSFRRQLAAEKKKHKE----AQEEVKILQEEIERLQQKLKEKEREL 193
PRK00106 PRK00106
ribonuclease Y;
558-652 6.06e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 6.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  558 NSLHRDSLVTLKRAL-EAKELARQHLrdqlDEVEKETRSKLQEIDIFNNQLKEL--------REIHNKQQL--QKQKSME 626
Cdd:PRK00106   60 KTAKRESKALKKELLlEAKEEARKYR----EEIEQEFKSERQELKQIESRLTERatsldrkdENLSSKEKTleSKEQSLT 135
                          90       100
                  ....*....|....*....|....*.
gi 768021416  627 AERLKQKEQERKIIELEKQKEEAQRR 652
Cdd:PRK00106  136 DKSKHIDEREEQVEKLEEQKKAELER 161
SH3_Eve1_2 cd11815
Second Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
748-795 6.24e-03

Second Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212749 [Multi-domain]  Cd Length: 52  Bit Score: 36.00  E-value: 6.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 768021416  748 LYPFESRSHDEITIQPGDIVMVDESQTGEpgWLGGELKGKTGWFPANY 795
Cdd:cd11815     5 LHDFPAEHSDDLSLNSGEIVYLLEKIDTE--WYRGKCKNTTGIFPANH 50
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
569-675 6.31e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.37  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   569 KRALEAKELARQHLRDQ--LDEVEKETRSKLQEIdifNNQLKELR--EIHNKQQLQKQKSMEAERlKQKEQERKIIELEK 644
Cdd:pfam05262  224 KKQIDADKAQQKADFAQdnADKQRDEVRQKQQEA---KNLPKPADtsSPKEDKQVAENQKREIEK-AQIEIKKNDEEALK 299
                           90       100       110
                   ....*....|....*....|....*....|..
gi 768021416   645 QKEE-AQRRAQERDKQWLEHVQQEDEHQRPRK 675
Cdd:pfam05262  300 AKDHkAFDLKQESKASEKEAEDKELEAQKKRE 331
SH3_JIP1_like cd11801
Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; ...
745-796 6.34e-03

Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; JNK-interacting proteins (JIPs) function as scaffolding proteins for c-Jun N-terminal kinase (JNK) signaling pathways. They bind to components of Mitogen-activated protein kinase (MAPK) pathways such as JNK, MKK, and several MAP3Ks such as MLK and DLK. There are four JIPs (JIP1-4); all contain a JNK binding domain. JIP1 and JIP2 also contain SH3 and Phosphotyrosine-binding (PTB) domains. Both are highly expressed in the brain and pancreatic beta-cells. JIP1 functions as an adaptor linking motor to cargo during axonal transport and also is involved in regulating insulin secretion. JIP2 form complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. The SH3 domain of JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212735  Cd Length: 55  Bit Score: 35.75  E-value: 6.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021416  745 YRALYPFESRSHDEITIQPGDIVMVDesQTGEPGWLGG-ELK-GKTGWFPANYA 796
Cdd:cd11801     2 HRALHKFIPRHEDEIELDIGDPVYVE--QEADDLWCEGtNLRtGQRGIFPAAYV 53
PRK12704 PRK12704
phosphodiesterase; Provisional
472-655 6.44e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  472 KAKKKTLEFELEALNDKKHQ-LEGKLQDIRcrlttQRQEIESTNKSRElriAEITHLQQqlqesqqmlgRLIPEKQILND 550
Cdd:PRK12704   39 EAKRILEEAKKEAEAIKKEAlLEAKEEIHK-----LRNEFEKELRERR---NELQKLEK----------RLLQKEENLDR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  551 QLKQVQQNslhRDSLVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEI------DIFNNQLKELREihnkqQLQKQKs 624
Cdd:PRK12704  101 KLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeEAKEILLEKVEE-----EARHEA- 171
                         170       180       190
                  ....*....|....*....|....*....|.
gi 768021416  625 meAERLKQKEqerkiielEKQKEEAQRRAQE 655
Cdd:PRK12704  172 --AVLIKEIE--------EEAKEEADKKAKE 192
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
565-668 6.47e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  565 LVTLKRALEAKELARQHLRDQLDEVEKETRSKLQEidifnnQLKELRE----IHNKQQLQKQKSMEAERLKQK--EQERK 638
Cdd:COG0542   413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRD------ELAELEEeleaLKARWEAEKELIEEIQELKEEleQRYGK 486
                          90       100       110
                  ....*....|....*....|....*....|
gi 768021416  639 IIELEKQKEEAQRRAQERDKQWLEHVQQED 668
Cdd:COG0542   487 IPELEKELAELEEELAELAPLLREEVTEED 516
SH3_DOCK1_5_A cd12051
Src Homology 3 domain of Class A Dedicator of Cytokinesis proteins 1 and 5; Dock1, also called ...
744-795 6.55e-03

Src Homology 3 domain of Class A Dedicator of Cytokinesis proteins 1 and 5; Dock1, also called Dock180, and Dock5 are class A DOCKs and are atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. Dock1 interacts with the scaffold protein Elmo and the resulting complex functions upstream of Rac in many biological events including phagocytosis of apoptotic cells, cell migration and invasion. Dock5 functions upstream of Rac1 to regulate osteoclast function. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). The DHR-1 domain binds phosphatidylinositol-3,4,5-triphosphate while DHR-2 contains the catalytic activity for Rac and/or Cdc42. Class A DOCKs also contain an SH3 domain at the N-terminal region and a PxxP motif at the C-terminus; they are specific GEFs for Rac. The SH3 domain of Dock1 binds to DHR-2 in an autoinhibitory manner; binding of Elmo to the SH3 domain of Dock1 exposes the DHR-2 domain and promotes GEF activity. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212984 [Multi-domain]  Cd Length: 56  Bit Score: 35.95  E-value: 6.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768021416  744 YYRALYPFESRSHDEITIQPGDIVMVDESQTgepGWLGG---ELKGKTGWFPANY 795
Cdd:cd12051     1 YGVAIYNYDARGPDELSLQIGDTVHILETYE---GWYRGytlRKKSKKGIFPASY 52
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
334-641 6.60e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 6.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   334 VLEDEQQQLEKKLPVTFEDKKRENFERGNLE------------LEKRRQALlEQQRKEQERLAQLERAEQERKERE--RQ 399
Cdd:TIGR04523  416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdsvkeliiknLDNTRESL-ETQLKVLSRSINKIKQNLEQKQKElkSK 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   400 EQERKRQLELEKQLEKQRELERQREEERRKEIERREAAKRELERQ-RQLEWE------RNRRQELLNQRNKEQEDIVVLK 472
Cdd:TIGR04523  495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKiSDLEDElnkddfELKKENLEKEIDEKNKEIEELK 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   473 AKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTqrQEIESTNKSRELRIAEITHLQQQLQESqqmlgRLIPEKQILNDQL 552
Cdd:TIGR04523  575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE--KEKKISSLEKELEKAKKENEKLSSIIK-----NIKSKKNKLKQEV 647
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   553 KQVQQnslhrdslvTLKRALEAKelarqhlrDQLDEVEKETRSKLQE-IDIFNNQLKELREIHNKQQLQKQKSMEAERLK 631
Cdd:TIGR04523  648 KQIKE---------TIKEIRNKW--------PEIIKKIKESKTKIDDiIELMKDWLKELSLHYKKYITRMIRIKDLPKLE 710
                          330
                   ....*....|....
gi 768021416   632 QK----EQERKIIE 641
Cdd:TIGR04523  711 EKykeiEKELKKLD 724
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
351-468 6.80e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.48  E-value: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   351 EDKKRENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERqrEEERRKE 430
Cdd:pfam05672   31 EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQK--QKEEAEA 108
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 768021416   431 IERREAAKRELERQRQLEWERNRRQEllnqRNKEQEDI 468
Cdd:pfam05672  109 KAREEAERQRQEREKIMQQEEQERLE----RKKRIEEI 142
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
373-482 6.90e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  373 LEQQRKEQErlAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERREAAK--RELERQRQLEWE 450
Cdd:PRK00409  525 LEELERELE--QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiiKELRQLQKGGYA 602
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 768021416  451 RNRRQEL------LNQRNKEQEDIVVlKAKKKTLEFEL 482
Cdd:PRK00409  603 SVKAHELiearkrLNKANEKKEKKKK-KQKEKQEELKV 639
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
363-493 7.20e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  363 LELEKRRQALLEQQRKEQERlaQLERAEQERKERERQEQERKRQLEleKQLEKqrelerqreeerrkeierreaakrelE 442
Cdd:cd16269   200 IEAERAKAEAAEQERKLLEE--QQRELEQKLEDQERSYEEHLRQLK--EKMEE--------------------------E 249
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768021416  443 RQRQLEwernRRQELLNQRNKEQEdivvlKAKKKTLEFELEALNDKKHQLE 493
Cdd:cd16269   250 RENLLK----EQERALESKLKEQE-----ALLEEGFKEQAELLQEEIRSLK 291
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
335-686 7.39e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLPVtfEDKKRENFERgnlELEKRRQALLEQQRKEQERLAQLERAEQERKERERqEQERKRQlelekqle 414
Cdd:pfam01576  494 LEDERNSLQEQLEE--EEEAKRNVER---QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR-ELEALTQ-------- 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   415 kqrelerqReeerrkeIERREAAKRELERQrqleweRNRRQEllnqrnkEQEDIVVLKAKKKTLEFELEALNDKKHQLEG 494
Cdd:pfam01576  560 --------Q-------LEEKAAAYDKLEKT------KNRLQQ-------ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   495 KLQDIRCRLTTQRQEIESTNKSRELRIAEITHLqqqlqesqqmlgrLIPEKQILNDQLKQVQQNSLHRDSLVT------- 567
Cdd:pfam01576  612 EEKAISARYAEERDRAEAEAREKETRALSLARA-------------LEEALEAKEELERTNKQLRAEMEDLVSskddvgk 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   568 ----LKRALEAKELARQHLRDQLDEVEKETR----SKLQ-EIDIFNNQLKELREIHN--------KQQLQKQ-KSMEAER 629
Cdd:pfam01576  679 nvheLERSKRALEQQVEEMKTQLEELEDELQatedAKLRlEVNMQALKAQFERDLQArdeqgeekRRQLVKQvRELEAEL 758
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021416   630 LKQKEQ-----------ERKIIELEKQKEEAQRRAQERDKQWLEHVQQEDEHQRPRklhEEEKLKREE 686
Cdd:pfam01576  759 EDERKQraqavaakkklELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQREL---EEARASRDE 823
iSH2_PI3K_IA_R cd12923
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
352-468 7.51e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.


Pssm-ID: 214016 [Multi-domain]  Cd Length: 152  Bit Score: 37.97  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  352 DKKRENFERGNLELEKRRQALleQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEI 431
Cdd:cd12923    25 DELYEKYNKLSQEIQLKRQAL--EAFEEAVKMFEEQLRTQEKFQKEAQPHEKQRLMENNELLKSRLKELEESKEQLEEDL 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 768021416  432 ERREAAKRELERQR--------QLEWERNRRQELLNQRNKEQEDI 468
Cdd:cd12923   103 RKQVAYNRELEREMnslkpelmQLRKQKDQYLRWLKRKGVSQEEI 147
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
335-657 7.73e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   335 LEDEQQQLEKKLPVTFEDKKRENFERGNLELEKRRqalLEQQRKEQERlaQLERAEQE-RKERERQEQERKRQleleKQL 413
Cdd:pfam07888   36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQ---WERQRRELES--RVAELKEElRQSREKHEELEEKY----KEL 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   414 EKQRELERQREEERRKEIERREAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVlkAKKKTLEFELEALNDKKHQLE 493
Cdd:pfam07888  107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAG--AQRKEEEAERKQLQAKLQQTE 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   494 GKLqdirCRLTTQRQEIESTNKSRELRIAEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQ--NSLHRdSLVTLKRA 571
Cdd:pfam07888  185 EEL----RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQErlNASER-KVEGLGEE 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   572 LEAKELARQHLRDQLDEVEKETRSKLQEIDIFNNQLKELREIHNKQQLQKQKSMEAERLKQKEQERKIIELEK--QKEEA 649
Cdd:pfam07888  260 LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEErlQEERM 339
                          330
                   ....*....|....
gi 768021416   650 QRR------AQERD 657
Cdd:pfam07888  340 EREklevelGREKD 353
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
490-682 7.76e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.21  E-value: 7.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   490 HQLEGKLQDIRCRLTTQRQEIEsTNKSRELRI--------AEITHLQQQLQESQQMLGRLIPEKQILNDQLKQVQQNSlh 561
Cdd:pfam12128  230 IQAIAGIMKIRPEFTKLQQEFN-TLESAELRLshlhfgykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDEL-- 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   562 RDSLVTLKRALEAKE-----LARQHLRDQLDEVEKeTRSKLQEIDIFNNQLKELREIHnKQQLQKQKSMEAE----RLKQ 632
Cdd:pfam12128  307 NGELSAADAAVAKDRseleaLEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERL-KALTGKHQDVTAKynrrRSKI 384
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 768021416   633 KEQERKIIELEKQKEEAQRRAQER-------DKQWLEHVQQEDEHQRPRKLHEEEKL 682
Cdd:pfam12128  385 KEQNNRDIAGIKDKLAKIREARDRqlavaedDLQALESELREQLEAGKLEFNEEEYR 441
SH3_CIP4-like cd11911
Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of ...
746-779 7.76e-03

Src Homology 3 domain of Cdc42-Interacting Protein 4; This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. It functions downstream of Cdc42 in PDGF-dependent actin reorganization and cell migration, and also regulates the activity of PDGFRbeta. It uses Src as a substrate in regulating the invasiveness of breast tumor cells. CIP4 may also play a role in the pathogenesis of Huntington's disease. Members of this subfamily typically contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. The SH3 domain of CIP4 associates with Gapex-5, a Rab31 GEF. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212844 [Multi-domain]  Cd Length: 55  Bit Score: 35.70  E-value: 7.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTGEpGW 779
Cdd:cd11911     3 TALYDFDGTSEGTLSMEEGEILLVLEEDGGD-GW 35
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
364-708 7.80e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.20  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  364 ELEKRRQALLEQQRKEQERLAQLEraEQERKERERQEQERKRQLELEKQLEKQrelerqreeerrkeIERREAAKRELER 443
Cdd:PRK04778  109 EIESLLDLIEEDIEQILEELQELL--ESEEKNREEVEQLKDLYRELRKSLLAN--------------RFSFGPALDELEK 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  444 Q-RQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLefELEALNDKKHQLEGKLQDIrcrLTTQRQEIESTnkSRELRIA 522
Cdd:PRK04778  173 QlENLEEEFSQFVELTESGDYVEAREILDQLEEELA--ALEQIMEEIPELLKELQTE---LPDQLQELKAG--YRELVEE 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  523 eithlqqqlqesqqmlGRLIPEKQI------LNDQLKQVQQNslhrdsLVTLKraLEAKELARQHLRDQLDE----VEKE 592
Cdd:PRK04778  246 ----------------GYHLDHLDIekeiqdLKEQIDENLAL------LEELD--LDEAEEKNEEIQERIDQlydiLERE 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  593 TRSK---LQEIDIFNNQLKELREihNKQQLQkqksMEAERLKQ------------KEQERKIIELEKQKEEAQRR----- 652
Cdd:PRK04778  302 VKARkyvEKNSDTLPDFLEHAKE--QNKELK----EEIDRVKQsytlneselesvRQLEKQLESLEKQYDEITERiaeqe 375
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021416  653 -----AQERDKQWLEHVQQ-EDEHQrprKLHEE-EKLKREEsvkkkdgeekgkQEAQDKLGRL 708
Cdd:PRK04778  376 iayseLQEELEEILKQLEEiEKEQE---KLSEMlQGLRKDE------------LEAREKLERY 423
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
355-599 8.22e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  355 RENFERGNLELEKRRQALLEQQRKEQERLAQLERAEQERKERERQEQERKRQLELEKQLEKQRELERQREEERRKEIERR 434
Cdd:COG1196   629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  435 EAAKRELERQRQLEWERNRRQELLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKhQLEGKLQdircRLTTQRQEIESTN 514
Cdd:COG1196   709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERELE----RLEREIEALGPVN 783
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  515 ksreLRiAEithlqqqlqesqqmlgrlipekqilnDQLKQVQQnslhR-DSLVTlKRA-LEAkelARQHLRDQLDEVEKE 592
Cdd:COG1196   784 ----LL-AI--------------------------EEYEELEE----RyDFLSE-QREdLEE---ARETLEEAIEEIDRE 824

                  ....*..
gi 768021416  593 TRSKLQE 599
Cdd:COG1196   825 TRERFLE 831
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
364-659 8.35e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 40.19  E-value: 8.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   364 ELEKRRQALLEQQRKE----QERLAQLE-RAEQERKERERQEQERKRQLELeKQLEKQRELERQREEERRKEIERREAAK 438
Cdd:pfam10174  116 ENFRRLQSEHERQAKElfllRKTLEEMElRIETQKQTLGARDESIKKLLEM-LQSKGLPKKSGEEDWERTRRIAEAEMQL 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   439 RELERQ-RQLEWERNRRQELLNQRNKEQEDivvlKAKKKTLEFELEALNDKKHQLEGKLQDIRcrlttqrQEIESTNKSr 517
Cdd:pfam10174  195 GHLEVLlDQKEKENIHLREELHRRNQLQPD----PAKTKALQTVIEMKDTKISSLERNIRDLE-------DEVQMLKTN- 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   518 elriaeithlqqqlqesqqmlGRLIPEKQilNDQLKQVQQNSLHRDSLVT----LKRALEAKELARQHLRDQLD------ 587
Cdd:pfam10174  263 ---------------------GLLHTEDR--EEEIKQMEVYKSHSKFMKNkidqLKQELSKKESELLALQTKLEtltnqn 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416   588 -------EVEKET-------RSKLQ-EIDIFNNQLKELREIHNK-----QQLQKQKSMEAERLKQKEQ-----ERKIIEL 642
Cdd:pfam10174  320 sdckqhiEVLKESltakeqrAAILQtEVDALRLRLEEKESFLNKktkqlQDLTEEKSTLAGEIRDLKDmldvkERKINVL 399
                          330
                   ....*....|....*..
gi 768021416   643 EKQKEEAQRRAQERDKQ 659
Cdd:pfam10174  400 QKKIENLQEQLRDKDKQ 416
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
457-648 9.01e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.20  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  457 LLNQRNKEQEDIVVLKAKKKTLEFELEALNDKKHQLEGKLQDIRCRLTTQRQEIESTNKsrELRIAEITHLqqqlqesqq 536
Cdd:PTZ00440  789 ILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDE--NLNLKELEKE--------- 857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021416  537 mlgrLIPEKQILNDQLKQVQQNSLHRDSLVTLKRALEAKELARQhlrdqldEVEKETRSKLQEIDIFNNQLKELR----- 611
Cdd:PTZ00440  858 ----FNENNQIVDNIIKDIENMNKNINIIKTLNIAINRSNSNKQ-------LVEHLLNNKIDLKNKLEQHMKIINtdnii 926
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 768021416  612 EIHNKQQLQKQKSMEAERLKQKEQERKIIELEKQKEE 648
Cdd:PTZ00440  927 QKNEKLNLLNNLNKEKEKIEKQLSDTKINNLKMQIEK 963
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
746-797 9.21e-03

N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212880 [Multi-domain]  Cd Length: 52  Bit Score: 35.54  E-value: 9.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768021416  746 RALYPFESRSHDEITIQPGDIVMVDESQTgepGWLGGELKGKTGWFPANYAE 797
Cdd:cd11947     3 RGKFDFTASGEDELSFKKGDVLKILSSDD---IWFKAELNGEEGYVPKNFVD 51
 
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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