Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683885 1477 VFVALFDYDPVSMSPNPDAGEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1538
Cdd:cd12012     1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148683885 1582 MVPL--YTPQHTHPGLPPslvgprKAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLEG 1645
Cdd:cd12013     2 MVALfdYDPRESSPNVDA------EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148683885  790 PSQLRIHRLTATSAEIAWVPGNSNLAHAI-YL---------NGEECPPARPSTYWATFCNLRPGTLYQARVEA 852
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVveyrekgsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683885 1477 VFVALFDYDPVSMSPNPDAGEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1538
Cdd:cd12012     1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148683885 1582 MVPL--YTPQHTHPGLPPslvgprKAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLEG 1645
Cdd:cd12013     2 MVALfdYDPRESSPNVDA------EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  152 ETEEKVRRLKRKnAELAVIAKRLEERAQKLQetnmrvvsapvprpgssLELCRKALARQRARdLSETASALLAKDKQIAA 231
Cdd:COG1196   197 ELERQLEPLERQ-AEKAERYRELKEELKELE-----------------AELLLLKLRELEAE-LEELEAELEELEAELEE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  232 LQRECRELQARLSLVGKEgpqwlHMRDFDRLLRESQREVLRLQRQIALRNQREPLRparspgptapsravlqddvespqv 311
Cdd:COG1196   258 LEAELAELEAELEELRLE-----LEELELELEEAQAEEYELLAELARLEQDIARLE------------------------ 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  312 vLREPEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSGRATEKEQvewENSEL 391
Cdd:COG1196   309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE---ELEEL 384

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148683885  392 KGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHEQARLSLQEKQEEVRRLQQ 459
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 148683885  1598 SLVGPRKAELPFRAGDVITVFGnMDDDGFYYGELNGQRGLVPSNFLE 1644
Cdd:pfam07653    7 DYVGTDKNGLTLKKGDVVKVLG-KDNDGWWEGETGGRVGLVPSTAVE 52

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.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 148683885    571 PFEGPNENpeaELPLTAGEYIYIYgNMDEDGFFEGELMDGRRGLVPSNFVE 621
Cdd:smart00326   10 DYTAQDPD---ELSFKKGDIITVL-EKSDDGWWKGRLGRGKEGLFPSNYVE 56

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.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683885   1474 PVRVFVALFDYDPVSmspnpdagEEELPFKEGQLLKVFGDKDaDGFYRGESG-GRTGYIPCNMVA 1537
Cdd:smart00326    1 EGPQVRALYDYTAQD--------PDELSFKKGDIITVLEKSD-DGWWKGRLGrGKEGLFPSNYVE 56

DNA double-strand break repair Rad50 ATPase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  146 RKSSFPETEEKVR---RLKRKNAE-LAVIAKRLEERAQKLQETnmrvvsapvprpgsslelcrkalARQRARDLSETASA 221
Cdd:PRK02224  322 RDEELRDRLEECRvaaQAHNEEAEsLREDADDLEERAEELREE-----------------------AAELESELEEAREA 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  222 LLAKDKQIAALQRECRELQARlslVGKEGPQWLHMRDFDRLLREsQREVLRLQ---RQIALRNQREPLRPARSPGPTAPS 298
Cdd:PRK02224  379 VEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDFLEELRE-ERDELREReaeLEATLRTARERVEEAEALLEAGKC 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  299 RAVLQDDVESPQVVLREpEKQQRVQQLESELCKKRKKCESLEQ------EARKKQRRCEELE-----LQLRAAQNEnARL 367
Cdd:PRK02224  455 PECGQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEerredLEELIAERR-ETI 532

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  368 VEENSRLSGRATEKEQVEWENSE---------------------LKGQLLGVTQERDSaLLKSQGLQSKLESLEQVLKHM 426
Cdd:PRK02224  533 EEKRERAEELRERAAELEAEAEEkreaaaeaeeeaeeareevaeLNSKLAELKERIES-LERIRTLLAAIADAEDEIERL 611

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 148683885  427 REvaqRRQQLEVEHEQARLSLQEKQEEVRRLQQTTDP 463
Cdd:PRK02224  612 RE---KREALAELNDERRERLAEKRERKRELEAEFDE 645

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885 1193 LEKPGPSRTSQDPSQPELSLLGPGCDSSQPQGPGLCPLSPELSGVREHLEDVlgvVGGNGRRRGGGSPEKLPNRKRPQDP 1272
Cdd:PHA03247 2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL---TSLADPPPPPPTPEPAPHALVSATP 2720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885 1273 REHCSRLLGNGGPQASARPVPPR--ERGSLPVIEGTRVG-QEPGGRGRPGLSRRCPRGPAPESS--LVSCLSPKCLEISI 1347
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAvpAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTrpAVASLSESRESLPS 2800

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885 1348 EYDSEDEQEAGSGGVS-INSSCYPTDGEAWGTAAVgrPRGPPKVNPGPNAYLRLPAW-EKGEPERRgrsaigrtkEPPSR 1425
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAaLPPAASPAGPLPPPTSAQ--PTAPPPPPGPPPPSLPLGGSvAPGGDVRR---------RPPSR 2869

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148683885 1426 ATETGESrgqdnSGRRGPQRRGARVPRSGTTE-LAPPRSPQEAPPHQDLPVR 1476
Cdd:PHA03247 2870 SPAAKPA-----APARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPPP 2916

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148683885    790 PSQLRIHRLTATSAEIAWVPGNSNLAHAIYLN----------GEECPPARPSTYWATFCNLRPGTLYQARVEA 852
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGyrveyreegsEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683885 1477 VFVALFDYDPVSMSPNPDAGEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1538
Cdd:cd12012     1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62

Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148683885  562 VFLARYSYNPFEG-PNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVE 621
Cdd:cd11851     1 LMVALYDYNPETMsPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGGRKGLVPSNFVQ 61

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148683885 1582 MVPL--YTPQHTHPGLPPslvgprKAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLEG 1645
Cdd:cd12013     2 MVALfdYDPRESSPNVDA------EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885 1479 VALFDYDPVSMSPNPDAgEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1538
Cdd:cd12013     3 VALFDYDPRESSPNVDA-EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683885 1571 LFLTRYHsalemvplYTPQHTHPGLPPslvgprKAELPFRAGDVITVFGNMDDDGFYYGEL-NGQRGLVPSNFLE 1644
Cdd:cd12014     1 VFVARYS--------YNPLRDSPNENP------EAELPLNAGDYVYVYGDMDEDGFYEGELlDGRRGLVPSNFVE 61

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148683885 1477 VFVALFDYDPVSMSPNpDAGEEELPFKEGQLLKVFGDKDADGFYRGES-GGRTGYIPCNMV 1536
Cdd:cd12014     1 VFVARYSYNPLRDSPN-ENPEAELPLNAGDYVYVYGDMDEDGFYEGELlDGRRGLVPSNFV 60

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   189 VSAPVPRPGSSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLSLVGKEGPQwlhMRDFDRLLRESQR 268
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE---LSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   269 EVLRLQRQIALRNQREPLRPARSpgptAPSRAVLQDDVESPQVVLREPEK------------QQRVQQLESELCKKRKKC 336
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTEL----EAEIEELEERLEEAEEELAEAEAeieeleaqieqlKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   337 ESLEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSGRAT----EKEQVEWENSELKGQLLGVTQERDSALLKSQGL 412
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALL 892

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 148683885   413 QSKLESLEQVLkhmREVAQRRQQLEVEHEQARLSLQEKQEEVRRLQQT 460
Cdd:TIGR02168  893 RSELEELSEEL---RELESKRSELRRELEELREKLAQLELRLEGLEVR 937

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   126 RALGELQQRCTILKEENQMLrKSSFPETEEKVRRLKRKNAELAVIAKRLEERAQKLQETnmrvvsapvprpgssLELCRK 205
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKL-KERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---------------LHKLEE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   206 ALARQRARDLSEtasallaKDKQIAALQRECRELQARLSLVGKEGPQWLHMRDFDRLLRESQREVLrLQRQIALRNQREP 285
Cdd:TIGR02169  780 ALNDLEARLSHS-------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKS 851

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   286 LRPARspgptapsrAVLQDDVESPQVVLREpeKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRaaqnena 365
Cdd:TIGR02169  852 IEKEI---------ENLNGKKEELEEELEE--LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE------- 913

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   366 rlvEENSRLSGRATEKEQVEWENSELkGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQRRQQlEVEHEQARL 445
Cdd:TIGR02169  914 ---KKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ-EYEEVLKRL 988

                          330       340
                   ....*....|....*....|..
gi 148683885   446 -SLQEKQ----EEVRRLQQTTD 462
Cdd:TIGR02169  989 dELKEKRakleEERKAILERIE 1010

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.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148683885  1477 VFVALFDYDPvsmspnpdAGEEELPFKEGQLLKVFgDKDADGFYRGESGGRTGYIPCNMVAEV 1539
Cdd:pfam07653    1 YGRVIFDYVG--------TDKNGLTLKKGDVVKVL-GKDNDGWWEGETGGRVGLVPSTAVEEI 54

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885    47 TALQV--KGLRfEESSKPEGAHSPGPVGNTdpeatetRLPKLGQQAESpgyscsgLEEEEAQAYKAKFNIgfgdRPNLEL 124
Cdd:pfam05622   31 NSLQQenKKLQ-ERLDQLESGDDSGTPGGK-------KYLLLQKQLEQ-------LQEENFRLETARDDY----RIKCEE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   125 L-RALGELQQR----------CTILKEENQMLRKSSfpeteEKVRRLKrknAELAVIAKRLEE----RAQ--KLQETNM- 186
Cdd:pfam05622   92 LeKEVLELQHRneeltslaeeAQALKDEMDILRESS-----DKVKKLE---ATVETYKKKLEDlgdlRRQvkLLEERNAe 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   187 ---RVVS-------APVPRpgSSLELCRKALARQRARDLSETASAllakDKqiaaLQRECRELQARLSLVGKEGPQWLHM 256
Cdd:pfam05622  164 ymqRTLQleeelkkANALR--GQLETYKRQVQELHGKLSEESKKA----DK----LEFEYKKLEEKLEALQKEKERLIIE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   257 RDfdrLLRESQREVLRLQRQIALRNQREPLRPARSPGPTAPSRAVLQDDVESPQVVLREPEKQQRVQQLESElckkRKKC 336
Cdd:pfam05622  234 RD---TLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSY----RERL 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885   337 ESLEQEARKKQRRCEELELQLRAAQnenarlveensrlsgratekEQVewenSELKGQ---LLGVTQERDSALLKSQGLQ 413
Cdd:pfam05622  307 TELQQLLEDANRRKNELETQNRLAN--------------------QRI----LELQQQveeLQKALQEQGSKAEDSSLLK 362

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 148683885   414 SKLES-LEQVLKHMREVAQRRQQLEVEHEQARLSLQEKQEE 453
Cdd:pfam05622  363 QKLEEhLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDE 403

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  204 RKALARQ-----RARDLSETASALlakDKQIAALQRecRELQARLSLVGKEgpqwlhmrdfdrlLRESQREVLRLQRQIA 278
Cdd:COG1196   202 LEPLERQaekaeRYRELKEELKEL---EAELLLLKL--RELEAELEELEAE-------------LEELEAELEELEAELA 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  279 LRNQRepLRPARSpgptapSRAVLQDDVEspqvvlrepEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLR 358
Cdd:COG1196   264 ELEAE--LEELRL------ELEELELELE---------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683885  359 AAQNENARLVEENSRLSGRATEKE-----------QVEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMR 427
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEeeleeaeaelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         250       260       270
                  ....*....|....*....|....*....|....
gi 148683885  428 EVAQRRQQLEVEHEQARLSLQEKQEEVRRLQQTT 461
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEE 440