hypothetical protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126 1419 NGEAEGPDGEAAE--PIGEAGQP----NGEAEQPNGDADE-PDGAGIEDPEERAEEPEGKAEEPEGDAdePDGVGIEDPE 1491
Cdd:PHA03169  122 NTSGSSPESPASHspPPSPPSHPgphePAPPESHNPSPNQqPSSFLQPSHEDSPEEPEPPTSEPEPDS--PGPPQSETPT 199

                          90
                  ....*....|..
gi 226053126 1492 EGEDQEIQVEEP 1503
Cdd:PHA03169  200 SSPPPQSPPDEP 211

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 226053126  1163 YECPKCGESFIHSSFLFEHQRIH 1185
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126   42 SEFFHQRFRNLIYVEFVGPRKTLIKLRNLCLDWLQPETRTKEEIIELLVLEQYLTIIPEKLKPWVRAKKPENCEKLVTLL 121
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80

                  ....
gi 226053126  122 ENYK 125
Cdd:cd07936    81 EDLL 84

hypothetical protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126 1419 NGEAEGPDGEAAE--PIGEAGQP----NGEAEQPNGDADE-PDGAGIEDPEERAEEPEGKAEEPEGDAdePDGVGIEDPE 1491
Cdd:PHA03169  122 NTSGSSPESPASHspPPSPPSHPgphePAPPESHNPSPNQqPSSFLQPSHEDSPEEPEPPTSEPEPDS--PGPPQSETPT 199

                          90
                  ....*....|..
gi 226053126 1492 EGEDQEIQVEEP 1503
Cdd:PHA03169  200 SSPPPQSPPDEP 211

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 226053126   969 YECQECGECFAHSSDLTEHQKIH 991
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 226053126   627 YECKVCGETFLHSSSLKEHQKIH 649
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126   42 SEFFHQRFRNLIYVEFVGPRKTLIKLRNLCLDWLQPETRTKEEIIELLVLEQYLTIIPEKLKPWVRAKKPENCEKLVTLL 121
Cdd:cd07936     1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80

                  ....
gi 226053126  122 ENYK 125
Cdd:cd07936    81 EDLL 84

hypothetical protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126 1419 NGEAEGPDGEAAE--PIGEAGQP----NGEAEQPNGDADE-PDGAGIEDPEERAEEPEGKAEEPEGDAdePDGVGIEDPE 1491
Cdd:PHA03169  122 NTSGSSPESPASHspPPSPPSHPgphePAPPESHNPSPNQqPSSFLQPSHEDSPEEPEPPTSEPEPDS--PGPPQSETPT 199

                          90
                  ....*....|..
gi 226053126 1492 EGEDQEIQVEEP 1503
Cdd:PHA03169  200 SSPPPQSPPDEP 211

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126  1420 GEAEGPDGEAAEPIGEAGQPNGEAEQPNGDADEPDGAGIEDPEERAEEPEGKAE-----EPEGDADEPDGVGIEDPEEGE 1494
Cdd:TIGR00927  697 GEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEgkhevETEGDRKETEHEGETEAEGKE 776

                           90
                   ....*....|.
gi 226053126  1495 DQ---EIQVEE 1502
Cdd:TIGR00927  777 DEdegEIQAGE 787

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                           10        20
                   ....*....|....*....|...
gi 226053126  1163 YECPKCGESFIHSSFLFEHQRIH 1185
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23

hypothetical protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226053126 1420 GEAEGPDGEAAEPIGEAGQPNGEAEQPNGDADEPDGAGIEDPEERAEEPEGK---AEEPEGD-ADEPDGVGIEDPEEGED 1495
Cdd:PHA03169  145 GPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSEtptSSPPPQSpPDEPGEPQSPTPQQAPS 224

                  ....
gi 226053126 1496 QEIQ 1499
Cdd:PHA03169  225 PNTQ 228